Amino Acid Substitutions in Gag Protein at Non-cleavage Sites Are Indispensable for the Development of a High Multitude of HIV-1 Resistance against Protease Inhibitors
Open Access
- 1 February 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (8), 5952-5961
- https://doi.org/10.1074/jbc.m108005200
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- A Potent Human Immunodeficiency Virus Type 1 Protease Inhibitor, UIC-94003 (TMC-126), and Selection of a Novel (A28S) Mutation in the Protease Active SiteJournal of Virology, 2002
- Structural Consequences of Cyclophilin A Binding on Maturational Refolding in Human Immunodeficiency Virus Type 1 Capsid ProteinJournal of Virology, 2001
- Structural biology of HIV 1 1Edited by P. E. WrightJournal of Molecular Biology, 1999
- Molecular recognition in the HIV-1 capsid/cyclophilin A complex 1 1Edited by J. A. WellsJournal of Molecular Biology, 1997
- Comparison of the NMR and X‐ray structures of the HIV‐1 matrix protein: Evidence for conformational changes during viral assemblyProtein Science, 1996
- Kinetic Characterization and Cross-Resistance Patterns Of HIV-1 Protease Mutants Selected under Drug PressureBiochemistry, 1995
- Thegagprecursor contains a specific HIV-1 protease cleavage site between the NC (P7) and P1 proteinsFEBS Letters, 1993
- Kynostatin (KNI-227 and -272, highly potent anti-HIV agents: conformationally constrained tripeptide inhibitors of HIV protease containing allophenylnorstatine.CHEMICAL & PHARMACEUTICAL BULLETIN, 1992
- Comparison of the HIV‐1 and HIV‐2 proteinases using oligopeptide substrates representing cleavage sites in Gag and Gag‐Pol polyproteinsFEBS Letters, 1991
- HIV-1 protease specificity of peptide cleavage is sufficient for processing of gag and pol polyproteinsBiochemical and Biophysical Research Communications, 1988