pubmed-article:9187656 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C0243044 | lld:lifeskim |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C1825534 | lld:lifeskim |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C0175721 | lld:lifeskim |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:9187656 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:9187656 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:9187656 | pubmed:dateCreated | 1997-7-14 | lld:pubmed |
pubmed-article:9187656 | pubmed:abstractText | Hsp90 is a highly specific chaperone for many signal transduction proteins, including steroid hormone receptors and a broad range of protein kinases. The crystal structure of the N-terminal domain of the yeast Hsp90 reveals a dimeric structure based on a highly twisted sixteen stranded beta-sheet, whose topology suggests a possible 30-domain-swapped structure for the intact Hsp90 dimer. The opposing faces of the beta-sheets in the dimer define a potential peptide-binding cleft, suggesting that the N-domain may serve as a molecular 'clamp' in the binding of ligand proteins to Hsp90. | lld:pubmed |
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pubmed-article:9187656 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9187656 | pubmed:language | eng | lld:pubmed |
pubmed-article:9187656 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9187656 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9187656 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9187656 | pubmed:month | Jun | lld:pubmed |
pubmed-article:9187656 | pubmed:issn | 1072-8368 | lld:pubmed |
pubmed-article:9187656 | pubmed:author | pubmed-author:PiperP WPW | lld:pubmed |
pubmed-article:9187656 | pubmed:author | pubmed-author:PearlL HLH | lld:pubmed |
pubmed-article:9187656 | pubmed:author | pubmed-author:ProdromouCC | lld:pubmed |
pubmed-article:9187656 | pubmed:author | pubmed-author:RoeS MSM | lld:pubmed |
pubmed-article:9187656 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9187656 | pubmed:volume | 4 | lld:pubmed |
pubmed-article:9187656 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9187656 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9187656 | pubmed:pagination | 477-82 | lld:pubmed |
pubmed-article:9187656 | pubmed:dateRevised | 2009-9-29 | lld:pubmed |
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pubmed-article:9187656 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9187656 | pubmed:articleTitle | A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. | lld:pubmed |
pubmed-article:9187656 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, University College London, UK. | lld:pubmed |
pubmed-article:9187656 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9187656 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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