| pubmed-article:8392074 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C0221920 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C0145779 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C0162326 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C0178555 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C0205438 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8392074 | lifeskim:mentions | umls-concept:C2744539 | lld:lifeskim |
| pubmed-article:8392074 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:8392074 | pubmed:dateCreated | 1993-8-12 | lld:pubmed |
| pubmed-article:8392074 | pubmed:abstractText | Activation of protein C by thrombin is stimulated by the endothelial cell cofactor thrombomodulin. The structural regions of thrombomodulin necessary for cofactor activity have been localized to the fourth through sixth epidermal growth factor (EGF)-like domains. The fourth EGF-like domain is unnecessary for high affinity thrombin binding, but is required for cofactor activity. To identify essential sequences within the fourth EGF-like domain, a series of recombinant human thrombomodulins consisting of EGF-like domains four through six were expressed in human kidney cells. These mutants contain replacements of disulfide loops within the fourth EGF-like domain, thereby conserving overall disulfide bond structure. All of the mutants bound to thrombin with high affinity, and inhibited the fibrinogen-clotting activity of thrombin to a similar extent. Two regions of the fourth EGF-like domain were identified to be essential for cofactor activity: 1) the sequence consisting of amino acids Glu-357, Tyr-358, and Gln-359 shared by the overlapping first and second disulfide loops, and 2) the amino-terminal region of the third disulfide loop containing amino acids Glu-374, Gly-375, and Phe-376. These results suggest that amino acids critical for thrombomodulin cofactor activity are located near the junction between the two subdomains of the fourth EGF-like domain. | lld:pubmed |
| pubmed-article:8392074 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8392074 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8392074 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8392074 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8392074 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8392074 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8392074 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8392074 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8392074 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8392074 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8392074 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8392074 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8392074 | pubmed:author | pubmed-author:ChenYY | lld:pubmed |
| pubmed-article:8392074 | pubmed:author | pubmed-author:SadlerJ EJE | lld:pubmed |
| pubmed-article:8392074 | pubmed:author | pubmed-author:LentzS RSR | lld:pubmed |
| pubmed-article:8392074 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8392074 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8392074 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8392074 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8392074 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8392074 | pubmed:pagination | 15312-7 | lld:pubmed |
| pubmed-article:8392074 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8392074 | pubmed:meshHeading | pubmed-meshheading:8392074-... | lld:pubmed |
| pubmed-article:8392074 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8392074 | pubmed:articleTitle | Sequences required for thrombomodulin cofactor activity within the fourth epidermal growth factor-like domain of human thrombomodulin. | lld:pubmed |
| pubmed-article:8392074 | pubmed:affiliation | Department of Internal Medicine, University of Iowa, Iowa City 52242. | lld:pubmed |
| pubmed-article:8392074 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8392074 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8392074 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8392074 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8392074 | lld:pubmed |
