Qualitative study of drug resistance in retroviral protease using structural modeling and site-directed mutagenesis.
Department of Molecular Systems, Merck Research Laboratories, West Point, Pennsylvania 19486.
J C
JC
Culberson
B L
BL
Bush
V V
VV
Sardana
D000595:Amino Acid Sequence; D000998:Antiviral Agents / Q000737:chemistry / Q000494:pharmacology*; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites; D003198:Computer Simulation; D004352:Drug Resistance, Microbial; D016333:HIV Protease / Q000737:chemistry / Q000235:genetics; D017320:HIV Protease Inhibitors / Q000737:chemistry / Q000494:pharmacology; D015497:HIV-1 / Q000187:drug effects / Q000201:enzymology; D015498:HIV-2 / Q000187:drug effects / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D011487:Protein Conformation; D012190:Retroviridae / Q000187:drug effects* / Q000235:genetics; D012191:Retroviridae Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics; D012984:Software; D013379:Substrate Specificity
D000998:Antiviral Agents; D017320:HIV Protease Inhibitors; D012191:Retroviridae Proteins; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease; C065184:p16 protease, Human immunodeficiency virus 2