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http://purl.uniprot.org/citations/17079146http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17079146http://www.w3.org/2000/01/rdf-schema#comment"Phosphatidate phosphatase (PAP) enzymes catalyze the dephosphorylation of phosphatidate, yielding diacylglycerol and inorganic phosphate. In eukaryotic cells, PAP activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signaling molecules that are related to phosphatidate. There are two types of PAP enzyme, Mg(2+) dependent (PAP1) and Mg(2+) independent (PAP2), but only genes encoding PAP2 enzymes had been identified until recently, when a gene (PAH1) encoding a PAP1 enzyme was found in Saccharomyces cerevisiae. This discovery has revealed a molecular function of the mammalian protein lipin, a deficiency of which causes lipodystrophy in mice. With molecular information now available for both types of PAP, the specific roles of these enzymes in lipid metabolism are being clarified."xsd:string
http://purl.uniprot.org/citations/17079146http://purl.org/dc/terms/identifier"doi:10.1016/j.tibs.2006.10.003"xsd:string
http://purl.uniprot.org/citations/17079146http://purl.uniprot.org/core/author"Carman G.M."xsd:string
http://purl.uniprot.org/citations/17079146http://purl.uniprot.org/core/author"Han G.S."xsd:string
http://purl.uniprot.org/citations/17079146http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17079146http://purl.uniprot.org/core/name"Trends Biochem Sci"xsd:string
http://purl.uniprot.org/citations/17079146http://purl.uniprot.org/core/pages"694-699"xsd:string
http://purl.uniprot.org/citations/17079146http://purl.uniprot.org/core/title"Roles of phosphatidate phosphatase enzymes in lipid metabolism."xsd:string
http://purl.uniprot.org/citations/17079146http://purl.uniprot.org/core/volume"31"xsd:string
http://purl.uniprot.org/citations/17079146http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17079146
http://purl.uniprot.org/citations/17079146http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17079146
http://purl.uniprot.org/uniprot/#_Q04396-mappedCitation-17079146http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17079146
http://purl.uniprot.org/uniprot/#_Q05521-mappedCitation-17079146http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17079146
http://purl.uniprot.org/uniprot/#_P32567-mappedCitation-17079146http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17079146
http://purl.uniprot.org/uniprot/P32567http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17079146
http://purl.uniprot.org/uniprot/Q05521http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17079146
http://purl.uniprot.org/uniprot/Q04396http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17079146