| http://purl.uniprot.org/citations/10461923 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10461923 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10461923 | http://www.w3.org/2000/01/rdf-schema#comment | "The beta-amyloid precursor protein (beta-APP) contains a copper-binding site localized between amino acids 135 and 156 (beta-APP(135-156)). We have employed synthetic beta-APP peptides to characterize their capacities to reduce Cu(II) to Cu(I). Analogues of the wild-type beta-APP(135-156) peptide, containing specific amino acid substitutions, were used to establish which residues are specifically involved in the reduction of copper by beta-APP(135-156). We report here that beta-APP's copper-binding domain reduced Cu(II) to Cu(I). The single-mutant beta-APP(His147-->Ala) and the double-mutant beta-APP(His147-->Ala/His149-->Ala) showed a small decrease in copper reduction in relation to the wild-type peptide and the beta-APP(Cys144-->Ser) mutation abolished it, suggesting that Cys144 is the key amino acid in the oxidoreduction reaction. Our results confirm that soluble beta-APP is involved in the reduction of Cu(II) to Cu(I)."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.org/dc/terms/identifier | "doi:10.1046/j.1471-4159.1999.0731288.x"xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.org/dc/terms/identifier | "doi:10.1046/j.1471-4159.1999.0731288.x"xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/author | "Gonzalez M."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/author | "Gonzalez M."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/author | "Bodini M."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/author | "Bodini M."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/author | "Inestrosa N.C."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/author | "Inestrosa N.C."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/author | "Opazo C."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/author | "Opazo C."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/author | "Ruiz F.H."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/author | "Ruiz F.H."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/name | "J. Neurochem."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/name | "J. Neurochem."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/pages | "1288-1292"xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/pages | "1288-1292"xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/title | "Cysteine 144 is a key residue in the copper reduction by the beta-amyloid precursor protein."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/title | "Cysteine 144 is a key residue in the copper reduction by the beta-amyloid precursor protein."xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/volume | "73"xsd:string |
| http://purl.uniprot.org/citations/10461923 | http://purl.uniprot.org/core/volume | "73"xsd:string |