The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

AC1L18FY     4-[2-[3-[[4-[[[5-(6- aminopurin-9-yl)-4...

Synonyms: 1553-55-5, 174531-EP2284158A1, 3-Hydroxy-3-methylglutaryl-CoA
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of hydroxymethylglutaryl-CoA


Psychiatry related information on hydroxymethylglutaryl-CoA

  • HMG-CoA (3-hydroxy-3-methylglutarylcoenzyme A) reductase inhibitors (statins) mediate clinically significant vascular risk reduction in patients without inflammatory disease and might have immunomodulatory function [6].

High impact information on hydroxymethylglutaryl-CoA


Chemical compound and disease context of hydroxymethylglutaryl-CoA


Biological context of hydroxymethylglutaryl-CoA


Anatomical context of hydroxymethylglutaryl-CoA


Associations of hydroxymethylglutaryl-CoA with other chemical compounds


Gene context of hydroxymethylglutaryl-CoA


Analytical, diagnostic and therapeutic context of hydroxymethylglutaryl-CoA


  1. Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene. Ishii, S., Xu, Y.H., Stratton, R.H., Roe, B.A., Merlino, G.T., Pastan, I. Proc. Natl. Acad. Sci. U.S.A. (1985) [Pubmed]
  2. Crystal structure of a statin bound to a class II hydroxymethylglutaryl-CoA reductase. Tabernero, L., Rodwell, V.W., Stauffacher, C.V. J. Biol. Chem. (2003) [Pubmed]
  3. Avian 3-hydroxy-3-methylglutaryl-CoA synthase. Characterization of a recombinant cholesterogenic isozyme and demonstration of the requirement for a sulfhydryl functionality in formation of the acetyl-enzyme reaction intermediate. Misra, I., Narasimhan, C., Miziorko, H.M. J. Biol. Chem. (1993) [Pubmed]
  4. Cholesterol metabolism in alloxan-induced diabetic rabbits. O'Meara, N.M., Devery, R.A., Owens, D., Collins, P.B., Johnson, A.H., Tomkin, G.H. Diabetes (1990) [Pubmed]
  5. Characterization of an HMG-CoA Reductase from Listeria monocytogenes That Exhibits Dual Coenzyme Specificity. Theivagt, A.E., Amanti, E.N., Beresford, N.J., Tabernero, L., Friesen, J.A. Biochemistry (2006) [Pubmed]
  6. Trial of Atorvastatin in Rheumatoid Arthritis (TARA): double-blind, randomised placebo-controlled trial. McCarey, D.W., McInnes, I.B., Madhok, R., Hampson, R., Scherbakov, O., Ford, I., Capell, H.A., Sattar, N. Lancet (2004) [Pubmed]
  7. Structural mechanism for statin inhibition of HMG-CoA reductase. Istvan, E.S., Deisenhofer, J. Science (2001) [Pubmed]
  8. Reproducing abnormal cholesterol biosynthesis as seen in the Smith-Lemli-Opitz syndrome by inhibiting the conversion of 7-dehydrocholesterol to cholesterol in rats. Xu, G., Salen, G., Shefer, S., Ness, G.C., Chen, T.S., Zhao, Z., Tint, G.S. J. Clin. Invest. (1995) [Pubmed]
  9. A cell-based, high-throughput screen for small molecule regulators of hepatitis C virus replication. Kim, S.S., Peng, L.F., Lin, W., Choe, W.H., Sakamoto, N., Schreiber, S.L., Chung, R.T. Gastroenterology (2007) [Pubmed]
  10. Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver. Clarke, P.R., Hardie, D.G. EMBO J. (1990) [Pubmed]
  11. Apparent coordination of the biosynthesis of lipids in cultured cells: its relationship to the regulation of the membrane sterol:phospholipid ratio and cell cycling. Cornell, R.B., Horwitz, A.F. J. Cell Biol. (1980) [Pubmed]
  12. Experimental lovastatin myopathy. Waclawik, A.J., Lindal, S., Engel, A.G. J. Neuropathol. Exp. Neurol. (1993) [Pubmed]
  13. Lipid-lowering therapy in patients with renal disease. Massy, Z.A., Ma, J.Z., Louis, T.A., Kasiske, B.L. Kidney Int. (1995) [Pubmed]
  14. Cloning, characterization and expression of the gene encoding cytochrome P-450sca-2 from Streptomyces carbophilus involved in production of pravastatin, a specific HMG-CoA reductase inhibitor. Watanabe, I., Nara, F., Serizawa, N. Gene (1995) [Pubmed]
  15. Toxicity of oxysterols to human monocyte-macrophages. Clare, K., Hardwick, S.J., Carpenter, K.L., Weeratunge, N., Mitchinson, M.J. Atherosclerosis (1995) [Pubmed]
  16. Syrian hamster 3-hydroxy-3-methylglutaryl-coenzyme A reductase expressed in Escherichia coli: production of homogeneous protein. Frimpong, K., Darnay, B.G., Rodwell, V.W. Protein Expr. Purif. (1993) [Pubmed]
  17. Optional exon in the 5'-untranslated region of 3-hydroxy-3-methylglutaryl coenzyme A synthase gene: conserved sequence and splicing pattern in humans and hamsters. Gil, G., Smith, J.R., Goldstein, J.L., Brown, M.S. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  18. Modulation of 3-hydroxy-3-methylglutaryl-CoA reductase by changes in microsomal cholesterol content or phospholipid composition. Davis, P.J., Poznansky, M.J. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  19. Regulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system. Ingebritsen, T.S., Parker, R.A., Gibson, D.M. J. Biol. Chem. (1981) [Pubmed]
