| pubmed-article:10359597 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10359597 | lifeskim:mentions | umls-concept:C0021701 | lld:lifeskim |
| pubmed-article:10359597 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:10359597 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:10359597 | lifeskim:mentions | umls-concept:C2247060 | lld:lifeskim |
| pubmed-article:10359597 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:10359597 | lifeskim:mentions | umls-concept:C0301625 | lld:lifeskim |
| pubmed-article:10359597 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:10359597 | pubmed:dateCreated | 1999-7-29 | lld:pubmed |
| pubmed-article:10359597 | pubmed:abstractText | The rapid modulation of ligand-binding affinity ("activation") is a central property of the integrin family of cell adhesion receptors. The small GTP-binding protein Ras and its downstream effector kinase Raf-1 suppress integrin activation. In this study we explored the relationship between Ras and the closely related small GTP-binding protein R-Ras in modulating the integrin affinity state. We found that R-Ras does not seem to be a direct activator of integrins in Chinese hamster ovary cells. However, we observed that GTP-bound R-Ras strongly antagonizes the Ras/Raf-initiated integrin suppression pathway. Furthermore, this reversal of the Ras/Raf suppressor pathway does not seem to be via a competition between Ras and R-Ras for common downstream effectors or via an inhibition of Ras/Raf-induced MAP kinase activation. Thus, R-Ras and Ras may act in concert to regulate integrin affinity via the activation of distinct downstream effectors. | lld:pubmed |
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| pubmed-article:10359597 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10359597 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10359597 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10359597 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10359597 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10359597 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:10359597 | pubmed:author | pubmed-author:GinsbergM HMH | lld:pubmed |
| pubmed-article:10359597 | pubmed:author | pubmed-author:SethiTT | lld:pubmed |
| pubmed-article:10359597 | pubmed:author | pubmed-author:DownwardJJ | lld:pubmed |
| pubmed-article:10359597 | pubmed:author | pubmed-author:HughesP EPE | lld:pubmed |
| pubmed-article:10359597 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10359597 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:10359597 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10359597 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10359597 | pubmed:pagination | 1799-809 | lld:pubmed |
| pubmed-article:10359597 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:10359597 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10359597 | pubmed:articleTitle | The small GTP-binding protein R-Ras can influence integrin activation by antagonizing a Ras/Raf-initiated integrin suppression pathway. | lld:pubmed |
| pubmed-article:10359597 | pubmed:affiliation | Department of Respiratory Medicine, University of Edinburgh Medical School, Edinburgh EH8 9AG, United Kingdom. | lld:pubmed |
| pubmed-article:10359597 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10359597 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10359597 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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