Drug Information

Drug (ID: DG00269) and It's Reported Resistant Information

• Name: Rilpivirine
• Synonyms: 500287-72-9; TMC278; Edurant; TMC 278; UNII-FI96A8X663; R278474; TMC-278; 4-{[4-({4-[(E)-2-Cyanoethenyl]-2,6-Dimethylphenyl}amino)pyrimidin-2-Yl]amino}benzonitrile; CHEBI:68606; FI96A8X663; R 278474; 4-{[4-({4-[(E)-2-cyanovinyl]-2,6-dimethylphenyl}amino)pyrimidin-2-yl]amino}benzonitrile; (E)-4-((4-((4-(2-cyanovinyl)-2,6-dimethylphenyl)amino)pyrimidin-2-yl)amino)benzonitrile; (E)-4-(4-(4-(2-cyanovinyl)-2,6-dimethylphenylamino)pyrimidin-2-ylamino)benzonitrile; W-202888; RPV; Mu O-conotoxin
• Indication:
  In total 2 Indication(s)
  Human immunodeficiency virus disease [ICD-11: 1C60-1C62]; Approved; [1]
  Pain [ICD-11: MG30]; Investigative; [1]
• Drug Resistance Disease(s):
  Disease(s) with Clinically Reported Resistance for This Drug (1 diseases)
  HIV infection [ICD-11: 1C62]; [2]
  Disease(s) with Resistance Information Validated by in-vivo Model for This Drug (1 diseases)
  HIV infection [ICD-11: 1C62]; [1]
• Target: Human immunodeficiency virus Reverse transcriptase (HIV RT); POL_HV1B1; [1]
• Target: Voltage-gated sodium channel alpha Nav1.8 (SCN10A); SCNAA_HUMAN; [1]
• Formula: C22H18N6
• IsoSMILES: CC1=CC(=CC(=C1NC2=NC(=NC=C2)NC3=CC=C(C=C3)C#N)C)/C=C/C#N
• InChI: 1S/C22H18N6/c1-15-12-18(4-3-10-23)13-16(2)21(15)27-20-9-11-25-22(28-20)26-19-7-5-17(14-24)6-8-19/h3-9,11-13H,1-2H3,(H2,25,26,27,28)/b4-3+
• InChIKey: YIBOMRUWOWDFLG-ONEGZZNKSA-N
• PubChem CID: 6451164
• ChEBI ID: CHEBI:68606
• TTD Drug ID: D0T6WN
• DrugBank ID: DB08864

Type(s) of Resistant Mechanism of This Drug

  ADTT: Aberration of the Drug's Therapeutic Target

Drug Resistance Data Categorized by Their Corresponding Diseases

ICD-01: Infectious/parasitic diseases

HIV infection [ICD-11: 1C62]

Drug Resistance Data Categorized by Their Corresponding Mechanisms

Aberration of the Drug's Therapeutic Target (ADTT)

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [1]

• Molecule Alteration: Missense mutation; p.K101E+p.K102Q+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Discovered Using In-vivo Testing Model
• In Vitro Model: HEK293T cells; Kidney; Homo sapiens (Human); CVCL_0063
• Experiment for Molecule Alteration: Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: The k101E substitution conferred large reductions in susceptibility to NVP and DLV, while more modest reductions in susceptibility to EFV, ETR, or RPV were observed. In contrast, the E138k substitution did not confer large reductions in susceptibility to any of the NNRTIs and only small reductions in susceptibility to ETR and RPV. That is because that the k101E substitution compensates for the impaired viral replication capacity of HIV-1 containing M184I.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [1]

• Molecule Alteration: Missense mutation; p.K102Q+p.E138K+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Discovered Using In-vivo Testing Model
• In Vitro Model: HEK293T cells; Kidney; Homo sapiens (Human); CVCL_0063
• Experiment for Molecule Alteration: Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: The k101E substitution conferred large reductions in susceptibility to NVP and DLV, while more modest reductions in susceptibility to EFV, ETR, or RPV were observed. In contrast, the E138k substitution did not confer large reductions in susceptibility to any of the NNRTIs and only small reductions in susceptibility to ETR and RPV. That is because that the k101E substitution compensates for the impaired viral replication capacity of HIV-1 containing M184I.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [1]

• Molecule Alteration: Missense mutation; p.K101E+p.K102Q+p.E138K+p.S162C+p.M184I+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Discovered Using In-vivo Testing Model
• In Vitro Model: HEK293T cells; Kidney; Homo sapiens (Human); CVCL_0063
• Experiment for Molecule Alteration: Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: The k101E substitution conferred large reductions in susceptibility to NVP and DLV, while more modest reductions in susceptibility to EFV, ETR, or RPV were observed. In contrast, the E138k substitution did not confer large reductions in susceptibility to any of the NNRTIs and only small reductions in susceptibility to ETR and RPV. That is because that the k101E substitution compensates for the impaired viral replication capacity of HIV-1 containing M184I.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [1]

• Molecule Alteration: Missense mutation; p.K102Q+p.E138K+p.S162C+p.M184I+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Discovered Using In-vivo Testing Model
• In Vitro Model: HEK293T cells; Kidney; Homo sapiens (Human); CVCL_0063
• Experiment for Molecule Alteration: Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: The k101E substitution conferred large reductions in susceptibility to NVP and DLV, while more modest reductions in susceptibility to EFV, ETR, or RPV were observed. In contrast, the E138k substitution did not confer large reductions in susceptibility to any of the NNRTIs and only small reductions in susceptibility to ETR and RPV. That is because that the k101E substitution compensates for the impaired viral replication capacity of HIV-1 containing M184I.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [1]

