RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/14644449http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14644449http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14644449http://www.w3.org/2000/01/rdf-schema#comment"Hsp105alpha and Hsp105beta are mammalian members of the Hsp105/110 family, a diverged subgroup of the Hsp70 family. Here, we show that Hsp105alpha and Hsp105beta bind non-native protein through the beta-sheet domain and suppress the aggregation of heat-denatured protein in the presence of ADP rather than ATP. In contrast, Hsc70/Hsp40 suppressed the aggregation of heat-denatured protein in the presence of ATP rather than ADP. Furthermore, the overexpression of Hsp105alpha but not Hsp70 in COS-7 cells rescued the inactivation of luciferase caused by ATP depletion. Thus, Hsp105/110 family proteins are suggested to function as a substitute for Hsp70 family proteins to suppress the aggregation of denatured proteins in cells under severe stress, in which the cellular ATP level decreases markedly."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(03)01292-4"xsd:string
http://purl.uniprot.org/citations/14644449http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(03)01292-4"xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/author"Saito Y."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/author"Saito Y."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/author"Ishihara K."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/author"Ishihara K."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/author"Yamagishi N."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/author"Yamagishi N."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/author"Hatayama T."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/author"Hatayama T."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/pages"390-396"xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/pages"390-396"xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/title"Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/title"Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP."xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/volume"555"xsd:string
http://purl.uniprot.org/citations/14644449http://purl.uniprot.org/core/volume"555"xsd:string
http://purl.uniprot.org/citations/14644449http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14644449
http://purl.uniprot.org/citations/14644449http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14644449