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http://purl.uniprot.org/citations/12242332http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12242332http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12242332http://www.w3.org/2000/01/rdf-schema#comment"This paper describes insig-2, a second protein of the endoplasmic reticulum that blocks the processing of sterol regulatory element-binding proteins (SREBPs) by binding to SCAP (SREBP cleavage-activating protein) in a sterol-regulated fashion, thus preventing it from escorting SREBPs to the Golgi. By blocking this movement, insig-2, like the previously described insig-1, prevents the proteolytic processing of SREBPs by Golgi enzymes, thereby blocking cholesterol synthesis. The sequences of human insig-1 and -2 are 59% identical. Both proteins are predicted to contain six transmembrane helices. The proteins differ functionally in two respects: (i) production of insig-1, but not insig-2, in cultured mammalian cells requires nuclear SREBPs; and (ii) at high levels of expression, insig-1, but not insig-2, can block SCAP movement in the absence of exogenous sterols. The combined actions of insig-1 and -2 permit feedback regulation of cholesterol synthesis over a wide range of sterol concentrations."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.org/dc/terms/identifier"doi:10.1073/pnas.162488899"xsd:string
http://purl.uniprot.org/citations/12242332http://purl.org/dc/terms/identifier"doi:10.1073/pnas.162488899"xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/author"Brown M.S."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/author"Brown M.S."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/author"Goldstein J.L."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/author"Goldstein J.L."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/author"Yabe D."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/author"Yabe D."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/pages"12753-12758"xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/pages"12753-12758"xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/title"Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/title"Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins."xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/volume"99"xsd:string
http://purl.uniprot.org/citations/12242332http://purl.uniprot.org/core/volume"99"xsd:string
http://purl.uniprot.org/citations/12242332http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12242332
http://purl.uniprot.org/citations/12242332http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12242332
http://purl.uniprot.org/citations/12242332http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12242332
http://purl.uniprot.org/citations/12242332http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12242332