| pubmed-article:17567739 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17567739 | lifeskim:mentions | umls-concept:C0220806 | lld:lifeskim |
| pubmed-article:17567739 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:17567739 | lifeskim:mentions | umls-concept:C0008266 | lld:lifeskim |
| pubmed-article:17567739 | lifeskim:mentions | umls-concept:C0008855 | lld:lifeskim |
| pubmed-article:17567739 | lifeskim:mentions | umls-concept:C1564779 | lld:lifeskim |
| pubmed-article:17567739 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:17567739 | lifeskim:mentions | umls-concept:C0392752 | lld:lifeskim |
| pubmed-article:17567739 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:17567739 | pubmed:dateCreated | 2007-6-25 | lld:pubmed |
| pubmed-article:17567739 | pubmed:abstractText | The molecular mechanism whereby the small heat-shock protein (sHsp) chaperones interact with and prevent aggregation of other proteins is not fully understood. We have characterized the sHsp-substrate protein interaction at normal and increased temperatures utilizing a model substrate protein, citrate synthase (CS), widely used in chaperone assays, and a dodecameric plant sHsp, Hsp21, by chemical cross-linking with 3,3'-Dithiobis[sulfosuccinimidylpropionate] (DTSSP) and mass spectrometric peptide mapping. In the absence of CS, the cross-linker captured Hsp21 in dodecameric form, even at increased temperature (47 degrees C). In the presence of equimolar amounts of CS, no Hsp21 dodecamer was captured, indicating a substrate-induced Hsp21 dodecamer dissociation by equimolar amounts of CS. Cross-linked Hsp21-Hsp21 dipeptides indicated an exposure of the Hsp21 C-terminal tails and substrate-binding sites normally covered by the C terminus. Cross-linked Hsp21-CS dipeptides mapped to several sites on the surface of the CS dimer, indicating that there are numerous weak and short-lived interactions between Hsp21 and CS, even at normal temperatures. The N-terminal arms especially interacted with a motif in the CS dimer, which is absent in thermostable forms of CS. The cross-linking data suggest that the presence of substrate rather than temperature influences the conformation of Hsp21. | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17567739 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17567739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17567739 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17567739 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:17567739 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:17567739 | pubmed:author | pubmed-author:AquilinaJ... | lld:pubmed |
| pubmed-article:17567739 | pubmed:author | pubmed-author:RobinsonCarol... | lld:pubmed |
| pubmed-article:17567739 | pubmed:author | pubmed-author:AhrmanEmmaE | lld:pubmed |
| pubmed-article:17567739 | pubmed:author | pubmed-author:LambertWietsk... | lld:pubmed |
| pubmed-article:17567739 | pubmed:author | pubmed-author:EmanuelssonCe... | lld:pubmed |
| pubmed-article:17567739 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17567739 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:17567739 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17567739 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17567739 | pubmed:pagination | 1464-78 | lld:pubmed |
| pubmed-article:17567739 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:meshHeading | pubmed-meshheading:17567739... | lld:pubmed |
| pubmed-article:17567739 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17567739 | pubmed:articleTitle | Chemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthase. | lld:pubmed |
