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http://purl.uniprot.org/citations/16982417http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16982417http://www.w3.org/2000/01/rdf-schema#comment"Alzheimer's disease (AD) may result from the accumulation of amyloid-beta (Abeta) peptides in the brain. The cysteine protease cathepsin B (CatB) is associated with amyloid plaques in AD brains and has been suspected to increase Abeta production. Here, we demonstrate that CatB actually reduces levels of Abeta peptides, especially the aggregation-prone species Abeta1-42, through proteolytic cleavage. Genetic inactivation of CatB in mice with neuronal expression of familial AD-mutant human amyloid precursor protein (hAPP) increased the relative abundance of Abeta1-42, worsening plaque deposition and other AD-related pathologies. Lentivirus-mediated expression of CatB in aged hAPP mice reduced preexisting amyloid deposits, even thioflavin S-positive plaques. Under cell-free conditions, CatB effectively cleaved Abeta1-42, generating C-terminally truncated Abeta peptides that are less amyloidogenic. Thus, CatB likely fulfills antiamyloidogenic and neuroprotective functions. Insufficient CatB activity might promote AD; increasing CatB activity could counteract the neuropathology of this disease."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.org/dc/terms/identifier"doi:10.1016/j.neuron.2006.07.027"xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Arai H."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Esposito L."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Gan L."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Sun B."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Wang X."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Zhou Y."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Yu G."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Roberson E.D."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Mucke L."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/author"Mueller-Steiner S."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/name"Neuron"xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/pages"703-714"xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/title"Antiamyloidogenic and neuroprotective functions of cathepsin B: implications for Alzheimer's disease."xsd:string
http://purl.uniprot.org/citations/16982417http://purl.uniprot.org/core/volume"51"xsd:string
http://purl.uniprot.org/citations/16982417http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16982417
http://purl.uniprot.org/citations/16982417http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16982417
http://purl.uniprot.org/uniprot/#_E0CXT9-mappedCitation-16982417http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16982417
http://purl.uniprot.org/uniprot/#_E0CYH3-mappedCitation-16982417http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16982417
http://purl.uniprot.org/uniprot/#_E0CYJ9-mappedCitation-16982417http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16982417
http://purl.uniprot.org/uniprot/#_E0CX28-mappedCitation-16982417http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16982417