Flap opening and dimer-interface flexibility in the free and inhibitor-bound HIV protease, and their implications for function
Open Access
- 1 September 1999
- Vol. 7 (9) , 1047-S12
- https://doi.org/10.1016/s0969-2126(99)80172-5
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- Resistance to HIV protease inhibitorsHaemophilia, 1998
- Increasing survival in AIDS patients with cytomegalovirus retinitis treated with combination antiretroviral therapy including HIV protease inhibitorsAIDS, 1998
- Domain Flexibility in Retroviral Proteases: Structural Implications for Drug Resistant Mutations,Biochemistry, 1998
- A Combined Quantum/Classical Molecular Dynamics Study of the Catalytic Mechanism of HIV ProteaseJournal of Molecular Biology, 1996
- Structural Mechanisms of HIV Drug ResistanceAnnual Review of Pharmacology and Toxicology, 1996
- Cyclic HIV Protease Inhibitors: Synthesis, Conformational Analysis, P2/P2‘ Structure−Activity Relationship, and Molecular Recognition of Cyclic UreasJournal of Medicinal Chemistry, 1996
- Crystal Structures of Complexes of a Peptidic Inhibitor with Wild-Type and Two Mutant HIV-1 Proteases,Biochemistry, 1996
- Flap opening in HIV-1 protease simulated by ‘activated’ molecular dynamicsNature Structural & Molecular Biology, 1995
- Molecular dynamics simulation of HIV-1 protease in a crystalline environment and in solutionBiochemistry, 1993
- Domain communication in the dynamical structure of human immunodeficiency virus 1 protease.Proceedings of the National Academy of Sciences, 1990