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http://purl.uniprot.org/citations/11809970http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11809970http://www.w3.org/2000/01/rdf-schema#comment"The organization of myosin into motile cellular structures requires precise temporal and spatial regulation. Proteins containing a UCS (UNC-45/CRO1/She4p) domain are necessary for the incorporation of myosin into the contractile ring during cytokinesis and into thick filaments during muscle development. We report that the carboxyl-terminal regions of UNC-45 bound and exerted chaperone activity on the myosin head. The amino-terminal tetratricopeptide repeat domain of UNC-45 bound the molecular chaperone Hsp90. Thus, UNC-45 functions both as a molecular chaperone and as an Hsp90 co-chaperone for myosin, which can explain previous findings of altered assembly and decreased accumulation of myosin in UNC-45 mutants of Caenorhabditis elegans."xsd:string
http://purl.uniprot.org/citations/11809970http://purl.org/dc/terms/identifier"doi:10.1126/science.1066648"xsd:string
http://purl.uniprot.org/citations/11809970http://purl.uniprot.org/core/author"Hartl F.U."xsd:string
http://purl.uniprot.org/citations/11809970http://purl.uniprot.org/core/author"Barral J.M."xsd:string
http://purl.uniprot.org/citations/11809970http://purl.uniprot.org/core/author"Epstein H.F."xsd:string
http://purl.uniprot.org/citations/11809970http://purl.uniprot.org/core/author"Hutagalung A.H."xsd:string
http://purl.uniprot.org/citations/11809970http://purl.uniprot.org/core/author"Brinker A."xsd:string
http://purl.uniprot.org/citations/11809970http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11809970http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/11809970http://purl.uniprot.org/core/pages"669-671"xsd:string
http://purl.uniprot.org/citations/11809970http://purl.uniprot.org/core/title"Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin."xsd:string
http://purl.uniprot.org/citations/11809970http://purl.uniprot.org/core/volume"295"xsd:string
http://purl.uniprot.org/citations/11809970http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11809970
http://purl.uniprot.org/citations/11809970http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11809970
http://purl.uniprot.org/uniprot/#_G5EG62-mappedCitation-11809970http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11809970
http://purl.uniprot.org/uniprot/#_Q18688-mappedCitation-11809970http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11809970
http://purl.uniprot.org/uniprot/#_P02566-mappedCitation-11809970http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11809970
http://purl.uniprot.org/uniprot/P02566http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11809970
http://purl.uniprot.org/uniprot/Q18688http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11809970
http://purl.uniprot.org/uniprot/G5EG62http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11809970