Cysteine Nitrosylation Inactivates the HIV-1 Protease
- 29 September 1998
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 250 (3), 575-576
- https://doi.org/10.1006/bbrc.1998.9350
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriersNature Structural & Molecular Biology, 1998
- Nitric Oxide Inhibits Apoptosis by Preventing Increases in Caspase-3-like Activity via Two Distinct MechanismsJournal of Biological Chemistry, 1997
- Biosynthesis and action of nitric oxide in mammalian cellsTrends in Biochemical Sciences, 1997
- S-nitrosylation regulates apoptosisNature, 1997
- Suppression of Apoptosis by Nitric Oxide via Inhibition of Interleukin-1β–converting Enzyme (ICE)-like and Cysteine Protease Protein (CPP)-32–like ProteasesThe Journal of Experimental Medicine, 1997
- Redox signaling: Nitrosylation and related target interactions of nitric oxideCell, 1994
- Reactivity of Cysteine Residues in the Protease from Human Immunodeficiency Virus: Identification of a Surface-Exposed Region Which Affects Enzyme FunctionArchives of Biochemistry and Biophysics, 1993
- Viral proteinases: weakness in strengthBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1990
- Structure of Complex of Synthetic HIV-1 Protease with a Substrate-Based Inhibitor at 2.3 Å ResolutionScience, 1989
- Active human immunodeficiency virus protease is required for viral infectivity.Proceedings of the National Academy of Sciences, 1988