http://purl.uniprot.org/citations/6580634 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/6580634 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/6580634 | http://www.w3.org/2000/01/rdf-schema#comment | "3-Hydroxy-3-methylglutaryl-CoA reductase (EC 1.1.1.34) is an abundant protein of the crystalloid endoplasmic reticulum of UT-1 cells, a line of cultured hamster cells that over-produces the reductase as a result of gene amplification. In the current studies, we show that reductase in UT-1 cells is a glycoprotein. The solubilized enzyme (Mr = 97,000) from UT-1 cells, Chinese hamster ovary cells, and rat liver was adsorbed quantitatively and specifically to concanavalin A-Sepharose. UT-1 cells incorporated [1,6-3H]glucosamine into the reductase; after release with endo-N-acetylglucosaminidase H most of the radioactivity was found in N-linked "high-mannose" chains, including Man6(GlcNAc)2, Man7(GlcNAc)2, and Man8(GlcNAc)2. The carbohydrate of the reductase was localized to a 30-to 35-kilodalton fragment that was separable proteolytically from a cytoplasmic 53-kilodalton fragment that contained the active site of the enzyme. We conclude that 3-hydroxy-3-methylglutaryl-CoA reductase is a transmembrane glycoprotein with an active site facing the cytoplasm and a carbohydrate-bearing site oriented toward the lumen of the endoplasmic reticulum."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.80.23.7165"xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.80.23.7165"xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "Anderson R.G."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "Anderson R.G."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "Cummings R.D."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "Cummings R.D."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "Brown M.S."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "Brown M.S."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "Goldstein J.L."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "Goldstein J.L."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "DeMartino G.N."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "DeMartino G.N."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "Liscum L."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/author | "Liscum L."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/date | "1983"xsd:gYear |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/date | "1983"xsd:gYear |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/pages | "7165-7169"xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/pages | "7165-7169"xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/title | "3-Hydroxy-3-methylglutaryl-CoA reductase: a transmembrane glycoprotein of the endoplasmic reticulum with N-linked 'high-mannose' oligosaccharides."xsd:string |
http://purl.uniprot.org/citations/6580634 | http://purl.uniprot.org/core/title | "3-Hydroxy-3-methylglutaryl-CoA reductase: a transmembrane glycoprotein of the endoplasmic reticulum with N-linked 'high-mannose' oligosaccharides."xsd:string |