• Molecule Alteration: Missense mutation; p.K101E+p.K102Q+p.E138K+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Discovered Using In-vivo Testing Model
• In Vitro Model: HEK293T cells; Kidney; Homo sapiens (Human); CVCL_0063
• Experiment for Molecule Alteration: Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: The k101E substitution conferred large reductions in susceptibility to NVP and DLV, while more modest reductions in susceptibility to EFV, ETR, or RPV were observed. In contrast, the E138k substitution did not confer large reductions in susceptibility to any of the NNRTIs and only small reductions in susceptibility to ETR and RPV. That is because that the k101E substitution compensates for the impaired viral replication capacity of HIV-1 containing M184I.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.K20R+p.V35I+p.K101KE+p.V106VI+p.D123E+p.I135T+p.K173T+p.Q174K+p.D177E+p.Y181I+p.M184V+p.G196E+p.T200K+p.Q207A+p.P243T+p.V245K+p.D256E+p.A272P+p.E291D+p.V292I+p.I293V+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.S48T+p.V90VI+p.K101E+p.Y115YF+p.Y181YC+p.M184I+p.R211N+p.K219KE+p.V245N+p.L283I+p.V292I+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35E+p.T39A+p.E138K+p.D177E+p.V179VI+p.Y181I+p.M184V+p.E194EK+p.G196EK+p.Q207E+p.R211K+p.V245K+p.I257L+p.K277R+p.T286A+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35I+p.L74V+p.L100I+p.K103N+p.M184V+p.Q207A+p.R211K+p.P225H+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.K20KR+p.A62AV+p.K65KN+p.V108VI+p.F171Y+p.D177E+p.I178IMV+p.M184MIV+p.T200A+p.Q207T+p.R211K+p.F227FC+p.L228LR+p.M230MI+p.L234LI+p.V245E+p.A272P
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35IM+p.G45X+p.V90I+p.K101KE+p.K122E+p.D123N+p.I135L+p.S162C+p.Q174K+p.V179I+p.Y181I+p.M184V+p.G196E+p.A272P+p.A288T
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35I+p.V90I+p.K122E+p.D123N+p.I135L+p.S162C+p.Q174K+p.V179I+p.Y181I+p.M184V+p.G196E+p.A272P+p.A288T
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.K11T+p.V35I+p.E40K+p.K65R+p.T69T_X+p.I135L+p.D177E+p.I178M+p.V179VI+p.Y181C+p.Y188H+p.V189VI+p.G196E+p.K219KE+p.E291D+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V8I+p.K20R+p.A98AG+p.K101KE+p.K122KE+p.D123X+p.E138EK+p.I178IM+p.Y181YC+p.M184I+p.R211K+p.H221HY+p.V245I+p.E248ED+p.A272P+p.K277KR+p.I293V+p.P294S+p.E297R
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35I+p.D67G+p.A98S+p.K101E+p.K122E+p.D123G+p.Y181C+p.M184I+p.T200A+p.K219E+p.M230L+p.V245E+p.K277R+p.I293V+p.P294A+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.K20R+p.V35L+p.T39A+p.K122E+p.D123DN+p.I135R+p.K173E+p.Q174QR+p.D177E+p.V179I+p.Y181C+p.M184V+p.G196E+p.T200I+p.I202IV+p.R211K+p.K249KR+p.A288S+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.P4S+p.D67DN+p.T69N+p.K70KR+p.V90I+p.L100LI+p.K122E+p.D123N+p.I135IL+p.S162C+p.D177E+p.V179I+p.M184I+p.Y188L+p.T200A+p.R211K+p.K219E+p.M230MIL+p.L234LI+p.A272P+p.K277R+p.T286A+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.P4T+p.E6D+p.K20R+p.A33G+p.V60I+p.D67N+p.T69N+p.K70R+p.L74I+p.K101E+p.K103S+p.V118I+p.D123E+p.I135T+p.E138A+p.M184V+p.G190A+p.D192N+p.I195KR+p.G196E+p.E203K+p.R211A+p.F214L+p.K219Q+p.H221Y+p.I257L+p.A272P+p.K281R+p.E291D+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.V35M+p.T69D+p.K102Q+p.K103N+p.K122E+p.E138G+p.S162SC+p.I178L+p.Q207E+p.A272P+p.K277R+p.L283I+p.I293V+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.V35L+p.M41L+p.K43E+p.D67N+p.T69N+p.K70R+p.K102Q+p.K103N+p.K122E+p.D123E+p.D177N+p.M184V+p.Y188L+p.G196E+p.I202V+p.R211T+p.T215F+p.D218E+p.K219Q+p.A272P+p.K277R+p.L283I+p.A288T+p.I293V+p.E297K+p.A304E
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35T+p.M41L+p.K43KN+p.V60I+p.K122E+p.K173KQ+p.D177EG+p.V179VI+p.Y188L+p.G196E+p.R211RK+p.T215D+p.V245E+p.I257L+p.K277R+p.I293V+p.E297R
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.V60I+p.K103N+p.D123E+p.I142V+p.Y181C+p.G196E+p.T200A+p.R211K+p.K219E+p.I293IM
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35T+p.M41L+p.L80I+p.K122E+p.D177E+p.Y188L+p.H198E+p.T215D+p.V245VE+p.I257IL+p.K277R+p.A288AT+p.I293V+p.E297R
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.T39AE+p.M41L+p.K43KR+p.E44D+p.L74LI+p.A98AG+p.K102KR+p.K103N+p.K122E+p.D123S+p.I135T+p.I142V+p.M184V+p.Y188L+p.H208Y+p.L210W+p.R211K+p.T215Y+p.L228H+p.R284K+p.T286A+p.P294T
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.T69TN+p.K101P+p.K103N+p.I135V+p.I142V+p.Q145V+p.M184V+p.T200A+p.V245N+p.E248D+p.A272P+p.K275R+p.I293IV
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K22R+p.V35M+p.S162C+p.I178L+p.V179I+p.Y181C+p.M184V+p.Y188L+p.T200A+p.Q207E+p.V245E+p.A272P+p.K277R
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.S3C+p.E28R+p.K32E+p.V35M+p.M41L+p.L74I+p.R83K+p.A98G+p.K101E+p.K103N+p.V108I+p.S162A+p.I167IV+p.E169D+p.D177E+p.I178L+p.M184V+p.G196E+p.T200A+p.E203D+p.Q207E+p.L210W+p.R211K+p.T215Y+p.L228H+p.L260V+p.A272P+p.K281R+p.T286A+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.E28K+p.K32E+p.T39K+p.M41L+p.K43E+p.E44A+p.V60I+p.D67N+p.V75M+p.R83K+p.K102KR+p.K103S+p.V118I+p.K122E+p.I135T+p.V179T+p.Y181V+p.M184V+p.T200A+p.E203V+p.Q207E+p.H208Y+p.L210W+p.R211K+p.T215Y+p.D218E+p.K219E+p.L228H+p.Q242H+p.V245E+p.D256E+p.A272P+p.T286TI+p.A288T+p.I293V+p.E297T
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.I5IV+p.E6K+p.K20KR+p.E44ED+p.D67N+p.T69D+p.V90VI+p.K102Q+p.K103N+p.K104KR+p.V118I+p.K122E+p.I142IV+p.V179I+p.Y181C+p.Y188L+p.T200A+p.Q207N+p.R211K+p.F214L+p.H221Y+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35VI+p.T39TA+p.V90VI+p.L100I+p.Y115F+p.K122E+p.A158S+p.E169D+p.V179VI+p.M184V+p.Y188L+p.G196D+p.T200TA+p.Q207K+p.R211RK+p.T215F+p.K219E+p.L228H+p.V245E
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.M41L+p.K43Q+p.V60I+p.D67N+p.T69D+p.L74LV+p.V75VIM+p.L100I+p.K103N+p.K122KE+p.I135L+p.E138G+p.I142V+p.I178L+p.M184V+p.G196E+p.Q207E+p.T215Y+p.V245E+p.A272P+p.V276VI+p.K277KR+p.T286A+p.E291A+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.P4S+p.V35VA+p.S48E+p.K101KE+p.K103KN+p.E169A+p.K173E+p.I178IM+p.I180IL+p.T200TA+p.V245VI+p.A272P
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35L+p.D67N+p.K70R+p.K101R+p.K103R+p.D177E+p.I178M+p.G190E+p.G196E+p.T200A+p.E204N+p.R211K+p.T215F+p.K219E+p.L228H+p.V245E+p.A272P+p.T286A+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.D67N+p.K70R+p.L74IV+p.L100I+p.K103N+p.D123E+p.I135T+p.K166R+p.G196E+p.T200A+p.I202V+p.T215I+p.K219E+p.L228LR+p.K277R+p.L283I+p.A288T+p.I293V+p.P294I+p.E297P
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.D67G+p.S68G+p.K70R+p.K101Q+p.K122E+p.V179I+p.Y181I+p.I195T+p.Q207E+p.R211K+p.F214L+p.K219Q+p.H221Y+p.L228H+p.V245E+p.A272P+p.K277R+p.T286A+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.E6D+p.K103N+p.L109LS+p.D123E+p.I135T+p.S162A+p.M184IV+p.T200I+p.E204Q+p.Q207E+p.F214L+p.M230L+p.I244V+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K11KRT+p.V60VI+p.W88C+p.D121H+p.K122E+p.I135T+p.D177E+p.Y181C+p.R211K+p.H221Y+p.V245E+p.V254VI+p.A272P+p.A288G+p.E291D+p.I293IV+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.E6D+p.K122E+p.E138A+p.I142T+p.D177E+p.I178M+p.I195L+p.I202V+p.R211K+p.V245I+p.A272P+p.L283I+p.I293V+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.D67N+p.K70R+p.K122E+p.I135V+p.E138A+p.S162C+p.M184MV+p.G190E+p.T200A+p.F214M+p.T215F+p.K219Q+p.L228H+p.V245E
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.M16MV+p.T69TN+p.V90I+p.L100I+p.K103N+p.D123E+p.I135V+p.G196E+p.P243S+p.V245E+p.E248DV+p.I293V+p.E297R
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.L74LV+p.Y115F+p.K122E+p.Y181C+p.M184V+p.R211K+p.F214L+p.H221Y+p.V241VM+p.I293V+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K11K*+p.K20R+p.K64R+p.D67G+p.K70R+p.K101P+p.K103N+p.D123E+p.R172K+p.M184V+p.Q207E+p.R211K+p.F214L+p.K219E+p.T253TS
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.T39TA+p.D67N+p.K70R+p.V90I+p.K101E+p.S162N+p.M184V+p.G190A+p.E203D+p.R211K+p.F214FL+p.K219H+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V60I+p.K64Y+p.D67N+p.K70R+p.V90VI+p.K101P+p.T139M+p.M184V+p.G190A+p.K219Q+p.E224D+p.L228H+p.V245E
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.M41L+p.E44D+p.D67N+p.V118VI+p.I135T+p.S162C+p.R172K+p.Y188L+p.V189I+p.T200A+p.L210W+p.T215Y+p.D218E+p.K219R+p.V245E+p.A272P
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K70KR+p.K122E+p.A158S+p.E169D+p.M184V+p.Y188L+p.G196D+p.Q207K+p.T215F+p.V245E
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.V60I+p.T69N+p.K70R+p.I142V+p.V179D+p.Y188L+p.R211K+p.V245I+p.K277R+p.A288S+p.I293V+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.M16MV+p.M41L+p.L74V+p.L100I+p.K103N+p.K122E+p.I135T+p.T139TA+p.K173KR+p.I178L+p.R211K+p.T215Y+p.A272P+p.I293V+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.T7A+p.M41L+p.K43E+p.D67N+p.K101Q+p.V106I+p.D123E+p.I135L+p.Y181I+p.M184V+p.Q197L+p.L210W+p.R211K+p.T215Y+p.A272P+p.I293V+p.L303P
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V60I+p.D67G+p.S68G+p.K70KR+p.L74V+p.I135V+p.E138A+p.K173E+p.I178M+p.G190E+p.R211A+p.K219N+p.V245E+p.E248D+p.D250E+p.A272P+p.T286A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.M41L+p.L74V+p.I142V+p.T165L+p.E169D+p.Y181I+p.M184V+p.R211K+p.T215Y
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.M41L+p.E44D+p.D67N+p.T69D+p.K70KR+p.A98S+p.Y181I+p.L210W+p.R211K+p.T215Y+p.D218DE
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35K+p.M41L+p.V60I+p.D67N+p.T69D+p.K70R+p.L74V+p.K101E+p.K104N+p.V118I+p.K122E+p.I135T+p.S162D+p.Y181C+p.M184V+p.G190S+p.F214L+p.T215F+p.K219Q+p.A272P
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.K20KR+p.T165TI+p.T200AV+p.E204EG+p.F214FL+p.K277R+p.T286A+p.A288S
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K20KR, T165TI, T200AV, E204EG, F214FL, K277R, T286A, A288S.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [5]

