| http://purl.uniprot.org/citations/7890674 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7890674 | http://www.w3.org/2000/01/rdf-schema#comment | "The tumor suppressor APC protein associates with the cadherin-binding proteins alpha- and beta-catenin. To examine the relationship between cadherin, catenins, and APC, we have tested combinatorial protein-protein interactions in vivo, using a yeast two-hybrid system, and in vitro, using purified proteins. beta-Catenin directly binds to APC at high and low affinity sites. alpha-Catenin cannot directly bind APC but associates with it by binding to beta-catenin. Plakoglobin, also known as gamma-catenin, directly binds to both APC and alpha-catenin and also to the APC-beta-catenin complex, but not directly to beta-catenin. beta-Catenin binds to multiple independent regions of APC, some of which include a previously identified consensus motif and others which contain the centrally located 20 amino acid repeat sequences. The APC binding site on beta-catenin may be discontinuous since neither the carboxyl-nor amino-terminal halves of beta-catenin will independently associate with APC, although the amino-terminal half independently binds alpha-catenin. The catenins bind to APC and E-cadherin in a similar fashion, but APC and E-cadherin do not associate with each other either in the presence or absence of catenins. Thus, APC forms distinct heteromeric complexes containing combinations of alpha-catenin, beta-catenin, and plakoglobin which are independent from the cadherin-catenin complexes."xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.270.10.5549"xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://purl.uniprot.org/core/author | "Souza B."xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://purl.uniprot.org/core/author | "Albert I."xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://purl.uniprot.org/core/author | "Munemitsu S."xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://purl.uniprot.org/core/author | "Polakis P."xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://purl.uniprot.org/core/author | "Rubinfeld B."xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7890674 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://purl.uniprot.org/core/pages | "5549-5555"xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://purl.uniprot.org/core/title | "The APC protein and E-cadherin form similar but independent complexes with alpha-catenin, beta-catenin, and plakoglobin."xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://purl.uniprot.org/core/volume | "270"xsd:string |
| http://purl.uniprot.org/citations/7890674 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7890674 |
| http://purl.uniprot.org/citations/7890674 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7890674 |
| http://purl.uniprot.org/uniprot/P25054#attribution-5CBBB06EE3EF56AD22CDF4108D823C90 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7890674 |
| http://purl.uniprot.org/uniprot/P35222#attribution-5CBBB06EE3EF56AD22CDF4108D823C90 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7890674 |
| http://purl.uniprot.org/uniprot/P35221#attribution-5CBBB06EE3EF56AD22CDF4108D823C90 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7890674 |
| http://purl.uniprot.org/uniprot/P14923#attribution-5CBBB06EE3EF56AD22CDF4108D823C90 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7890674 |