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http://purl.uniprot.org/citations/11953458http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11953458http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11953458http://www.w3.org/2000/01/rdf-schema#comment"beta-Site APP-cleaving enzyme (BACE) initiates the processing of the amyloid precursor protein (APP) leading to the generation of beta-amyloid, the main component of Alzheimer's disease senile plaques. BACE (Asp2, memapsin 2) is a type I transmembrane aspartic protease responsible for the beta-secretase cleavage of APP producing a soluble form of the ectodomain (sAPPbeta) and the membrane-bound, carboxy-terminal intermediates C99 and C89. BACE maturation involves cysteine bridge formation, N -glycosylation and propeptide removal. We investigated variants of BACE in which the disulphide bonds of the catalytic domain spanning between Cys216/Cys420, Cys278/Cys443 and Cys330/Cys380 were removed by mutagenesis. When transfected in cultured cells, these mutants showed impaired maturation. Nevertheless, a fraction of mutated protein retained both the competence to mature as well as the activity to process APP. For the generation of a functional enzyme the conserved Cys330/Cys380 bond was the most critical, whereas the two bonds between Cys216/Cys420 and Cys278/Cys443, which are typical for the membrane-bound BACE, appeared to be less important."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.org/dc/terms/identifier"doi:10.1046/j.0022-3042.2002.00806.x"xsd:string
http://purl.uniprot.org/citations/11953458http://purl.org/dc/terms/identifier"doi:10.1046/j.0022-3042.2002.00806.x"xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/author"Molinari M."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/author"Molinari M."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/author"Fischer F."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/author"Fischer F."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/author"Bodendorf U."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/author"Bodendorf U."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/author"Paganetti P."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/author"Paganetti P."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/name"J. Neurochem."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/name"J. Neurochem."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/pages"1079-1088"xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/pages"1079-1088"xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/title"The disulphide bonds in the catalytic domain of BACE are critical but not essential for amyloid precursor protein processing activity."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/title"The disulphide bonds in the catalytic domain of BACE are critical but not essential for amyloid precursor protein processing activity."xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/volume"80"xsd:string
http://purl.uniprot.org/citations/11953458http://purl.uniprot.org/core/volume"80"xsd:string
http://purl.uniprot.org/citations/11953458http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11953458
http://purl.uniprot.org/citations/11953458http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11953458