• Molecule Alteration: Missense mutation; p.K122E+p.M184I+p.F214L+p.A272P+p.K277R+p.A376T+p.A400T
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K122E, M184I, F214L, A272P, K277R, A376T, A400T.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [5]

• Molecule Alteration: Missense mutation; p.K122E+p.F214L+p.A272P+p.K277R+p.A376T+p.A400T
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K122E, F214L, A272P, K277R, A376T, A400T.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.V35I+p.R83K+p.K103N+p.I135T+p.E138G+p.K166KR+p.T200TA+p.H208HY+p.R211K+p.I244V+p.D250E+p.A272P+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35I, R83K, K103N, I135T, E138G, K166KR, T200TA, H208HY, R211K, I244V, D250E, A272P, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.V35IM+p.T39TA+p.R83K+p.K102KQ+p.K103N+p.D123E+p.S162C+p.D177E+p.I178R+p.V179F+p.R211RK+p.V245EQ+p.D250E+p.K277R+p.T286A+p.I293V+p.M357AS+p.E370ED+p.T377TMI
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35IM, T39TA, R83K, K102KQ, K103N, D123E, S162C, D177E, I178R, V179F, R211RK, V245EQ, D250E, K277R, T286A, I293V, M357AS, E370ED, T377TMI.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.K20KR+p.K22R+p.V106I+p.I178L+p.R211K+p.F214FL+p.D250E+p.S251SN+p.K277R
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K20KR, K22R, V106I, I178L, R211K, F214FL, D250E, S251SN, K277R.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.K20KR+p.V35I+p.K101H+p.I135V+p.S162C+p.D177E+p.I178IV+p.G190A+p.T200E+p.E203ED+p.R211K+p.I244IV+p.V245M+p.A272P+p.T286A+p.I293V+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K20KR, V35I, K101H, I135V, S162C, D177E, I178IV, G190A, T200E, E203ED, R211K, I244IV, V245M, A272P, T286A, I293V, E297A.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.K20R+p.V35M+p.T69D+p.K102Q+p.K122KE+p.E138EAG+p.S162C+p.I178L+p.M184MV+p.Q207E+p.A272P+p.K277R+p.L283I+p.I293V+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K20R, V35M, T69D, K102Q, K122KE, E138EAG, S162C, I178L, M184MV, Q207E, A272P, K277R, L283I, I293V, E297A.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [5]

• Molecule Alteration: Missense mutation; p.K122E+p.E138K+p.M184V+p.F214L+p.A272P+p.K277R+p.A376T+p.A400T
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K122E, E138K, M184V, F214L, A272P, K277R, A376T, A400T.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.D67G+p.K70E+p.V90I+p.K122E+p.I135IT+p.S162F+p.I178IM+p.Y181C+p.T200E+p.R211HQ+p.V245E+p.A272P+p.K277R+p.T286A+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included D67G, K70E, V90I, K122E, I135IT, S162F, I178IM, Y181C, T200E, R211HQ, V245E, A272P, K277R, T286A, E297K.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.D67G+p.K70E+p.V90I+p.K102Q+p.I135T+p.S162F+p.I178IM+p.Y181C+p.T200E+p.R211QH+p.V245E+p.K277R+p.T286A+p.I293V+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included D67G, K70E, V90I, K102Q, I135T, S162F, I178IM, Y181C, T200E, R211QH, V245E, K277R, T286A, I293V, E297K.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [5]

