Disease Information
General Information of the Disease (ID: DIS00136)
Name |
Bacterial genitourinary infection
|
---|---|
ICD |
ICD-11: GA0Z-GC8Z
|
Resistance Map |
Type(s) of Resistant Mechanism of This Disease
DISM: Drug Inactivation by Structure Modification
Drug Resistance Data Categorized by Drug
Approved Drug(s)
5 drug(s) in total
Dibekacin
Drug Resistance Data Categorized by Their Corresponding Mechanisms | ||||
Drug Inactivation by Structure Modification (DISM) | ||||
Key Molecule: Bifunctional AAC/APH (AAC/APH) | [1] | |||
Resistant Disease | Gram-negative pathogens infection [ICD-11: 1B74-1G40] | |||
Molecule Alteration | Expression | Up-regulation |
||
Resistant Drug | Dibekacin | |||
Experimental Note | Identified from the Human Clinical Data | |||
In Vitro Model | Escherichia coli BL21(DE3) | 469008 | ||
Escherichia coli JM83 | 562 | |||
Experiment for Molecule Alteration |
SDS-PAGE assay | |||
Experiment for Drug Resistance |
Broth microdilution method assay | |||
Mechanism Description | Aminoglycoside 2"-phosphotransferases are the major aminoglycoside-modifying enzymes in clinical isolates of enterococci and staphylococci.APH(2")-If. This enzyme confers resistance to the 4,6-disubstituted aminoglycosides kanamycin, tobramycin, dibekacin, gentamicin, and sisomicin, but not to arbekacin, amikacin, isepamicin, or netilmicin. |
Gentamicin A
Drug Resistance Data Categorized by Their Corresponding Mechanisms | ||||
Drug Inactivation by Structure Modification (DISM) | ||||
Key Molecule: Bifunctional AAC/APH (AAC/APH) | [1] | |||
Resistant Disease | Gram-negative pathogens infection [ICD-11: 1B74-1G40] | |||
Molecule Alteration | Expression | Up-regulation |
||
Resistant Drug | Gentamicin A | |||
Experimental Note | Identified from the Human Clinical Data | |||
In Vitro Model | Escherichia coli BL21(DE3) | 469008 | ||
Escherichia coli JM83 | 562 | |||
Experiment for Molecule Alteration |
SDS-PAGE assay | |||
Experiment for Drug Resistance |
Broth microdilution method assay | |||
Mechanism Description | Aminoglycoside 2"-phosphotransferases are the major aminoglycoside-modifying enzymes in clinical isolates of enterococci and staphylococci.APH(2")-If. This enzyme confers resistance to the 4,6-disubstituted aminoglycosides kanamycin, tobramycin, dibekacin, gentamicin, and sisomicin, but not to arbekacin, amikacin, isepamicin, or netilmicin. |
Kanamycin
Drug Resistance Data Categorized by Their Corresponding Mechanisms | ||||
Drug Inactivation by Structure Modification (DISM) | ||||
Key Molecule: Bifunctional AAC/APH (AAC/APH) | [1] | |||
Resistant Disease | Gram-negative pathogens infection [ICD-11: 1B74-1G40] | |||
Molecule Alteration | Expression | Up-regulation |
||
Resistant Drug | Kanamycin | |||
Experimental Note | Identified from the Human Clinical Data | |||
In Vitro Model | Escherichia coli BL21(DE3) | 469008 | ||
Escherichia coli JM83 | 562 | |||
Experiment for Molecule Alteration |
SDS-PAGE assay | |||
Experiment for Drug Resistance |
Broth microdilution method assay | |||
Mechanism Description | Aminoglycoside 2"-phosphotransferases are the major aminoglycoside-modifying enzymes in clinical isolates of enterococci and staphylococci.APH(2")-If. This enzyme confers resistance to the 4,6-disubstituted aminoglycosides kanamycin, tobramycin, dibekacin, gentamicin, and sisomicin, but not to arbekacin, amikacin, isepamicin, or netilmicin. |
Sisomicin
Drug Resistance Data Categorized by Their Corresponding Mechanisms | ||||
Drug Inactivation by Structure Modification (DISM) | ||||
Key Molecule: Bifunctional AAC/APH (AAC/APH) | [1] | |||
Resistant Disease | Gram-negative pathogens infection [ICD-11: 1B74-1G40] | |||
Molecule Alteration | Expression | Up-regulation |
||
Resistant Drug | Sisomicin | |||
Experimental Note | Identified from the Human Clinical Data | |||
In Vitro Model | Escherichia coli BL21(DE3) | 469008 | ||
Escherichia coli JM83 | 562 | |||
Experiment for Molecule Alteration |
SDS-PAGE assay | |||
Experiment for Drug Resistance |
Broth microdilution method assay | |||
Mechanism Description | Aminoglycoside 2"-phosphotransferases are the major aminoglycoside-modifying enzymes in clinical isolates of enterococci and staphylococci.APH(2")-If. This enzyme confers resistance to the 4,6-disubstituted aminoglycosides kanamycin, tobramycin, dibekacin, gentamicin, and sisomicin, but not to arbekacin, amikacin, isepamicin, or netilmicin. |
Tobramycin
Drug Resistance Data Categorized by Their Corresponding Mechanisms | ||||
Drug Inactivation by Structure Modification (DISM) | ||||
Key Molecule: Bifunctional AAC/APH (AAC/APH) | [1] | |||
Resistant Disease | Gram-negative pathogens infection [ICD-11: 1B74-1G40] | |||
Molecule Alteration | Expression | Up-regulation |
||
Resistant Drug | Tobramycin | |||
Experimental Note | Identified from the Human Clinical Data | |||
In Vitro Model | Escherichia coli BL21(DE3) | 469008 | ||
Escherichia coli JM83 | 562 | |||
Experiment for Molecule Alteration |
SDS-PAGE assay | |||
Experiment for Drug Resistance |
Broth microdilution method assay | |||
Mechanism Description | Aminoglycoside 2"-phosphotransferases are the major aminoglycoside-modifying enzymes in clinical isolates of enterococci and staphylococci.APH(2")-If. This enzyme confers resistance to the 4,6-disubstituted aminoglycosides kanamycin, tobramycin, dibekacin, gentamicin, and sisomicin, but not to arbekacin, amikacin, isepamicin, or netilmicin. |
References
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