Oligomerization State Influences the Degradation Rate of 3-Hydroxy-3-methylglutaryl-CoA Reductase
Open Access
- 1 June 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (24) , 17171-17178
- https://doi.org/10.1074/jbc.274.24.17171
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Niemann-Pick C1 Disease Gene: Homology to Mediators of Cholesterol HomeostasisScience, 1997
- Degradation of 3-Hydroxy-3-methylglutaryl-CoA Reductase in Endoplasmic Reticulum Membranes Is Accelerated as a Result of Increased Susceptibility to ProteolysisJournal of Biological Chemistry, 1996
- Dimerization of Transcobalamin II ReceptorJournal of Biological Chemistry, 1996
- Crystal Structure of Pseudomonas mevalonii HMG-CoA Reductase at 3.0 Angstrom ResolutionScience, 1995
- Controlling Signal Transduction with Synthetic LigandsScience, 1993
- Biosynthesis of N-acetylglucosamine-P-P-dolichol, the committed step of asparagine-linked oligosaccharide assemblyGlycobiology, 1991
- Regulation of the mevalonate pathwayNature, 1990
- In sire determination of the functional size of hepatic 3-hydroxy-3-methylglutaryl-CoA reductase by radiation inactivation analysisBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Partial deletion of membrane-bound domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase eliminates sterol-enhanced degradation and prevents formation of crystalloid endoplasmic reticulum.The Journal of cell biology, 1987
- Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzymeCell, 1985