• Molecule Alteration: Missense mutation; p.K122E+p.E138K+p.F214L+p.A272P+p.K277R+p.A376T+p.A400T
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K122E, E138K, F214L, A272P, K277R, A376T, A400T.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [5]

• Molecule Alteration: Missense mutation; p.K122E+p.E138K+p.M184I+p.F214L+p.A272P+p.K277R+p.A376T+p.A400T
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K122E, E138K, M184I, F214L, A272P, K277R, A376T, A400T.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.M41L+p.A62V+p.D67N+p.T69D+p.V75I+p.R83K+p.K103N+p.V108I+p.F116Y+p.D123E+p.Q151M+p.K166R+p.D177E+p.I202V+p.L210W+p.T215Y+p.M230L+p.A272P+p.I293V+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included M41L, A62V, D67N, T69D, V75I, R83K, K103N, V108I, F116Y, D123E, Q151M, K166R, D177E, I202V, L210W, T215Y, M230L, A272P, I293V, E297K.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.D123E+p.E138EK+p.S162C+p.I178L+p.Q207E+p.R211K+p.A272P+p.K277R+p.T286A+p.A288T+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included D123E, E138EK, S162C, I178L, Q207E, R211K, A272P, K277R, T286A, A288T, E297K.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.V35M+p.K70E+p.K102Q+p.K103N+p.D123E+p.S162C+p.K173E+p.Q174R+p.I178L+p.M184V+p.T200A+p.R211K+p.L228HR+p.M230L+p.L234I+p.V245KQ+p.K277R+p.L283I+p.V292I+p.I293V+p.Q334QR+p.G335X+p.T369TA+p.V381VI
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35M, K70E, K102Q, K103N, D123E, S162C, K173E, Q174R, I178L, M184V, T200A, R211K, L228HR, M230L, L234I, V245KQ, K277R, L283I, V292I, I293V, Q334QR, G335X, T369TA, V381VI.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [6]

• Molecule Alteration: Missense mutation; p.M41L+p.A98G+p.K101E+p.K122E+p.I135T+p.E138K+p.S162Y+p.Y181C+p.T200A+p.L210F+p.T215D+p.P243T+p.V245E+p.D250E+p.A272P+p.I274V+p.Q278H+p.K281R+p.T286A+p.A288S+p.K311R
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included M41L, A98G, K101E, K122E, I135T, E138K, S162Y, Y181C, T200A, L210F, T215D, P243T, V245E, D250E, A272P, I274V, Q278H, K281R, T286A, A288S, K311R.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [6]

• Molecule Alteration: Missense mutation; p.M41L+p.A98S+p.K101P+p.K102Q+p.K103N+p.D123E+p.K166R+p.D177E+p.D192N+p.R211K+p.T215Y+p.V245K+p.K277R+p.R284K+p.T286A+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included M41L, A98S, K101P, K102Q, K103N, D123E, K166R, D177E, D192N, R211K, T215Y, V245K, K277R, R284K, T286A, E297K.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.K20R+p.K64KR+p.L74V+p.K103N+p.V108I+p.Y181C+p.M184V+p.T200A+p.R211K+p.H221Y+p.L228H+p.V245L+p.A272P+p.K277R+p.T286A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K20R, K64KR, L74V, K103N, V108I, Y181C, M184V, T200A, R211K, H221Y, L228H, V245L, A272P, K277R, T286A.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [6]

• Molecule Alteration: Missense mutation; p.M41L+p.K122E+p.E138G+p.D177E+p.I178L+p.L210W+p.R211K+p.T215Y+p.H221Y+p.F227L+p.M230L+p.V245M+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included M41L, K122E, E138G, D177E, I178L, L210W, R211K, T215Y, H221Y, F227L, M230L, V245M, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.K20R+p.K32KQ+p.M41L+p.E53ED+p.P59PS+p.L74V+p.I135T+p.Q145QR+p.Y181V+p.R211K+p.T215Y+p.K249R
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K20R, K32KQ, M41L, E53ED, P59PS, L74V, I135T, Q145QR, Y181V, R211K, T215Y, K249R.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.K20R+p.V35L+p.T39A+p.K101P+p.K103KR+p.K122E+p.I135R+p.D177E+p.I178M+p.T200TA+p.R211K+p.A272P+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K20R, V35L, T39A, K101P, K103KR, K122E, I135R, D177E, I178M, T200TA, R211K, A272P, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [6]

• Molecule Alteration: Missense mutation; p.V35I+p.M41L+p.D67G+p.L74I+p.L100I+p.K103R+p.K122E+p.V179D+p.M184V+p.I202V+p.R211K+p.T215Y+p.M230L+p.T240K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35I, M41L, D67G, L74I, L100I, K103R, K122E, V179D, M184V, I202V, R211K, T215Y, M230L, T240K.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.K20R+p.V35I+p.K65KR+p.L74LV+p.K103N+p.K122E+p.Y181C+p.T200A+p.R211K+p.F227C+p.M230L+p.V245Q+p.I293V+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K20R, V35I, K65KR, L74LV, K103N, K122E, Y181C, T200A, R211K, F227C, M230L, V245Q, I293V, E297A.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.M41L+p.K43Q+p.A62AV+p.T69S_ST+p.K101P+p.K103N+p.V118I+p.K122E+p.S162D+p.K166R+p.D177N+p.V179I+p.M184V+p.T200A+p.Q207E+p.L210F+p.R211K+p.T215Y+p.V245E+p.A272P+p.K277R+p.E291D+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included M41L, K43Q, A62AV, T69S_ST, K101P, K103N, V118I, K122E, S162D, K166R, D177N, V179I, M184V, T200A, Q207E, L210F, R211K, T215Y, V245E, A272P, K277R, E291D, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.T39TP+p.D67N+p.K70R+p.V90I+p.K101P+p.K102R+p.K103N+p.K122E+p.I135V+p.Q151M+p.G196E+p.Q207K+p.R211A+p.K219Q+p.L228LH+p.E248D+p.I293V+p.E297A
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included T39TP, D67N, K70R, V90I, K101P, K102R, K103N, K122E, I135V, Q151M, G196E, Q207K, R211A, K219Q, L228LH, E248D, I293V, E297A.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [7]

• Molecule Alteration: Missense mutation; p.V60VI+p.D67G+p.S68G+p.T69N+p.K70R+p.K101P+p.K102Q+p.K103S+p.I142IV+p.D177E+p.I178L+p.M184V+p.T200A+p.T215V+p.K219E+p.I293V+p.E297K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V60VI, D67G, S68G, T69N, K70R, K101P, K102Q, K103S, I142IV, D177E, I178L, M184V, T200A, T215V, K219E, I293V, E297K.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [8]

• Molecule Alteration: Missense mutation; p.L100I+p.K102Q+p.K103R+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included L100I, K102Q, K103R, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [8]

• Molecule Alteration: Missense mutation; p.K102Q+p.K103R+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, K103R, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [9]

