pubmed-article:18643017 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18643017 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
pubmed-article:18643017 | lifeskim:mentions | umls-concept:C1511997 | lld:lifeskim |
pubmed-article:18643017 | lifeskim:mentions | umls-concept:C0301630 | lld:lifeskim |
pubmed-article:18643017 | lifeskim:mentions | umls-concept:C0443221 | lld:lifeskim |
pubmed-article:18643017 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
pubmed-article:18643017 | pubmed:issue | 5 Pt 1 | lld:pubmed |
pubmed-article:18643017 | pubmed:dateCreated | 2008-7-22 | lld:pubmed |
pubmed-article:18643017 | pubmed:abstractText | Recent single-molecule experiments found that the thioredoxin-catalyzed reduction of individual disulfide bonds placed under a stretching mechanical force has distinct characteristics: the reduction rate of human thioredoxin monotonically decreases with the force, while the rate of E. coli thioredoxin first decreases and then increases as the force goes beyond a certain threshold. In this work, we present a force-dependent two-pathway four-state model to uniformly quantify these intriguing observations. Although our model is indistinguishable from the previous two-pathway three-state model in predicting the mean reduction rate, the distributions of dwell times of the two models are significantly distinctive. The very recent experiment favors our model. | lld:pubmed |
pubmed-article:18643017 | pubmed:language | eng | lld:pubmed |
pubmed-article:18643017 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18643017 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18643017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18643017 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18643017 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18643017 | pubmed:month | May | lld:pubmed |
pubmed-article:18643017 | pubmed:issn | 1539-3755 | lld:pubmed |
pubmed-article:18643017 | pubmed:author | pubmed-author:CoxP NPN | lld:pubmed |
pubmed-article:18643017 | pubmed:author | pubmed-author:Ou-YangZhong-... | lld:pubmed |
pubmed-article:18643017 | pubmed:author | pubmed-author:XueXiaochuanX | lld:pubmed |
pubmed-article:18643017 | pubmed:author | pubmed-author:GongLinchenL | lld:pubmed |
pubmed-article:18643017 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18643017 | pubmed:volume | 77 | lld:pubmed |
pubmed-article:18643017 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18643017 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18643017 | pubmed:pagination | 050903 | lld:pubmed |
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pubmed-article:18643017 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18643017 | pubmed:articleTitle | Two-pathway four-state kinetic model of thioredoxin-catalyzed reduction of single forced disulfide bonds. | lld:pubmed |
pubmed-article:18643017 | pubmed:affiliation | Center for Advanced Study, Tsinghua University, Beijing 100084, China. | lld:pubmed |
pubmed-article:18643017 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18643017 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:948289 | entrezgene:pubmed | pubmed-article:18643017 | lld:entrezgene |