pubmed-article:7585949 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7585949 | lifeskim:mentions | umls-concept:C0441635 | lld:lifeskim |
pubmed-article:7585949 | lifeskim:mentions | umls-concept:C0134835 | lld:lifeskim |
pubmed-article:7585949 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:7585949 | lifeskim:mentions | umls-concept:C1419941 | lld:lifeskim |
pubmed-article:7585949 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:7585949 | lifeskim:mentions | umls-concept:C1511545 | lld:lifeskim |
pubmed-article:7585949 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:7585949 | pubmed:dateCreated | 1995-11-24 | lld:pubmed |
pubmed-article:7585949 | pubmed:abstractText | P-selectin glycoprotein ligand 1 (PSGL-1) is a mucin-like glycoprotein expressed on the surface of myeloid cells and serves as the high affinity counterreceptor for P-selectin. The PSGL-1-P-selectin interaction is calcium dependent and requires presentation of sialyl-Lewisx (sLex)-type structures on the O-linked glycans of PSGL-1. We report here the identification of a non-carbohydrate component of the binding determinant that is critical for high affinity binding to P-selectin. Located within the first 19 amino acids, this anionic polypeptide segment contains at least one sulfated tyrosine residue. We propose that this sulfotyrosine-containing segment of PSGL-1, in conjunction with sLex presented on O-linked glycans, constitutes the high affinity P-selectin-binding site. | lld:pubmed |
pubmed-article:7585949 | pubmed:language | eng | lld:pubmed |
pubmed-article:7585949 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7585949 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7585949 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7585949 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7585949 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7585949 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7585949 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7585949 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7585949 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7585949 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7585949 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7585949 | pubmed:month | Oct | lld:pubmed |
pubmed-article:7585949 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:7585949 | pubmed:author | pubmed-author:SakaRR | lld:pubmed |
pubmed-article:7585949 | pubmed:author | pubmed-author:ComessK MKM | lld:pubmed |
pubmed-article:7585949 | pubmed:author | pubmed-author:BaroneK MKM | lld:pubmed |
pubmed-article:7585949 | pubmed:author | pubmed-author:CummingD ADA | lld:pubmed |
pubmed-article:7585949 | pubmed:author | pubmed-author:CamphausenR... | lld:pubmed |
pubmed-article:7585949 | pubmed:author | pubmed-author:ShawG DGD | lld:pubmed |
pubmed-article:7585949 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7585949 | pubmed:day | 20 | lld:pubmed |
pubmed-article:7585949 | pubmed:volume | 83 | lld:pubmed |
pubmed-article:7585949 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7585949 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7585949 | pubmed:pagination | 323-31 | lld:pubmed |
pubmed-article:7585949 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:7585949 | pubmed:meshHeading | pubmed-meshheading:7585949-... | lld:pubmed |
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pubmed-article:7585949 | pubmed:meshHeading | pubmed-meshheading:7585949-... | lld:pubmed |
pubmed-article:7585949 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7585949 | pubmed:articleTitle | A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding. | lld:pubmed |
pubmed-article:7585949 | pubmed:affiliation | Genetics Institute, Small Molecule Drug Discovery Group, Cambridge, Massachusetts 02140, USA. | lld:pubmed |
pubmed-article:7585949 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7585949 | pubmed:publicationType | Comparative Study | lld:pubmed |
entrez-gene:6404 | entrezgene:pubmed | pubmed-article:7585949 | lld:entrezgene |
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