• Molecule Alteration: Missense mutation; p.M41L+p.K43N+p.D67G+p.T69N+p.K70R+p.L74I+p.K103N+p.I142V+p.Y181C+p.M184V+p.G196E+p.I202V+p.T215F+p.K219Q+p.V245K+p.K277R+p.A288S+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included M41L, K43N, D67G, T69N, K70R, L74I, K103N, I142V, Y181C, M184V, G196E, I202V, T215F, K219Q, V245K, K277R, A288S, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [8]

• Molecule Alteration: Missense mutation; p.K102Q+p.K103S+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, K103S, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [9]

• Molecule Alteration: Missense mutation; p.V35R+p.M41L+p.K49R+p.V60I+p.K64H+p.D67N+p.T69N+p.K70R+p.V108I+p.K122Q+p.I135T+p.S162D+p.D177E+p.Y181C+p.M184V+p.V189I+p.T200A+p.T215F+p.D218E+p.K219Q+p.L228R+p.V245E
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35R, M41L, K49R, V60I, K64H, D67N, T69N, K70R, V108I, K122Q, I135T, S162D, D177E, Y181C, M184V, V189I, T200A, T215F, D218E, K219Q, L228R, V245E.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [9]

• Molecule Alteration: Missense mutation; p.D67N+p.T69N+p.K70R+p.V90I+p.K103N+p.V118I+p.I135M
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included D67N, T69N, K70R, V90I, K103N, V118I, I135M.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K102Q+p.E138A+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, E138A, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K102Q+p.S162C+p.Y181C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, S162C, Y181C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K102Q+p.E138G+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, E138G, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [9]

• Molecule Alteration: Missense mutation; p.K64H+p.D67N+p.T69N+p.K70R+p.V90I+p.K103N+p.V118I+p.I135M+p.T215E+p.K219Q+p.A272P
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K64H, D67N, T69N, K70R, V90I, K103N, V118I, I135M, T215E, K219Q, A272P.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K101Q+p.K102Q+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K101Q, K102Q, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K102Q+p.E138R+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, E138R, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K101E+p.K102Q+p.S162C+p.M184V+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K101E, K102Q, S162C, M184V, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [9]

• Molecule Alteration: Missense mutation; p.V35T+p.K43R+p.K64Y+p.D67N+p.K70R+p.L74I+p.K103S+p.V106A+p.D123E+p.D177E+p.M184V+p.G196E+p.T200A+p.R211S+p.T215F+p.K219Q+p.L228H+p.Q242H+p.K277R+p.R284K
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35T, K43R, K64Y, D67N, K70R, L74I, K103S, V106A, D123E, D177E, M184V, G196E, T200A, R211S, T215F, K219Q, L228H, Q242H, K277R, R284K.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K101E+p.K102Q+p.S162C+p.M184I+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K101E, K102Q, S162C, M184I, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K101E+p.K102Q+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K101E, K102Q, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [9]

• Molecule Alteration: Missense mutation; p.V35R+p.M41L+p.K49R+p.V60I+p.D67N+p.T69N+p.K70R+p.V108I+p.K122Q+p.I135T+p.S162D+p.D177E+p.Y181C+p.M184V+p.V189I+p.T200A+p.T215F+p.D218E+p.K219Q+p.L228R+p.V245E+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35R, M41L, K49R, V60I, D67N, T69N, K70R, V108I, K122Q, I135T, S162D, D177E, Y181C, M184V, V189I, T200A, T215F, D218E, K219Q, L228R, V245E, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [8]

• Molecule Alteration: Missense mutation; p.K102Q+p.K103R+p.S162C+p.V179D+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, K103R, S162C, V179D, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K102Q+p.E138Q+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, E138Q, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [11]

• Molecule Alteration: Missense mutation; p.Y188L
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included Y188L.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [8]

• Molecule Alteration: Missense mutation; p.L100I+p.K102Q+p.K103R+p.S162C+p.V179D+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included L100I, K102Q, K103R, S162C, V179D, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K102Q+p.S162C+p.Y181I+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, S162C, Y181I, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K101P+p.K102Q+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K101P, K102Q, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [8]

• Molecule Alteration: Missense mutation; p.L100I+p.K102Q+p.K103N+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included L100I, K102Q, K103N, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [8]

• Molecule Alteration: Missense mutation; p.L100I+p.K102Q+p.K103S+p.S162C+p.K277R+p.I293V
• Resistant Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included L100I, K102Q, K103S, S162C, K277R, I293V.

Drug Sensitivity Data Categorized by Their Corresponding Mechanisms

Aberration of the Drug's Therapeutic Target (ADTT)

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V8VI+p.K20KR+p.V35I+p.D123E+p.I135T+p.K173T+p.Q174K+p.D177E+p.V179VD+p.G196E+p.T200K+p.Q207A+p.P243T+p.V245K+p.D256E+p.A272AP+p.T286TA+p.E291D+p.V292I+p.I293V+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.T39S+p.S48T+p.V60I+p.S68G+p.K102Q+p.K122KE+p.D123X+p.A158S+p.I178L+p.V179DE+p.I195IL+p.T200TA+p.R211K+p.I244V+p.V245E+p.A272P+p.K277KR+p.R284K+p.A288S+p.V292I+p.I293V+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.S48T+p.R211N+p.V245N+p.L283I+p.V292I+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35E+p.T39A+p.D177E+p.G196E+p.Q207E+p.R211K+p.V245K+p.I257L+p.K277R+p.T286A+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35T+p.E40ED+p.V60I+p.K122KE+p.I135V+p.S162A+p.K173T+p.Q174EK+p.P176PS+p.D177E+p.I178M+p.T200A+p.E204EK+p.Q207E+p.R211K+p.V245Q+p.A272P+p.K277R+p.K281R+p.T286A+p.I293V+p.P294T
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35M+p.K49KR+p.V60I+p.R83K+p.K122E+p.I135T+p.S162H+p.E248D+p.A272P+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.K11KR+p.V35I+p.R83K+p.T200TA+p.Q207A+p.R211K+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.A98S+p.K122E+p.A158AS+p.I159IV+p.S162SA+p.D177E+p.G196E+p.R211S+p.A272S+p.T286A+p.P294T
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.F171Y+p.D177E+p.I178IMV+p.T200A+p.Q207T+p.R211K+p.V245E+p.A272P+p.K277KR
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35I+p.K122E+p.D123N+p.I135L+p.S162C+p.K173N+p.Q174K+p.V179I+p.G196E+p.A272P+p.A288T
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.E6ED+p.V8VI+p.V35I+p.D86DE+p.K122P+p.D123E+p.I135L+p.T139I+p.D177E+p.Q207QK+p.R211RK+p.A272P+p.T286A+p.A288AG+p.I293IV
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35I+p.R83K+p.D177E+p.G196E+p.H208HY+p.L210LF+p.R211K+p.E291D+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.K20KR+p.V60I+p.S68G+p.I178ILM+p.G196E+p.T200TA+p.E248D+p.A272P+p.G273R+p.K275R+p.K281KR+p.V292I+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V8I+p.K20R+p.T69TA+p.K122KE+p.D123X+p.I178IM+p.R211K+p.V245VI+p.E248ED+p.A272P+p.K277R+p.I293V+p.P294S+p.E297R
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.T39TA+p.T69TA+p.K82KR+p.R83RK+p.S162SN+p.P170PL+p.K173Q+p.I178M+p.T200A+p.Q207E+p.R211K+p.P225PL+p.L228LF+p.A272P+p.K277KR+p.L282LF+p.I293V+p.T296S+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.V35I+p.L80LF+p.A98S+p.K122E+p.T128TA+p.K166KR+p.I178IL+p.R211K+p.V245E+p.K277R+p.I293V+p.P294A+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [3]

