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http://purl.uniprot.org/citations/10833507http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10833507http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10833507http://www.w3.org/2000/01/rdf-schema#comment"We isolated a cDNA encoding a novel protein, XB51, that interacts with the amino-terminal domain of the neuron-specific X11-like protein (X11L). The protein XB51 inhibited the association of X11L with amyloid precursor protein through a non-competitive mechanism and abolished the suppression of beta-amyloid production by X11L. The majority of XB51 is localized around the nucleus and recovered in 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS) buffer-insoluble fraction when XB51 is expressed in cells. Association of XB51 with X11L changed the intracellular distribution of XB51 and resulted in redistribution of XB51 into the CHAPS buffer-soluble fraction. These observations suggest that XB51, together with X11L, plays an important role in the regulatory system of amyloid precursor protein metabolism and beta-amyloid generation."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c000302200"xsd:string
http://purl.uniprot.org/citations/10833507http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c000302200"xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/author"Lee D.-S."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/author"Lee D.-S."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/author"Suzuki T."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/author"Suzuki T."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/author"Kirino Y."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/author"Kirino Y."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/author"Tomita S."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/author"Tomita S."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/pages"23134-23138"xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/pages"23134-23138"xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/title"Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/title"Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein."xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/volume"275"xsd:string
http://purl.uniprot.org/citations/10833507http://purl.uniprot.org/core/volume"275"xsd:string
http://purl.uniprot.org/citations/10833507http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10833507
http://purl.uniprot.org/citations/10833507http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10833507