http://purl.uniprot.org/citations/20036665 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20036665 | http://www.w3.org/2000/01/rdf-schema#comment | "The neural adaptor protein FE65 interacts with the amyloid beta-protein precursor (APP). In osmotically stressed cells, the membrane APP-tethered FE65 is released into the cytoplasm and translocates to the nuclear matrix, where it stabilizes p53 via a non-canonical pathway. In this study, we found that the second phosphotyrosine interaction domain (PI2) of FE65 mediated its trans-accumulation in the nuclear matrix of osmotically stressed cells. The carboxyl-terminal half of FE65, which contains the PI2 domain, failed to stabilize p53, suggesting that the amino-terminal half of the protein plays an important role in the stabilization of p53 in osmotically stressed cells."xsd:string |
http://purl.uniprot.org/citations/20036665 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.febslet.2009.12.040"xsd:string |
http://purl.uniprot.org/citations/20036665 | http://purl.uniprot.org/core/author | "Kawai T."xsd:string |
http://purl.uniprot.org/citations/20036665 | http://purl.uniprot.org/core/author | "Nakaya T."xsd:string |
http://purl.uniprot.org/citations/20036665 | http://purl.uniprot.org/core/author | "Suzuki T."xsd:string |
http://purl.uniprot.org/citations/20036665 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20036665 | http://purl.uniprot.org/core/name | "FEBS Lett"xsd:string |
http://purl.uniprot.org/citations/20036665 | http://purl.uniprot.org/core/pages | "765-769"xsd:string |
http://purl.uniprot.org/citations/20036665 | http://purl.uniprot.org/core/title | "Roles of the intramolecular regions of FE65 in its trans-accumulation and in p53 stabilization in the nuclear matrix of osmotically stressed cells."xsd:string |
http://purl.uniprot.org/citations/20036665 | http://purl.uniprot.org/core/volume | "584"xsd:string |
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