RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/15498567http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15498567http://www.w3.org/2000/01/rdf-schema#comment"Here, we produced the C-terminal truncation variants of mouse inducible heat shock protein 72 (Hsp72) to elucidate the regulatory role of the C-terminal helical lid of Hsp70 for substrate recognition. All of the truncation variants containing the substrate binding domain bound a short-length peptide substrate CLLLSAPRR. When a large mass reduced carboxymethyl alpha-lactalbumin (RCMLA) as a substrate was used in gel filtration experiment, we observed the complex formation only for the truncation variants containing the long alpha-helix C in the helical lid. However, RCMLA binding occurred even for the variants lacking alpha-helix C when their C-terminal region was anchored onto a solid phase. Together with the finding that helix C is involved in the self-association of Hsp70, our present data suggest that the C-terminal region of Hsp70 modulates the substrate recognition and its kinetics may be substrate-mass dependent."xsd:string
http://purl.uniprot.org/citations/15498567http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2004.09.044"xsd:string
http://purl.uniprot.org/citations/15498567http://purl.uniprot.org/core/author"Ohno M."xsd:string
http://purl.uniprot.org/citations/15498567http://purl.uniprot.org/core/author"Tani F."xsd:string
http://purl.uniprot.org/citations/15498567http://purl.uniprot.org/core/author"Kitabatake N."xsd:string
http://purl.uniprot.org/citations/15498567http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15498567http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/15498567http://purl.uniprot.org/core/pages"381-386"xsd:string
http://purl.uniprot.org/citations/15498567http://purl.uniprot.org/core/title"Role of the C-terminal region of mouse inducible Hsp72 in the recognition of peptide substrate for chaperone activity."xsd:string
http://purl.uniprot.org/citations/15498567http://purl.uniprot.org/core/volume"576"xsd:string
http://purl.uniprot.org/citations/15498567http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15498567
http://purl.uniprot.org/citations/15498567http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15498567
http://purl.uniprot.org/uniprot/#_A1E2B8-mappedCitation-15498567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/#_O88687-mappedCitation-15498567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/#_O88688-mappedCitation-15498567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/#_Q3TU85-mappedCitation-15498567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/#_P17156-mappedCitation-15498567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/#_Q3TAI8-mappedCitation-15498567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/#_Q61696-mappedCitation-15498567http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/O88688http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/O88687http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/Q61696http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/Q3TU85http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15498567
http://purl.uniprot.org/uniprot/Q3TAI8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15498567