• Molecule Alteration: Missense mutation; p.K20R+p.V35L+p.T39A+p.R83RK+p.K122E+p.I135R+p.K173E+p.D177E+p.V179I+p.G196E+p.T200I+p.I202V+p.R211K+p.V245VE+p.A288S+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: GeneSeq assay; PhenoSense GT assay
• Experiment for Drug Resistance: Viral load assay
• Mechanism Description: Amino acid changes in IN may contribute to drug resistance or sensitivity.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.E6D+p.V106I+p.V118I+p.I135V+p.T165I+p.T200A+p.F214L+p.V245R+p.D250E+p.A272P
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.M41L+p.K43Q+p.E44D+p.V60I+p.D67N+p.G93GR+p.K101H+p.V118I+p.K122P+p.D123E+p.I135T+p.I142V+p.D177E+p.I178IM+p.M184V+p.G190A+p.G196E+p.E203K+p.Q207E+p.L210W+p.R211K+p.T215Y+p.A272P+p.K277R
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35I+p.R83K+p.S162A+p.I178IM+p.Q207E+p.I293V+p.E297A+p.L301M
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K64KR+p.K102KR+p.D123E+p.K173X+p.P176PAT+p.D177DE+p.I178L+p.M184MV+p.Q197QEK+p.Q207E+p.R211K+p.V245VI+p.E248D+p.A272P+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35I+p.S48T+p.K101KR+p.K103N+p.V106VI+p.T139TA+p.P157PS+p.T200I+p.E203D+p.Q207E+p.R211RK+p.D250E+p.A272P+p.K275R+p.K277R+p.T286TA+p.I293IV
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.P4T+p.E6K+p.K20R+p.T39TK+p.M41L+p.K43E+p.E44AD+p.D67N+p.L74I+p.K101E+p.V118I+p.K122E+p.S162A+p.V179F+p.Y181C+p.M184V+p.G190A+p.I195K+p.L210W+p.R211K+p.T215Y+p.K219N+p.V245K+p.I293V+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.K122E+p.R211K+p.V245M+p.G262GE+p.A272P+p.V292VI+p.I293IV+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.P4S+p.E6D+p.K122E+p.D123N+p.I142V+p.S162C+p.D177E+p.I178L+p.R211K+p.A272P+p.I293V+p.E297R
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.E6K+p.V35I+p.T39TI+p.K102KQ+p.V106VI+p.K122E+p.I135IMV+p.I142M+p.S162C+p.R211K+p.K277R+p.A288S+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.I50IV+p.R83K+p.K166KR+p.K173X+p.Q174K+p.D177DE+p.I178L+p.V189VI+p.Q197QK+p.H198GE+p.Q207E+p.R211K+p.V245EQ+p.D250E+p.A272P+p.K277R
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.E6D+p.M41L+p.E44D+p.K49R+p.V60I+p.D67N+p.K70R+p.K103N+p.V108VI+p.D123E+p.I135T+p.M184V+p.T200I+p.I202V+p.T215V+p.K219E+p.P225PH+p.L228H+p.V245T+p.E248K+p.K249KR+p.I293V+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35T+p.T39TR+p.K122KE+p.D177E+p.K281R+p.T286A+p.I293IV+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.R83K+p.K101KE+p.K122E+p.D123DE+p.S162A+p.Q174G+p.G196E+p.T200A+p.Q207E+p.V245E+p.A272P+p.K277R+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V90I+p.D123E+p.I202V+p.E204Q+p.Q207D+p.R211K+p.V245T+p.I293V+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35T+p.T39E+p.K46T+p.E53D+p.V60I+p.K64KR+p.K101Q+p.K104KR+p.K122E+p.D123S+p.I135K+p.K166R+p.K173A+p.D177E+p.T200A+p.Q207E+p.R211K+p.V245E+p.D250E+p.V254I+p.A272P+p.K277R+p.T286A+p.E291D+p.V292I+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.I135V+p.P176S+p.D177E+p.A272P+p.G285A+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K13KR+p.K122E+p.I135T+p.S162C+p.M184V+p.G196E+p.K277R+p.I293V+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.V35M+p.T69D+p.K102Q+p.K122KE+p.E138EAG+p.S162C+p.I178L+p.M184MV+p.Q207E+p.A272P+p.K277R+p.L283I+p.I293V+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.V60I+p.V90I+p.K101Q+p.K103N+p.V108I+p.I135V+p.I142V+p.D177E+p.M184I+p.T200I+p.R211K+p.T215D+p.A272P+p.V276I+p.L283I+p.I293V+p.E302EG
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.P4S+p.K122KE+p.D123E+p.E169D+p.I178L+p.T200A+p.I202IV+p.R211K+p.L246LP+p.E248D+p.A272P+p.T286TA+p.V292VI+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35VIL+p.K103N+p.K122E+p.K173Q+p.I178M+p.M184MV+p.T200TA+p.V245M+p.E248D+p.D250DE+p.T286A+p.A288S
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.P4PH+p.K20R+p.T39A+p.L74LI+p.R83K+p.V106VI+p.V179VI+p.M184V+p.E224D+p.V245E+p.T286A+p.P294PS+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V60I+p.I135V+p.D177E+p.R211K+p.I244V+p.V245I+p.D250E+p.A272P+p.K277KR+p.E297V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35I+p.R83RK+p.T165TI+p.F171Y+p.T200A+p.I202V+p.V245M+p.A272P+p.K277R+p.T286A+p.P294Q+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.I135V+p.Y181C+p.M184V+p.G196E+p.T200A+p.Q207E+p.R211K+p.T215Y+p.V245K+p.K277R+p.E291D+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20KR+p.T27TS+p.V60I+p.R83K+p.K122KE+p.Q174L+p.I178IL+p.T200X+p.R211RK+p.V245E+p.L283LI+p.T286TA+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K122E+p.D123N+p.L210F+p.R211K+p.E248D+p.A272P+p.Q278H+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.I135T+p.T165TI+p.E169D+p.D177E+p.V179L+p.I202V+p.A272P+p.T296S+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.V35I+p.K122KE+p.I135T+p.E138K+p.R172K+p.T200V+p.R211RK+p.F214L+p.T286A+p.V292I+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V60A+p.D67G+p.K103R+p.V118I+p.D123N+p.E138K+p.T165I+p.M184V+p.I202V+p.F214L+p.D250V+p.A272P+p.V276T+p.K277R+p.T286A+p.P294A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.V35L+p.A62AV+p.S68SG+p.K70KN+p.V75T+p.R83K+p.S162N+p.T165I+p.F214L+p.H221Y+p.V245Q+p.E248N+p.D250E+p.G262GR+p.A272P+p.Q278H+p.K281R+p.T286A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.D67N+p.K70R+p.I135T+p.S162C+p.Q174QE+p.Y181C+p.M184V+p.Q207KR+p.R211Q+p.K219Q+p.H221Y+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.Y181C+p.T200TA+p.F214L+p.H221Y+p.E291D+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.R83K+p.K122E+p.D123G+p.E138A+p.K166R+p.T200E+p.R211K+p.V245E+p.A272P+p.V276I+p.K277R+p.L283I+p.I293V+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.E28K+p.S68G+p.A98S+p.K101E+p.D123E+p.I135V+p.I142IT+p.R143RG+p.M184V+p.L210LW+p.R211K+p.T215Y+p.T286TA+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.E28K+p.V35M+p.M41L+p.T69N+p.K70R+p.R83K+p.K101E+p.K122P+p.S162C+p.D177E+p.M184V+p.I195L+p.V276T+p.K277R+p.E297EK
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35M+p.T39S+p.R83K+p.K122KE+p.D123E+p.E138A+p.I178IL+p.I202V+p.R211K+p.T286P+p.I293V+p.I329L+p.Q334E+p.M357T+p.A376T+p.E449D+p.D460N+p.S468P+p.H483N+p.L491P+p.Q524E+p.V559VI
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K20R+p.K101E+p.K122E+p.M184V+p.G190A+p.D250E+p.A272P+p.P294Q+p.E302D
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.K11KT+p.M41L+p.K43N+p.E44D+p.V75M+p.K101E+p.V118I+p.D123E+p.D177E+p.Y181C+p.E203D+p.Q207E+p.H208Y+p.L210W+p.R211K+p.T215Y+p.K219N+p.L228LR+p.A272P+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.I31V+p.D67N+p.T69N+p.D123E+p.E138K+p.D177E+p.M184V+p.G196E+p.K219Q+p.D237E+p.K277R+p.T286TA+p.I293V+p.E297A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.M41L+p.K101H+p.I135T+p.M184V+p.G190A+p.L210W+p.R211K+p.T215Y+p.E248V+p.A272P+p.K277R+p.Q278QL
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.M41L+p.V60I+p.D67N+p.K101E+p.I135T+p.E138A+p.M184V+p.R211K+p.T215F+p.D218E+p.K219Q+p.K277KR+p.T286A+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.S3SR+p.V35I+p.M41L+p.K43E+p.V60I+p.D67N+p.V75M+p.K101E+p.V118I+p.D121Y+p.K122E+p.Q174K+p.D177E+p.I178M+p.G190S+p.T200A+p.Q207A+p.L210W+p.R211K+p.T215Y+p.A272P+p.T286A+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.E40F+p.M41L+p.K43E+p.D67N+p.L74I+p.K101H+p.V118I+p.K122E+p.S162C+p.E169D+p.H208Y+p.L210W+p.R211K+p.T215Y+p.K219N+p.V245M+p.Q278QH+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [2]

