pubmed-article:14499114 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C0449738 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C0028778 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C0021701 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1417683 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1328819 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C0243076 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:14499114 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:14499114 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:14499114 | pubmed:dateCreated | 2003-9-22 | lld:pubmed |
pubmed-article:14499114 | pubmed:abstractText | Leukocyte integrins contain an inserted (I) domain in their alpha subunits and an I-like domain in their beta(2) subunit, which directly bind ligand and regulate ligand binding, respectively. We describe a novel mechanistic class of integrin inhibitors that bind to the metal ion-dependent adhesion site of the beta(2) I-like domain and prevent its interaction with and activation of the alpha(L) I domain. The inhibitors do not bind to the alpha(L) I domain but stabilize alpha/beta subunit association and can show selectivity for alpha(L)beta(2) compared to alpha(M)beta(2). The inhibitors reveal a crucial intersection for relaying conformational signals within integrin extracellular domains. While blocking signals in one direction to the I domain, the antagonists induce the active conformation of the I-like domain and stalk domains, and thus transmit conformational signals in the other direction toward the transmembrane domains. | lld:pubmed |
pubmed-article:14499114 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14499114 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14499114 | pubmed:language | eng | lld:pubmed |
pubmed-article:14499114 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14499114 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14499114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14499114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14499114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14499114 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14499114 | pubmed:month | Sep | lld:pubmed |
pubmed-article:14499114 | pubmed:issn | 1074-7613 | lld:pubmed |
pubmed-article:14499114 | pubmed:author | pubmed-author:SpringerTimot... | lld:pubmed |
pubmed-article:14499114 | pubmed:author | pubmed-author:YangWeiW | lld:pubmed |
pubmed-article:14499114 | pubmed:author | pubmed-author:Weitz-Schmidt... | lld:pubmed |
pubmed-article:14499114 | pubmed:author | pubmed-author:ShimaokaMotom... | lld:pubmed |
pubmed-article:14499114 | pubmed:author | pubmed-author:SalasAzucenaA | lld:pubmed |
pubmed-article:14499114 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14499114 | pubmed:volume | 19 | lld:pubmed |
pubmed-article:14499114 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14499114 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14499114 | pubmed:pagination | 391-402 | lld:pubmed |
pubmed-article:14499114 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:14499114 | pubmed:meshHeading | pubmed-meshheading:14499114... | lld:pubmed |
pubmed-article:14499114 | pubmed:meshHeading | pubmed-meshheading:14499114... | lld:pubmed |
pubmed-article:14499114 | pubmed:meshHeading | pubmed-meshheading:14499114... | lld:pubmed |
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pubmed-article:14499114 | pubmed:meshHeading | pubmed-meshheading:14499114... | lld:pubmed |
pubmed-article:14499114 | pubmed:meshHeading | pubmed-meshheading:14499114... | lld:pubmed |
pubmed-article:14499114 | pubmed:meshHeading | pubmed-meshheading:14499114... | lld:pubmed |
pubmed-article:14499114 | pubmed:meshHeading | pubmed-meshheading:14499114... | lld:pubmed |
pubmed-article:14499114 | pubmed:meshHeading | pubmed-meshheading:14499114... | lld:pubmed |
pubmed-article:14499114 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:14499114 | pubmed:articleTitle | Small molecule integrin antagonists that bind to the beta2 subunit I-like domain and activate signals in one direction and block them in the other. | lld:pubmed |
pubmed-article:14499114 | pubmed:affiliation | The CBR Institute for Biomedical Research, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA. shimaoka@cbr.med.harvard.edu | lld:pubmed |
pubmed-article:14499114 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14499114 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:14499114 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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