Proteolytic Processing of HIV-1 Protease Precursor, Kinetics and Mechanism
Open Access
- 1 August 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (33) , 23437-23442
- https://doi.org/10.1074/jbc.274.33.23437
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- HIV-Protease InhibitorsNew England Journal of Medicine, 1998
- Molecular mechanisms for the conversion of zymogens to active proteolytic enzymesProtein Science, 1998
- Hydrophilic Peptides Derived from the Transframe Region of Gag-Pol Inhibit the HIV-1 ProteaseBiochemistry, 1998
- Sequence‐Specific Resonance Assignments of the 1H‐NMR Spectra and Structural Characterization in Solution of the HIV‐1 Transframe Protein p6*European Journal of Biochemistry, 1996
- A Transient Precursor of the HIV-1 ProteaseJournal of Biological Chemistry, 1996
- Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein.Proceedings of the National Academy of Sciences, 1994
- Overexpression of the HIV-1 Gag-Pol Polyprotein Results in Intracellular Activation of HIV-1 Protease and Inhibition of Assembly and Budding of Virus-like ParticlesVirology, 1993
- Intrinsic activity of precursor forms of HIV‐1 proteinaseFEBS Letters, 1992
- Deletion of sequences upstream of the proteinase improves the proteolytic processing of human immunodeficiency virus type 1.Proceedings of the National Academy of Sciences, 1991
- Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity.Proceedings of the National Academy of Sciences, 1991