• Molecule Alteration: Missense mutation; p.V35T+p.T39A+p.M41L+p.E44ED+p.V60I+p.D67N+p.T69D+p.V75M+p.F77L+p.V118I+p.K122E+p.I135T+p.E138K+p.S162X+p.M184V+p.H208HY+p.L210W+p.R211RK+p.T215Y+p.A272P+p.K277R+p.T286A
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Site-directed mutagenesis; Sanger sequencing assay
• Experiment for Drug Resistance: PhenoSense assay
• Mechanism Description: Sixteen mutations at eight positions had a mean regression coefficient >=1.0 log10 (a contribution to decreased susceptibility of 10-fold or greater) for nevirapine, efavirenz, etravirine and/or rilpivirine: L100I, k101P, k103N/S, V106A/M, Y181C/I/V, Y188C/L, G190A/E/Q/S and F227C. With the exception of L100I and F227C, each mutation had a mean regression coefficient >=1.0 log10 for nevirapine. With the exception of k103S, V106A, Y181C/I/V and F227C, each had a mean regression coefficient >=1.0 log10 for efavirenz. Five mutations, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >=1.0 log10 for etravirine. Six mutations, L100I, k101P, Y181I/V, G190E and F227C, had a mean regression coefficient >= 1.0 log10 for rilpivirine.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.V35L+p.M41L+p.K43AT+p.S68G+p.L74LI+p.K103S+p.V118I+p.K122E+p.D177G+p.V179I+p.M184V+p.G190A+p.L210W+p.T215Y+p.K219KN+p.K223KQ+p.V245E+p.A272P+p.R284RK
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35L, M41L, K43AT, S68G, L74LI, K103S, V118I, K122E, D177G, V179I, M184V, G190A, L210W, T215Y, K219KN, K223KQ, V245E, A272P, R284RK.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.V35IM+p.T39TA+p.R83K+p.K102KQ+p.K103N+p.D123E+p.S162C+p.D177E+p.I178R+p.V179F+p.R211RK+p.V245EQ+p.D250E+p.K277R+p.T286A+p.I293V+p.M357AS+p.E370ED+p.T377TMI
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35IM, T39TA, R83K, K102KQ, K103N, D123E, S162C, D177E, I178R, V179F, R211RK, V245EQ, D250E, K277R, T286A, I293V, M357AS, E370ED, T377TMI.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.I135V+p.Y181C+p.M184V+p.G196E+p.T200A+p.Q207E+p.R211K+p.T215Y+p.V245K+p.K277R+p.E291D+p.E297K
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included I135V, Y181C, M184V, G196E, T200A, Q207E, R211K, T215Y, V245K, K277R, E291D, E297K.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.N57ND+p.V60I+p.D67DN+p.K70GR+p.V118VI+p.K166KR+p.M184V+p.E203EK+p.R211RK+p.F214L+p.K219Q+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included N57ND, V60I, D67DN, K70GR, V118VI, K166KR, M184V, E203EK, R211RK, F214L, K219Q, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.A62AV+p.K65R+p.K102R+p.K103N+p.A158T+p.M184V+p.T200E+p.R211K+p.L234I+p.A272S+p.I293V+p.P294S
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included A62AV, K65R, K102R, K103N, A158T, M184V, T200E, R211K, L234I, A272S, I293V, P294S.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.T39TA+p.K70E+p.K102Q+p.D123E+p.I142IM+p.S162C+p.M184V+p.R211K+p.K277R+p.T286A+p.V292I+p.I293V+p.E297K+p.A304E+p.S322SA
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included T39TA, K70E, K102Q, D123E, I142IM, S162C, M184V, R211K, K277R, T286A, V292I, I293V, E297K, A304E, S322SA.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.V35L+p.T39A+p.R83K+p.A98APS+p.D123E+p.Q174HN+p.G196E+p.T200I+p.R211RK+p.V245VM+p.D250E+p.A272P+p.K277R+p.T286A+p.P294PS+p.E297R
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35L, T39A, R83K, A98APS, D123E, Q174HN, G196E, T200I, R211RK, V245VM, D250E, A272P, K277R, T286A, P294PS, E297R.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.P4S+p.V35T+p.V60I+p.D67N+p.K70G+p.K102Q+p.V118I+p.D123E+p.E138A+p.S162C+p.K173KR+p.Q174K+p.M184V+p.G196E+p.Q207E+p.K219Q+p.D237E+p.V245M+p.S251N+p.K277R+p.I293IV+p.E297A+p.R358KT+p.D364DE
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included P4S, V35T, V60I, D67N, K70G, K102Q, V118I, D123E, E138A, S162C, K173KR, Q174K, M184V, G196E, Q207E, K219Q, D237E, V245M, S251N, K277R, I293IV, E297A, R358KT, D364DE.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.R211K+p.F214FL
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included R211K, F214FL.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.R83K+p.I135T+p.S162Y+p.I178L+p.D192DN+p.T200TA+p.R211RG+p.F214L+p.I244V+p.V245E+p.A272P+p.K277R+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included R83K, I135T, S162Y, I178L, D192DN, T200TA, R211RG, F214L, I244V, V245E, A272P, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.D67G+p.K70E+p.K102Q+p.K103KR+p.V106M+p.Y115F+p.D123E+p.I142V+p.S162C+p.E169D+p.K173Q+p.I178L+p.V179D+p.M184V+p.T200A+p.K277R+p.T286A+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included D67G, K70E, K102Q, K103KR, V106M, Y115F, D123E, I142V, S162C, E169D, K173Q, I178L, V179D, M184V, T200A, K277R, T286A, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [4]

