| pubmed-article:10547062 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10547062 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:10547062 | lifeskim:mentions | umls-concept:C0242606 | lld:lifeskim |
| pubmed-article:10547062 | lifeskim:mentions | umls-concept:C0008266 | lld:lifeskim |
| pubmed-article:10547062 | lifeskim:mentions | umls-concept:C1564779 | lld:lifeskim |
| pubmed-article:10547062 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:10547062 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10547062 | pubmed:dateCreated | 1999-11-19 | lld:pubmed |
| pubmed-article:10547062 | pubmed:abstractText | The nuclear-encoded chloroplast-localized Hsp21 is an oligomeric heat shock protein (Hsp), belonging to the protein family of small Hsps and alpha-crystallins. We have investigated the effects of high temperature and oxidation treatments on the structural properties of Hsp21, both in purified recombinant form and in transgenic Arabidopsis thaliana plants engineered to constitutively overexpress Hsp21. A conformational change was observed for the 300 kDa oligomeric Hsp21 protein during moderate heat stress (< or =40 degrees C) of Arabidopsis plants, as judged by a shift to lower mobility in non-denaturing electrophoresis. Similar changes in mobility were observed when purified recombinant Hsp21 protein was subjected to an oxidant. Exposure of Hsp21 protein to temperatures above 70 degrees C led to irreversible aggregation, which was prevented in presence of the reductant dithiothreitol. The transgenic plants that constitutively overexpressed Hsp21 were more resistant to heat stress than were wildtype plants when the heat stress was imposed under high light conditions. These results suggest that the physiological role of Hsp21 involves a response to temperature-dependent oxidative stress. | lld:pubmed |
| pubmed-article:10547062 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10547062 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10547062 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10547062 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10547062 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10547062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10547062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10547062 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10547062 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10547062 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10547062 | pubmed:issn | 1355-8145 | lld:pubmed |
| pubmed-article:10547062 | pubmed:author | pubmed-author:VierlingEE | lld:pubmed |
| pubmed-article:10547062 | pubmed:author | pubmed-author:OsteryoungK... | lld:pubmed |
| pubmed-article:10547062 | pubmed:author | pubmed-author:SundbyCC | lld:pubmed |
| pubmed-article:10547062 | pubmed:author | pubmed-author:HahmP CPC | lld:pubmed |
| pubmed-article:10547062 | pubmed:author | pubmed-author:HärndahlUU | lld:pubmed |
| pubmed-article:10547062 | pubmed:author | pubmed-author:BornmanJ FJF | lld:pubmed |
| pubmed-article:10547062 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10547062 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:10547062 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10547062 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10547062 | pubmed:pagination | 129-38 | lld:pubmed |
| pubmed-article:10547062 | pubmed:dateRevised | 2008-11-20 | lld:pubmed |
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| pubmed-article:10547062 | pubmed:meshHeading | pubmed-meshheading:10547062... | lld:pubmed |
| pubmed-article:10547062 | pubmed:meshHeading | pubmed-meshheading:10547062... | lld:pubmed |
| pubmed-article:10547062 | pubmed:meshHeading | pubmed-meshheading:10547062... | lld:pubmed |
| pubmed-article:10547062 | pubmed:meshHeading | pubmed-meshheading:10547062... | lld:pubmed |
| pubmed-article:10547062 | pubmed:meshHeading | pubmed-meshheading:10547062... | lld:pubmed |
| pubmed-article:10547062 | pubmed:meshHeading | pubmed-meshheading:10547062... | lld:pubmed |
| pubmed-article:10547062 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10547062 | pubmed:articleTitle | The chloroplast small heat shock protein undergoes oxidation-dependent conformational changes and may protect plants from oxidative stress. | lld:pubmed |
| pubmed-article:10547062 | pubmed:affiliation | Department of Biochemistry, University of Lund, Sweden. | lld:pubmed |
| pubmed-article:10547062 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10547062 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10547062 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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