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http://purl.uniprot.org/citations/9827555http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9827555http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9827555http://www.w3.org/2000/01/rdf-schema#comment"Members of the Hsp100/Clp-family of molecular chaperones form regulatory subunits of ATP-dependent Clp proteases and fulfill crucial roles for cellular thermotolerance. We have identified a Clp-like protein in Saccharomyces cerevisiae, Mcx1p, which shares approximately 30% sequence identity with ClpX-proteins in bacteria, plants and nematodes. Mcx1p localizes to the matrix space of mitochondria and is peripherally associated with the inner membrane. A homologue of E. coli ClpP protease was not identified when screening the yeast genome. We therefore propose that Mcx1p represents a novel molecular chaperone of mitochondria with non-proteolytic function."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)01310-6"xsd:string
http://purl.uniprot.org/citations/9827555http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(98)01310-6"xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/author"van Dyck L."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/author"van Dyck L."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/author"Langer T."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/author"Langer T."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/author"Neupert W."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/author"Neupert W."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/author"Dembowski M."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/author"Dembowski M."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/pages"250-254"xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/pages"250-254"xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/title"Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/title"Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/volume"438"xsd:string
http://purl.uniprot.org/citations/9827555http://purl.uniprot.org/core/volume"438"xsd:string
http://purl.uniprot.org/citations/9827555http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9827555
http://purl.uniprot.org/citations/9827555http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9827555