• Molecule Alteration: Missense mutation; p.V35VI+p.R83K+p.K102Q+p.V106M+p.K122E+p.I135V+p.S162C+p.T165TI+p.Q174R+p.D177E+p.V179D+p.G196E+p.I202V+p.R211Q+p.F214L+p.A272P+p.K277R+p.L283LI+p.I293V+p.M357ML+p.I375IV
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35VI, R83K, K102Q, V106M, K122E, I135V, S162C, T165TI, Q174R, D177E, V179D, G196E, I202V, R211Q, F214L, A272P, K277R, L283LI, I293V, M357ML, I375IV.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [5]

• Molecule Alteration: Missense mutation; p.K122E+p.M184V+p.F214L+p.A272P+p.K277R+p.A376T+p.A400T
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K122E, M184V, F214L, A272P, K277R, A376T, A400T.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [9]

• Molecule Alteration: Missense mutation; p.T39A+p.K64N+p.D67N+p.T69N+p.K70R+p.K103R+p.I135L+p.F214L+p.K219Q+p.A272P
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included T39A, K64N, D67N, T69N, K70R, K103R, I135L, F214L, K219Q, A272P.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [9]

• Molecule Alteration: Missense mutation; p.M41L+p.D67N+p.T69D+p.V75T+p.V118I+p.K122E+p.D123E+p.Q207E+p.L210W+p.T215Y+p.V245A+p.Q278H+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included M41L, D67N, T69D, V75T, V118I, K122E, D123E, Q207E, L210W, T215Y, V245A, Q278H, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K102Q+p.S162C+p.M184V+p.K277R+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, S162C, M184V, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [9]

• Molecule Alteration: Missense mutation; p.T39A+p.D67N+p.T69N+p.K70R+p.K103R+p.I135L+p.F214L+p.K219Q+p.A272P
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included T39A, D67N, T69N, K70R, K103R, I135L, F214L, K219Q, A272P.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [9]

• Molecule Alteration: Missense mutation; p.V35T+p.D67N+p.K70R+p.K103N+p.V106A+p.D123E+p.D177E+p.M184V+p.G196E+p.T200A+p.R211N+p.T215F+p.K219Q+p.K277R+p.K281X
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included V35T, D67N, K70R, K103N, V106A, D123E, D177E, M184V, G196E, T200A, R211N, T215F, K219Q, K277R, K281X.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [8]

• Molecule Alteration: Missense mutation; p.L100I+p.K102Q+p.S162C+p.K277R+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included L100I, K102Q, S162C, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K102Q+p.S162C+p.H221Y+p.K277R+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, S162C, H221Y, K277R, I293V.

Key Molecule: HIV1 Reverse transcriptase (HIV1 RT) [10]

• Molecule Alteration: Missense mutation; p.K102Q+p.K103N+p.S162C+p.K277R+p.I293V
• Sensitive Disease: Human immunodeficiency virus infection [ICD-11: 1C62.0]
• Experimental Note: Identified from the Human Clinical Data
• Experiment for Molecule Alteration: Sanger sequencing assay; GeneSeq assay; Population sequencing of the integrase region assay; DNA sequencing assay; Site-directed mutagenesis
• Experiment for Drug Resistance: PhenoSense assay; Viral load assay; A single-cycle assay; TZM-bl cell line-based phenotypic assay; SDMs and phenotyping assay
• Mechanism Description: Some mutations identified were assiacted with resistance in the HIV isolates, those mutations included K102Q, K103N, S162C, K277R, I293V.

References

• Ref 1: Role of the K101E substitution in HIV-1 reverse transcriptase in resistance to rilpivirine and other nonnucleoside reverse transcriptase inhibitors. Antimicrob Agents Chemother. 2013 Nov;57(11):5649-57. doi: 10.1128/AAC.01536-13. Epub 2013 Sep 3.
• Ref 2: Non-nucleoside reverse transcriptase inhibitor (NNRTI) cross-resistance: implications for preclinical evaluation of novel NNRTIs and clinical genotypic resistance testing. J Antimicrob Chemother. 2014 Jan;69(1):12-20. doi: 10.1093/jac/dkt316. Epub 2013 Aug 9.
• Ref 3: Characterization of HIV-1 drug resistance development through week 48 in antiretroviral naive subjects on rilpivirine/emtricitabine/tenofovir DF or efavirenz/emtricitabine/tenofovir DF in the STaR study (GS-US-264-0110). J Acquir Immune Defic Syndr. 2014 Mar 1;65(3):318-26. doi: 10.1097/QAI.0000000000000017.
• Ref 4: Standardized comparison of the relative impacts of HIV-1 reverse transcriptase (RT) mutations on nucleoside RT inhibitor susceptibilityAntimicrob Agents Chemother. 2012 May;56(5):2305-13. doi: 10.1128/AAC.05487-11. Epub 2012 Feb 13.
• Ref 5: The HIV-1 reverse transcriptase M184I mutation enhances the E138K-associated resistance to rilpivirine and decreases viral fitnessJ Acquir Immune Defic Syndr. 2012 Jan 1;59(1):47-54. doi: 10.1097/QAI.0b013e31823aca74.
• Ref 6: Panel of prototypical recombinant infectious molecular clones resistant to nevirapine, efavirenz, etravirine, and rilpivirineAntimicrob Agents Chemother. 2012 Aug;56(8):4522-4. doi: 10.1128/AAC.00648-12. Epub 2012 Jun 4.
• Ref 7: Genotypic predictors of human immunodeficiency virus type 1 drug resistanceProc Natl Acad Sci U S A. 2006 Nov 14;103(46):17355-60. doi: 10.1073/pnas.0607274103. Epub 2006 Oct 25.
• Ref 8: Combinations of HIV-1 reverse transcriptase mutations L100I+K103N/S and L100I+K103R+V179D reduce susceptibility to rilpivirine.
• Ref 9: Phenotypic evidence for NRTI resistance in HIV-1 isolates with the RT mutation K64H.
• Ref 10: Comparison of the Antivirogram and PhenoSense assays to determine phenotypic susceptibility to rilpivirine in patient samples from the Phase III ECHO and THRIVE trials.
• Ref 11: Mutation Y188L of HIV-1 reverse transcriptase is strongly associated with reduced susceptibility to rilpivirine