pubmed-article:7957962 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7957962 | lifeskim:mentions | umls-concept:C0178539 | lld:lifeskim |
pubmed-article:7957962 | lifeskim:mentions | umls-concept:C0002202 | lld:lifeskim |
pubmed-article:7957962 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:7957962 | pubmed:dateCreated | 1994-12-21 | lld:pubmed |
pubmed-article:7957962 | pubmed:abstractText | The bovine eye lens protein alpha A-crystallin has been overexpressed both by stable transfection of HeLa cells and by transient transfection of NIH 3T3 cells. In both experimental systems alpha A-crystallin overexpression results in an increased cellular thermoresistance as judged by different clonal survival assays. In contrast, similar overexpression of another stable lens protein, beta B2-crystallin, does not confer thermoresistance. These results indicate that the structural relationship of alpha A-crystallin to the small heat shock proteins HSP25/27 and to alpha B-crystallin is sufficient for the shared thermoprotective function of all of these molecules and strongly suggests that the chaperone-like properties that they have in common are responsible for the conferred cellular thermoresistance. | lld:pubmed |
pubmed-article:7957962 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7957962 | pubmed:language | eng | lld:pubmed |
pubmed-article:7957962 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7957962 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7957962 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7957962 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7957962 | pubmed:month | Nov | lld:pubmed |
pubmed-article:7957962 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:7957962 | pubmed:author | pubmed-author:de JongW WWW | lld:pubmed |
pubmed-article:7957962 | pubmed:author | pubmed-author:GaestelMM | lld:pubmed |
pubmed-article:7957962 | pubmed:author | pubmed-author:KnaufUU | lld:pubmed |
pubmed-article:7957962 | pubmed:author | pubmed-author:van den... | lld:pubmed |
pubmed-article:7957962 | pubmed:author | pubmed-author:OverkampPP | lld:pubmed |
pubmed-article:7957962 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7957962 | pubmed:day | 21 | lld:pubmed |
pubmed-article:7957962 | pubmed:volume | 355 | lld:pubmed |
pubmed-article:7957962 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7957962 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7957962 | pubmed:pagination | 54-6 | lld:pubmed |
pubmed-article:7957962 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:7957962 | pubmed:meshHeading | pubmed-meshheading:7957962-... | lld:pubmed |
pubmed-article:7957962 | pubmed:meshHeading | pubmed-meshheading:7957962-... | lld:pubmed |
pubmed-article:7957962 | pubmed:meshHeading | pubmed-meshheading:7957962-... | lld:pubmed |
pubmed-article:7957962 | pubmed:meshHeading | pubmed-meshheading:7957962-... | lld:pubmed |
pubmed-article:7957962 | pubmed:meshHeading | pubmed-meshheading:7957962-... | lld:pubmed |
pubmed-article:7957962 | pubmed:meshHeading | pubmed-meshheading:7957962-... | lld:pubmed |
pubmed-article:7957962 | pubmed:meshHeading | pubmed-meshheading:7957962-... | lld:pubmed |
pubmed-article:7957962 | pubmed:meshHeading | pubmed-meshheading:7957962-... | lld:pubmed |
pubmed-article:7957962 | pubmed:meshHeading | pubmed-meshheading:7957962-... | lld:pubmed |
pubmed-article:7957962 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7957962 | pubmed:articleTitle | Alpha A-crystallin confers cellular thermoresistance. | lld:pubmed |
pubmed-article:7957962 | pubmed:affiliation | Department of Biochemistry, University of Nijmegen, The Netherlands. | lld:pubmed |
pubmed-article:7957962 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7957962 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7957962 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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