| http://purl.uniprot.org/citations/11297421 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11297421 | http://www.w3.org/2000/01/rdf-schema#comment | "Amyloid precursor protein (APP) is the source of the neurotoxic amyloid beta (Abeta) peptide associated with Alzheimer's disease. Apolipoprotein A-I (apoA-I), a constituent of high-density lipoprotein complexes, was identified by a yeast two-hybrid system as a strong and specific binding partner of full-length APP (APPfl). This association between apoA-I and APPfl was localized to the extracellular domain of APP (APPextra). Furthermore, the interaction between apoA-I and APPfl was confirmed by coprecipitation using recombinant epitope-tagged APPextra and purified apoA-I. Several functional domains have been identified in APPextra, and we focused on a possible interaction between apoA-1 and the pathologically important Abeta peptide, because APPextra contains the nontransmembrane domain of Abeta. The binding between apoA-I and Abeta was saturable (K(d) = 6 nM), specific, and reversible. APPextra also competed with apoA-I for binding to Abeta. Direct evidence for this interaction was obtained by the formation of an SDS-resistant Abeta-apoA-I complex in polyacrylamide gels. Competitive experiments with apolipoprotein E (isoforms E2 and E4) showed that apoA-I had a higher binding affinity for Abeta. We also found that apoA-I inhibited the beta-sheet formation of Abeta with a mean inhibitory concentration close to that of alpha2-macroglobulin. Finally, we demonstrated that apoA-I attenuated Abeta-induced cytotoxicity. These results suggest apoA-I binds to at least one extracellular domain of APP and has a functional role in controlling Abeta aggregation and toxicity."xsd:string |
| http://purl.uniprot.org/citations/11297421 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi002186k"xsd:string |
| http://purl.uniprot.org/citations/11297421 | http://purl.uniprot.org/core/author | "Lazo J.S."xsd:string |
| http://purl.uniprot.org/citations/11297421 | http://purl.uniprot.org/core/author | "Lefterova M.I."xsd:string |
| http://purl.uniprot.org/citations/11297421 | http://purl.uniprot.org/core/author | "Koldamova R.P."xsd:string |
| http://purl.uniprot.org/citations/11297421 | http://purl.uniprot.org/core/author | "Lefterov I.M."xsd:string |
| http://purl.uniprot.org/citations/11297421 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11297421 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/11297421 | http://purl.uniprot.org/core/pages | "3553-3560"xsd:string |
| http://purl.uniprot.org/citations/11297421 | http://purl.uniprot.org/core/title | "Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity."xsd:string |
| http://purl.uniprot.org/citations/11297421 | http://purl.uniprot.org/core/volume | "40"xsd:string |
| http://purl.uniprot.org/citations/11297421 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11297421 |
| http://purl.uniprot.org/citations/11297421 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11297421 |
| http://purl.uniprot.org/uniprot/P02647#attribution-A2D85BBACDC4C882BFC0F830B743243B | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/11297421 |
| http://purl.uniprot.org/uniprot/#_P02647-mappedCitation-11297421 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11297421 |
| http://purl.uniprot.org/uniprot/#_P05067-mappedCitation-11297421 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11297421 |
| http://purl.uniprot.org/uniprot/P05067 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11297421 |
| http://purl.uniprot.org/uniprot/P02647 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11297421 |