| pubmed-article:14645047 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14645047 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
| pubmed-article:14645047 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:14645047 | lifeskim:mentions | umls-concept:C0162847 | lld:lifeskim |
| pubmed-article:14645047 | lifeskim:mentions | umls-concept:C0332621 | lld:lifeskim |
| pubmed-article:14645047 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:14645047 | lifeskim:mentions | umls-concept:C0679932 | lld:lifeskim |
| pubmed-article:14645047 | lifeskim:mentions | umls-concept:C0679083 | lld:lifeskim |
| pubmed-article:14645047 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:14645047 | pubmed:dateCreated | 2003-12-3 | lld:pubmed |
| pubmed-article:14645047 | pubmed:abstractText | The living cell is inherently crowded with proteins and macromolecules. To avoid aggregation of denatured proteins in the living cell, molecular chaperones play important roles. Here we introduce a simple model to describe crowded protein solutions with chaperone-like species based on a dynamic density functional theory. As predicted by others, our simulations show that macromolecular crowding enhances the association of proteins and chaperones. However, when the intrinsic folding rate of the protein is slow, it is possible that crowding also enhances aggregation of proteins. The results of simulation suggest that, when the concentration of the crowding agent is as high as that in the cell, the association of the protein and unbound chaperone becomes correlated with the aggregation process, and that the protein-bound chaperones efficiently destroy the potential nuclei of aggregates and thus prevent the aggregation. | lld:pubmed |
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| pubmed-article:14645047 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14645047 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14645047 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14645047 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14645047 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14645047 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14645047 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14645047 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14645047 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14645047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14645047 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14645047 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14645047 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:14645047 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:14645047 | pubmed:author | pubmed-author:TakadaShojiS | lld:pubmed |
| pubmed-article:14645047 | pubmed:author | pubmed-author:KinjoAkira... | lld:pubmed |
| pubmed-article:14645047 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14645047 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:14645047 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14645047 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14645047 | pubmed:pagination | 3521-31 | lld:pubmed |
| pubmed-article:14645047 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:meshHeading | pubmed-meshheading:14645047... | lld:pubmed |
| pubmed-article:14645047 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14645047 | pubmed:articleTitle | Competition between protein folding and aggregation with molecular chaperones in crowded solutions: insight from mesoscopic simulations. | lld:pubmed |
| pubmed-article:14645047 | pubmed:affiliation | PRESTO, Japan Science and Technology Corporation, Kobe University, Kobe, Japan. | lld:pubmed |
| pubmed-article:14645047 | pubmed:publicationType | Journal Article | lld:pubmed |
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