| http://purl.uniprot.org/citations/8289821 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8289821 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8289821 | http://www.w3.org/2000/01/rdf-schema#comment | "The majority of mouse HSP90 exists as alpha-alpha and beta-beta homodimers. Truncation of the 15-kDa carboxy-terminal region of mouse HSP90 by digestion with the Ca(2+)-dependent protease m-calpain caused dissociation of the dimer. When expressed in a reticulocyte lysate, the full-length human HSP90 alpha formed a dimeric form. A plasmid harboring human HSP90 alpha cDNA was constructed so that the carboxy-terminal 49 amino acid residues were removed when translated in vitro. This carboxy-terminally truncated human HSP90 alpha was found to exist as a monomer. In contrast, loss of the 118 amino acid residues from the amino terminus of human HSP90 alpha did not affect its in vitro dimerization. Introduction of an expression plasmid harboring the full-length human HSP90 alpha complements the lethality caused by the double mutations of two HSP90-related genes, hsp82 and hsc82, in a haploid strain of Saccharomyces cerevisiae. The carboxy-terminally truncated human HSP90 alpha neither formed dimers in yeast cells nor rescued the lethal double mutant."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.14.2.1459-1464.1994"xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.14.2.1459-1464.1994"xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/author | "Kimura Y."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/author | "Kimura Y."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/author | "Minami Y."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/author | "Minami Y."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/author | "Suzuki K."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/author | "Suzuki K."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/author | "Yahara I."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/author | "Yahara I."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/author | "Kawasaki H."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/author | "Kawasaki H."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/name | "Mol. Cell. Biol."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/pages | "1459-1464"xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/pages | "1459-1464"xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/title | "The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/title | "The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo."xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/volume | "14"xsd:string |
| http://purl.uniprot.org/citations/8289821 | http://purl.uniprot.org/core/volume | "14"xsd:string |