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http://purl.uniprot.org/citations/22267734http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22267734http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22267734http://www.w3.org/2000/01/rdf-schema#comment"The cellular levels of β-site APP cleaving enzyme 1 (BACE1), the rate-limiting enzyme for the generation of the Alzheimer disease (AD) amyloid β-peptide (Aβ), are tightly regulated by two ER-based acetyl-CoA:lysine acetyltransferases, ATase1 and ATase2. Here we report that both acetyltransferases are expressed in neurons and glial cells, and are up-regulated in the brain of AD patients. We also report the identification of first and second generation compounds that inhibit ATase1/ATase2 and down-regulate the expression levels as well as activity of BACE1. The mechanism of action involves competitive and non-competitive inhibition as well as generation of unstable intermediates of the ATases that undergo degradation."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.310136"xsd:string
http://purl.uniprot.org/citations/22267734http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.310136"xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Ding Y."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Ding Y."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Luo Y."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Luo Y."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Pehar M."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Pehar M."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Puglielli L."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Puglielli L."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Ko M.H."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Ko M.H."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Peters N.R."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Peters N.R."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Kotch F."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Kotch F."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Salamat S.M."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/author"Salamat S.M."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/22267734http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string