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http://purl.uniprot.org/citations/12297508http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12297508http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12297508http://www.w3.org/2000/01/rdf-schema#comment"Presenilin and nicastrin are essential components of the gamma-secretase complex that is required for the intramembrane proteolysis of an increasing number of membrane proteins including the amyloid-beta precursor protein (APP) and Notch. By using co-immunoprecipitation and nickel affinity pull-down approaches, we now show that mammalian APH-1 (mAPH-1), a conserved multipass membrane protein, physically associates with nicastrin and the heterodimers of the presenilin amino- and carboxyl-terminal fragments in human cell lines and in rat brain. Similar to the loss of presenilin or nicastrin, the inactivation of endogenous mAPH-1 using small interfering RNAs results in the decrease of presenilin levels, accumulation of gamma-secretase substrates (APP carboxyl-terminal fragments), and reduction of gamma-secretase products (amyloid-beta peptides and the intracellular domains of APP and Notch). These data indicate that mAPH-1 is probably a functional component of the gamma-secretase complex required for the intramembrane proteolysis of APP and Notch."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m208164200"xsd:string
http://purl.uniprot.org/citations/12297508http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m208164200"xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Han W."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Han W."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Shah S."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Shah S."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Yu C."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Yu C."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Yu G."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Yu G."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Lee S.-F."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/author"Lee S.-F."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/pages"45013-45019"xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/pages"45013-45019"xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/title"Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch."xsd:string
http://purl.uniprot.org/citations/12297508http://purl.uniprot.org/core/title"Mammalian APH-1 interacts with presenilin and nicastrin and is required for intramembrane proteolysis of amyloid-beta precursor protein and Notch."xsd:string