Degradation of 3-Hydroxy-3-methylglutaryl-CoA Reductase in Endoplasmic Reticulum Membranes Is Accelerated as a Result of Increased Susceptibility to Proteolysis

This publication has 42 references indexed in Scilit:

• Inhibition of Proteasome Activities and Subunit-Specific Amino-Terminal Threonine Modification by Lactacystin
  Science, 1995
• Distinct sterol and nonsterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase.
  Published by Elsevier ,1992
• Immunological evidence for eight spans in the membrane domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase: implications for enzyme degradation in the endoplasmic reticulum
  The Journal of cell biology, 1992
• The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase.
  Published by Elsevier ,1992
• Involvement of calcium in the mevalonate-accelerated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase
  Published by Elsevier ,1991
• The regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase requires a short-lived protein and occurs in the endoplasmic reticulum.
  Published by Elsevier ,1990
• Regulation of the mevalonate pathway
  Nature, 1990
• Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme
  Cell, 1985
• Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes
  Analytical Biochemistry, 1984
• Preparation of delipidized serum protein for use in cell culture systems
  In Vitro Cellular & Developmental Biology - Plant, 1976