| http://purl.uniprot.org/citations/25446099 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25446099 | http://www.w3.org/2000/01/rdf-schema#comment | "Huntington's disease is a polyglutamine expansion disorder, characterized by mutant HTT-mediated aggregate formation and cytotoxicity. Many reports suggests roles of N-terminal 17 amino acid domain of HTT (HTT-N17) towards subcellular localization, aggregate formation and subsequent pathogenicity induced by N-terminal HTT harboring polyQ stretch in pathogenic range. HYPK is a HTT-interacting chaperone which can reduce N-terminal mutant HTT-mediated aggregate formation and cytotoxicity in neuronal cell lines. However, how HYPK interacts with N-terminal fragment of HTT remained unknown. Here we report that specific interaction of HYPK with HTT-N17 is crucial for the chaperone activity of HYPK. Deletion of HTT-N17 leads to formation of tinier, SDS-soluble nuclear aggregates formed by N-terminal mutant HTT. The increased cytotoxicity imparted by these tiny aggregates might be contributed due to loss of interaction with HYPK."xsd:string |
| http://purl.uniprot.org/citations/25446099 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2014.11.035"xsd:string |
| http://purl.uniprot.org/citations/25446099 | http://purl.uniprot.org/core/author | "Choudhury K.R."xsd:string |
| http://purl.uniprot.org/citations/25446099 | http://purl.uniprot.org/core/author | "Bhattacharyya N.P."xsd:string |
| http://purl.uniprot.org/citations/25446099 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25446099 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/25446099 | http://purl.uniprot.org/core/pages | "66-73"xsd:string |
| http://purl.uniprot.org/citations/25446099 | http://purl.uniprot.org/core/title | "Chaperone protein HYPK interacts with the first 17 amino acid region of Huntingtin and modulates mutant HTT-mediated aggregation and cytotoxicity."xsd:string |
| http://purl.uniprot.org/citations/25446099 | http://purl.uniprot.org/core/volume | "456"xsd:string |
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