| pubmed-article:14501945 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14501945 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:14501945 | lifeskim:mentions | umls-concept:C1956015 | lld:lifeskim |
| pubmed-article:14501945 | lifeskim:mentions | umls-concept:C0243043 | lld:lifeskim |
| pubmed-article:14501945 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:14501945 | pubmed:dateCreated | 2003-9-22 | lld:pubmed |
| pubmed-article:14501945 | pubmed:abstractText | The expression of heat shock or stress proteins (hsps) is a widespread response to stress that results in the protection of cells from subsequent insults, coined stress tolerance. Stress tolerance is apparently due to the preservation of several cellular structures and processes, such as translation. Protection of protein synthesis has been correlated with the presence of Hsp70. In the present study, Hsp70 was found to interact with translating ribosomes. This interaction is due to the preferential binding of Hsp70 to the 40S ribosomal subunit. Additionally, Hsp70 seems to interact weakly with nascent polypeptides within the 60S subunit. The interaction between Hsp70 and ribosomal subunits could also be observed in vitro conditions. Binding of Hsp70 to ribosomes was salt resistant, suggesting that this protein is not bound to transiently associated translational factors. Moreover, protection of protein synthesis requires new gene expression. We speculate that the binding of Hsp70 to ribosomes is part of a mechanism to guarantee the rapid and abundant protein synthesis during stress, particularly the translation of mRNAs encoding for hsps. | lld:pubmed |
| pubmed-article:14501945 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14501945 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14501945 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14501945 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14501945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14501945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14501945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14501945 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14501945 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:14501945 | pubmed:issn | 1073-2322 | lld:pubmed |
| pubmed-article:14501945 | pubmed:author | pubmed-author:CornivelliLiz... | lld:pubmed |
| pubmed-article:14501945 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:14501945 | pubmed:author | pubmed-author:ZeidanQuiraQ | lld:pubmed |
| pubmed-article:14501945 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14501945 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:14501945 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14501945 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14501945 | pubmed:pagination | 320-5 | lld:pubmed |
| pubmed-article:14501945 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:meshHeading | pubmed-meshheading:14501945... | lld:pubmed |
| pubmed-article:14501945 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14501945 | pubmed:articleTitle | HSP70 interacts with ribosomal subunits of thermotolerant cells. | lld:pubmed |
| pubmed-article:14501945 | pubmed:affiliation | Department of Physiology, Johns Hopkins Medical School, Baltimore, Maryland 21205, USA. | lld:pubmed |
| pubmed-article:14501945 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14501945 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:14501945 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14501945 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
