Resistance to the HIV protease inhibitor amprenavir in vitro and in clinical studies: A review

Clinical Drug Investigation

Volumn 20, Issue 4, 2000, Pages 267-285

  Tisdale, Margaret ^a   Myers, Richard ^a   Randall, Sharon ^a   Maguire, Michael ^a   Ait Khaled, Mounir ^a   Elston, Rob ^a   Snowden, Wendy ^a  

^a GLAXOSMITHKLINE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMPRENAVIR; INDINAVIR; ISOLEUCINE; LAMIVUDINE; NELFINAVIR; PROTEINASE INHIBITOR; RITONAVIR; RNA DIRECTED DNA POLYMERASE INHIBITOR; SAQUINAVIR; VALINE; ZIDOVUDINE;

AMINO ACID SUBSTITUTION; CONTROLLED STUDY; CROSS RESISTANCE; DRUG ACTIVITY; DRUG HYPERSENSITIVITY; DRUG STRUCTURE; GENOTYPE; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; IN VITRO STUDY; PHENOTYPE; PRIORITY JOURNAL; REVIEW; TREATMENT FAILURE;

EID: 0033766373     PISSN: 11732563     EISSN: None     Source Type: Journal    
DOI: 10.2165/00044011-200020040-00008     Document Type: Review

References (4)

1. Kohl NE, Emini EA, Schleif WA, et al. Active human immunodeficiency virus protease is required for viral infectivity. Proc Natl Acad Sci USA 1998: 85: 4686-90
2. Navia MA, Fitzgerald PMD, McKeever BM, et al. Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1. Nature 1989 Feb; 337 (6208): 615-20
3. Wlodawer A, Miller M. Jaskolski M, et al. Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease. Science 1989 Aug; 245: 616-21
4. Wlodawer A, Erickson JW. Structure-based inhibitors of HIV-1 protease. Annu Rev Biochem 1993; 62: 543-85