| pubmed-article:8016869 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8016869 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8016869 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
| pubmed-article:8016869 | lifeskim:mentions | umls-concept:C0243043 | lld:lifeskim |
| pubmed-article:8016869 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:8016869 | lifeskim:mentions | umls-concept:C0182953 | lld:lifeskim |
| pubmed-article:8016869 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8016869 | pubmed:dateCreated | 1994-7-22 | lld:pubmed |
| pubmed-article:8016869 | pubmed:abstractText | The folding of proteins and the assembly of protein complexes within subcompartments of the eukaryotic cell is catalysed by different members of the Hsp70 protein family. The chaperone function of Hsp70 proteins in these events is regulated by members of the DnaJ-like protein family, which occurs through direct interaction of different Hsp70 and DnaJ-like protein pairs that appear to be specifically adapted to each other. This review highlights the diversity of functions of DnaJ-like proteins by using specific examples of DnaJ-Hsp70 interactions with polypeptides in yeast protein-biogenesis pathways. | lld:pubmed |
| pubmed-article:8016869 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8016869 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8016869 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8016869 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8016869 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8016869 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8016869 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8016869 | pubmed:issn | 0968-0004 | lld:pubmed |
| pubmed-article:8016869 | pubmed:author | pubmed-author:DouglasM GMG | lld:pubmed |
| pubmed-article:8016869 | pubmed:author | pubmed-author:LangerTT | lld:pubmed |
| pubmed-article:8016869 | pubmed:author | pubmed-author:LoNN | lld:pubmed |
| pubmed-article:8016869 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8016869 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:8016869 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8016869 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8016869 | pubmed:pagination | 176-81 | lld:pubmed |
| pubmed-article:8016869 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:8016869 | pubmed:meshHeading | pubmed-meshheading:8016869-... | lld:pubmed |
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| pubmed-article:8016869 | pubmed:meshHeading | pubmed-meshheading:8016869-... | lld:pubmed |
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| pubmed-article:8016869 | pubmed:meshHeading | pubmed-meshheading:8016869-... | lld:pubmed |
| pubmed-article:8016869 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8016869 | pubmed:articleTitle | DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. | lld:pubmed |
| pubmed-article:8016869 | pubmed:affiliation | Institute of Physiolological Chemistry, University of Munich, Germany. | lld:pubmed |
| pubmed-article:8016869 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8016869 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8016869 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:8016869 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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