  20. Markedly reduced bile acid synthesis but maintained levels of cholesterol and vitamin D metabolites in mice with disrupted sterol 27-hydroxylase gene. Rosen, H., Reshef, A., Maeda, N., Lippoldt, A., Shpizen, S., Triger, L., Eggertsen, G., Björkhem, I., Leitersdorf, E. J. Biol. Chem. (1998) [Pubmed]
  21. Mannose 6-phosphate receptor-mediated uptake of modified low density lipoprotein results in down regulation of hydroxymethylglutaryl-CoA reductase in normal and familial hypercholesterolemic fibroblasts. Murray, G.J., Neville, D.M. J. Biol. Chem. (1980) [Pubmed]
  22. Biogenesis of 3-hydroxy-3-methylglutaryl-coenzyme A reductase, an integral glycoprotein of the endoplasmic reticulum. Brown, D.A., Simoni, R.D. Proc. Natl. Acad. Sci. U.S.A. (1984) [Pubmed]
  23. Blattella germanica has two HMG-CoA synthase genes. Both are regulated in the ovary during the gonadotrophic cycle. Buesa, C., Martínez-Gonzalez, J., Casals, N., Haro, D., Piulachs, M.D., Bellés, X., Hegardt, F.G. J. Biol. Chem. (1994) [Pubmed]
  24. Involvement of calcium in the mevalonate-accelerated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase. Roitelman, J., Bar-Nun, S., Inoue, S., Simoni, R.D. J. Biol. Chem. (1991) [Pubmed]
  25. Dissociation of beta-hydroxy-beta-methylglutaryl-CoA reductase activity from the overall rate of cholesterol synthesis in the liver following the intravenous administration of lipid. Nervi, F.O., Carrella, M., Dietschy, J.M. J. Biol. Chem. (1976) [Pubmed]
  26. Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism. Hunt, M.C., Solaas, K., Kase, B.F., Alexson, S.E. J. Biol. Chem. (2002) [Pubmed]
  27. Roles of endogenously synthesized sterols in the endocytic pathway. Sugii, S., Lin, S., Ohgami, N., Ohashi, M., Chang, C.C., Chang, T.Y. J. Biol. Chem. (2006) [Pubmed]
  28. A novel human hepatic organic anion transporting polypeptide (OATP2). Identification of a liver-specific human organic anion transporting polypeptide and identification of rat and human hydroxymethylglutaryl-CoA reductase inhibitor transporters. Hsiang, B., Zhu, Y., Wang, Z., Wu, Y., Sasseville, V., Yang, W.P., Kirchgessner, T.G. J. Biol. Chem. (1999) [Pubmed]
  29. Inactivation of hydroxymethylglutaryl-CoA reductase from yeast by coenzyme A disulfide. Gilbert, H.F., Stewart, M.D. J. Biol. Chem. (1981) [Pubmed]
  30. Evidence for substrate channeling in the early steps of cholesterogenesis. Miziorko, H.M., Laib, F.E., Behnke, C.E. J. Biol. Chem. (1990) [Pubmed]
  31. ERG10 from Saccharomyces cerevisiae encodes acetoacetyl-CoA thiolase. Hiser, L., Basson, M.E., Rine, J. J. Biol. Chem. (1994) [Pubmed]
  32. Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae. Loayza, D., Tam, A., Schmidt, W.K., Michaelis, S. Mol. Biol. Cell (1998) [Pubmed]
  33. Bacterial expression of the catalytic domain of 3-hydroxy-3-methylglutaryl-CoA reductase (isoform HMGR1) from Arabidopsis thaliana, and its inactivation by phosphorylation at Ser577 by Brassica oleracea 3-hydroxy-3-methylglutaryl-CoA reductase kinase. Dale, S., Arró, M., Becerra, B., Morrice, N.G., Boronat, A., Hardie, D.G., Ferrer, A. Eur. J. Biochem. (1995) [Pubmed]
  34. Overexpression of OSBP-related protein 2 (ORP2) induces changes in cellular cholesterol metabolism and enhances endocytosis. Hynynen, R., Laitinen, S., Käkelä, R., Tanhuanpää, K., Lusa, S., Ehnholm, C., Somerharju, P., Ikonen, E., Olkkonen, V.M. Biochem. J. (2005) [Pubmed]
  35. Mutant clone of Chinese hamster ovary cells lacking 3-hydroxy-3 -methylglutaryl coenzyme A reductase. Mosley, S.T., Brown, M.S., Anderson, R.G., Goldstein, J.L. J. Biol. Chem. (1983) [Pubmed]
  36. Characterization of the hydroxymethylglutaryl-CoA lyase precursor, a protein targeted to peroxisomes and mitochondria. Ashmarina, L.I., Robert, M.F., Elsliger, M.A., Mitchell, G.A. Biochem. J. (1996) [Pubmed]
  37. Protein engineering of the HMG-CoA reductase of Pseudomonas mevalonii. Construction of mutant enzymes whose activity is regulated by phosphorylation and dephosphorylation. Friesen, J.A., Rodwell, V.W. Biochemistry (1997) [Pubmed]
  38. 26-hydroxycholesterol: regulation of hydroxymethylglutaryl-CoA reductase activity in Chinese hamster ovary cell culture. Esterman, A.L., Baum, H., Javitt, N.B., Darlington, G.J. J. Lipid Res. (1983) [Pubmed]
WikiGenes - Universities