| http://purl.uniprot.org/citations/10677483 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10677483 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10677483 | http://www.w3.org/2000/01/rdf-schema#comment | "The cDNAs of two new human membrane-associated aspartic proteases, memapsin 1 and memapsin 2, have been cloned and sequenced. The deduced amino acid sequences show that each contains the typical pre, pro, and aspartic protease regions, but each also has a C-terminal extension of over 80 residues, which includes a single transmembrane domain and a C-terminal cytosolic domain. Memapsin 2 mRNA is abundant in human brain. The protease domain of memapsin 2 cDNA was expressed in Escherichia coli and was purified. Recombinant memapsin 2 specifically hydrolyzed peptides derived from the beta-secretase site of both the wild-type and Swedish mutant beta-amyloid precursor protein (APP) with over 60-fold increase of catalytic efficiency for the latter. Expression of APP and memapsin 2 in HeLa cells showed that memapsin 2 cleaved the beta-secretase site of APP intracellularly. These and other results suggest that memapsin 2 fits all of the criteria of beta-secretase, which catalyzes the rate-limiting step of the in vivo production of the beta-amyloid (Abeta) peptide leading to the progression of Alzheimer's disease. Recombinant memapsin 2 also cleaved a peptide derived from the processing site of presenilin 1, albeit with poor kinetic efficiency. Alignment of cleavage site sequences of peptides indicates that the specificity of memapsin 2 resides mainly at the S(1)' subsite, which prefers small side chains such as Ala, Ser, and Asp."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.97.4.1456"xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.97.4.1456"xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Lin X."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Lin X."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Wu S."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Wu S."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Tang J."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Tang J."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Dashti A."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Dashti A."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Downs D."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Downs D."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Koelsch G."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/author | "Koelsch G."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/pages | "1456-1460"xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/pages | "1456-1460"xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/title | "Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein."xsd:string |
| http://purl.uniprot.org/citations/10677483 | http://purl.uniprot.org/core/title | "Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein."xsd:string |