Structure and Expression of 3‐Hydroxy‐3‐methylglutaryl Coenzyme A Reductase^a

This publication has 20 references indexed in Scilit:

• Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation.
  Journal of Biological Chemistry, 1985
• Control of eukaryotic messenger RNA synthesis by sequence-specific DNA-binding proteins
  Nature, 1985
• 5′ end of hmg CoA reductase gene contains sequences responsible for cholesterol-mediated inhibition of transcription
  Cell, 1985
• Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme
  Cell, 1985
• Sterols accelerate degradation of hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase encoded by a constitutively expressed cDNA.
  Molecular and Cellular Biology, 1985
• Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum.
  Journal of Biological Chemistry, 1985
• HMG CoA reductase: A negatively regulated gene with unusual promoter and 5′ untranslated regions
  Cell, 1984
• Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum
  Nature, 1984
• Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold increase in 3-hydroxy-3-methylglutaryl-coenzyme A reductase.
  Proceedings of the National Academy of Sciences, 1982
• Competitive inhibition of 3‐hydroxy‐3‐methylglutaryl coenzyme a reductase by ML‐236A and ML‐236B fungal metabolites, having hypocholesterolemic activity
  FEBS Letters, 1976