| pubmed-article:15701706 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15701706 | lifeskim:mentions | umls-concept:C0007578 | lld:lifeskim |
| pubmed-article:15701706 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
| pubmed-article:15701706 | lifeskim:mentions | umls-concept:C0231617 | lld:lifeskim |
| pubmed-article:15701706 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
| pubmed-article:15701706 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15701706 | pubmed:dateCreated | 2005-2-9 | lld:pubmed |
| pubmed-article:15701706 | pubmed:abstractText | The unbinding dynamics of complexes involving cell-adhesion molecules depends on the specific ligands. Atomic force microscopy measurements have shown that for the specific P-selectin-P-selectin glycoprotein ligand (sPSGL-1) the average bond lifetime t initially increases (catch bonds) at low (< or =10 pN) constant force, f, and decreases when f > 10 pN (slip bonds). In contrast, for the complex with G1 anti-P-selectin monoclonal antibody t monotonically decreases with f. To quantitatively map the energy landscape of such complexes we use a model that considers the possibility of redistribution of population from one force-free state to another force-stabilized bound state. The excellent agreement between theory and experiments allows us to extract energy landscape parameters by fitting the calculated curves to the lifetime measurements for both sPSGL-1 and G1. Surprisingly, the unbinding transition state for P-selectin-G1 complex is close (0.32 nm) to the bound state, implying that the interaction is brittle, i.e., once deformed, the complex fractures. In contrast, the unbinding transition state of the P-selectin-sPSGL-1 complex is far (approximately 1.5 nm) from the bound state, indicative of a compliant structure. Constant f energy landscape parameters are used to compute the distributions of unbinding times and unbinding forces as a function of the loading rate, rf. For a given rf, unbinding of sPSGL-1 occurs over a broader range of f with the most probable f being an order of magnitude less than for G1. The theory for cell adhesion complexes can be used to predict the outcomes of unbinding of other protein-protein complexes. | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15701706 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15701706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701706 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15701706 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15701706 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:15701706 | pubmed:author | pubmed-author:ThirumalaiDD | lld:pubmed |
| pubmed-article:15701706 | pubmed:author | pubmed-author:BarsegovVV | lld:pubmed |
| pubmed-article:15701706 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15701706 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:15701706 | pubmed:volume | 102 | lld:pubmed |
| pubmed-article:15701706 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15701706 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15701706 | pubmed:pagination | 1835-9 | lld:pubmed |
| pubmed-article:15701706 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:15701706 | pubmed:meshHeading | pubmed-meshheading:15701706... | lld:pubmed |
| pubmed-article:15701706 | pubmed:meshHeading | pubmed-meshheading:15701706... | lld:pubmed |
| pubmed-article:15701706 | pubmed:meshHeading | pubmed-meshheading:15701706... | lld:pubmed |
| pubmed-article:15701706 | pubmed:meshHeading | pubmed-meshheading:15701706... | lld:pubmed |
| pubmed-article:15701706 | pubmed:meshHeading | pubmed-meshheading:15701706... | lld:pubmed |
| pubmed-article:15701706 | pubmed:meshHeading | pubmed-meshheading:15701706... | lld:pubmed |
| pubmed-article:15701706 | pubmed:meshHeading | pubmed-meshheading:15701706... | lld:pubmed |
| pubmed-article:15701706 | pubmed:meshHeading | pubmed-meshheading:15701706... | lld:pubmed |
| pubmed-article:15701706 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15701706 | pubmed:articleTitle | Dynamics of unbinding of cell adhesion molecules: transition from catch to slip bonds. | lld:pubmed |
| pubmed-article:15701706 | pubmed:affiliation | Institute for Physical Science and Technology, University of Maryland, College Park, MD 20742, USA. | lld:pubmed |
| pubmed-article:15701706 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15701706 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15701706 | lld:pubmed |
