| pubmed-article:8289821 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C0243044 | lld:lifeskim |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C1825534 | lld:lifeskim |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:8289821 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:8289821 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8289821 | pubmed:dateCreated | 1994-2-24 | lld:pubmed |
| pubmed-article:8289821 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:8289821 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8289821 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8289821 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8289821 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8289821 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8289821 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:8289821 | pubmed:author | pubmed-author:SuzukiKK | lld:pubmed |
| pubmed-article:8289821 | pubmed:author | pubmed-author:KawasakiHH | lld:pubmed |
| pubmed-article:8289821 | pubmed:author | pubmed-author:KimuraYY | lld:pubmed |
| pubmed-article:8289821 | pubmed:author | pubmed-author:YaharaII | lld:pubmed |
| pubmed-article:8289821 | pubmed:author | pubmed-author:MinamiYY | lld:pubmed |
| pubmed-article:8289821 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8289821 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:8289821 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8289821 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8289821 | pubmed:pagination | 1459-64 | lld:pubmed |
| pubmed-article:8289821 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8289821 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8289821 | pubmed:articleTitle | The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. | lld:pubmed |
| pubmed-article:8289821 | pubmed:affiliation | Department of Cell Biology, Tokyo Metropolitan Institute of Medical Science, Japan. | lld:pubmed |
| pubmed-article:8289821 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8289821 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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