pubmed-article:8752218 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8752218 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:8752218 | lifeskim:mentions | umls-concept:C0134835 | lld:lifeskim |
pubmed-article:8752218 | lifeskim:mentions | umls-concept:C0016790 | lld:lifeskim |
pubmed-article:8752218 | lifeskim:mentions | umls-concept:C1326500 | lld:lifeskim |
pubmed-article:8752218 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:8752218 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
pubmed-article:8752218 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
pubmed-article:8752218 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:8752218 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
pubmed-article:8752218 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:8752218 | pubmed:dateCreated | 1996-10-3 | lld:pubmed |
pubmed-article:8752218 | pubmed:abstractText | alpha(1,3)Fucosylated oligosaccharides represent components of leukocyte counterreceptors for E- and P-selectins and of L-selectin ligands expressed by lymph node high endothelial venules (HEV). The identity of the alpha(1,3)fucosyltransferase(s) required for their expression has been uncertain, as has a requirement for alpha(1,3)fucosylation in HEV L-selectin ligand activity. We demonstrate here that mice deficient in alpha(1,3) fucosyltransferase Fuc-TVII exhibit a leukocyte adhesion deficiency characterized by absent leukocyte E- and P-selectin ligand activity and deficient HEV L-selectin ligand activity. Selectin ligand deficiency is distinguished by blood leukocytosis, impaired leukocyte extravasation in inflammation, and faulty lymphocyte homing. These observations demonstrate an essential role for Fuc-TVII in E-, P-, and L-selectin ligand biosynthesis and imply that this locus can control leukocyte trafficking in health and disease. | lld:pubmed |
pubmed-article:8752218 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8752218 | pubmed:language | eng | lld:pubmed |
pubmed-article:8752218 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8752218 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8752218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8752218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8752218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8752218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8752218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8752218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8752218 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8752218 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8752218 | pubmed:month | Aug | lld:pubmed |
pubmed-article:8752218 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:SmithP LPL | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:LINSKJJ | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:ChengGG | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:ThaleJJ | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:HindsgaulOO | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:IsogaiYY | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:LoweJ BJB | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:CamperS ASA | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:MarksR MRM | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:RogersC ECE | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:MalýPP | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:SullivanF XFX | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:PetryniakBB | lld:pubmed |
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pubmed-article:8752218 | pubmed:author | pubmed-author:SaundersT LTL | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:CamphausenR... | lld:pubmed |
pubmed-article:8752218 | pubmed:author | pubmed-author:GerstenK MKM | lld:pubmed |
pubmed-article:8752218 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8752218 | pubmed:day | 23 | lld:pubmed |
pubmed-article:8752218 | pubmed:volume | 86 | lld:pubmed |
pubmed-article:8752218 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8752218 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8752218 | pubmed:pagination | 643-53 | lld:pubmed |
pubmed-article:8752218 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:8752218 | pubmed:meshHeading | pubmed-meshheading:8752218-... | lld:pubmed |
pubmed-article:8752218 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8752218 | pubmed:articleTitle | The alpha(1,3)fucosyltransferase Fuc-TVII controls leukocyte trafficking through an essential role in L-, E-, and P-selectin ligand biosynthesis. | lld:pubmed |
pubmed-article:8752218 | pubmed:affiliation | Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor 48109-0650, USA. | lld:pubmed |
pubmed-article:8752218 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8752218 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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