pubmed-article:19812165 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19812165 | lifeskim:mentions | umls-concept:C0206558 | lld:lifeskim |
pubmed-article:19812165 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:19812165 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:19812165 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:19812165 | lifeskim:mentions | umls-concept:C0032594 | lld:lifeskim |
pubmed-article:19812165 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:19812165 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
pubmed-article:19812165 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
pubmed-article:19812165 | lifeskim:mentions | umls-concept:C1709450 | lld:lifeskim |
pubmed-article:19812165 | pubmed:issue | 24 | lld:pubmed |
pubmed-article:19812165 | pubmed:dateCreated | 2009-11-20 | lld:pubmed |
pubmed-article:19812165 | pubmed:abstractText | Paired immunoglobulin-like type 2 receptor alpha (PILRalpha) is an inhibitory receptor expressed on both hematopoietic and nonhematopoietic cells. Its binding to a cellular ligand, CD99, depends on the presence of sialylated O-linked glycans on CD99. Glycoprotein B (gB) of herpes simplex virus type 1 (HSV-1) binds to PILRalpha, and this association is involved in HSV-1 infection. Here, we found that the presence of sialylated O-glycans on gB is required for gB to associate with PILRalpha. Furthermore, we identified two threonine residues on gB that are essential for the addition of the principal O-glycans acquired by gB and that are also essential for the binding of PILRalpha to gB. | lld:pubmed |
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pubmed-article:19812165 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:19812165 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19812165 | pubmed:language | eng | lld:pubmed |
pubmed-article:19812165 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19812165 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19812165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19812165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19812165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19812165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19812165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19812165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19812165 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19812165 | pubmed:month | Dec | lld:pubmed |
pubmed-article:19812165 | pubmed:issn | 1098-5514 | lld:pubmed |
pubmed-article:19812165 | pubmed:author | pubmed-author:SpearPatricia... | lld:pubmed |
pubmed-article:19812165 | pubmed:author | pubmed-author:KawaguchiYasu... | lld:pubmed |
pubmed-article:19812165 | pubmed:author | pubmed-author:SatohTakeshiT | lld:pubmed |
pubmed-article:19812165 | pubmed:author | pubmed-author:AraseHisashiH | lld:pubmed |
pubmed-article:19812165 | pubmed:author | pubmed-author:LanierLewis... | lld:pubmed |
pubmed-article:19812165 | pubmed:author | pubmed-author:WangJingJ | lld:pubmed |
pubmed-article:19812165 | pubmed:author | pubmed-author:FanQingQ | lld:pubmed |
pubmed-article:19812165 | pubmed:author | pubmed-author:AriiJunJ | lld:pubmed |
pubmed-article:19812165 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19812165 | pubmed:volume | 83 | lld:pubmed |
pubmed-article:19812165 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19812165 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19812165 | pubmed:pagination | 13042-5 | lld:pubmed |
pubmed-article:19812165 | pubmed:dateRevised | 2010-9-27 | lld:pubmed |
pubmed-article:19812165 | pubmed:meshHeading | pubmed-meshheading:19812165... | lld:pubmed |
pubmed-article:19812165 | pubmed:meshHeading | pubmed-meshheading:19812165... | lld:pubmed |
pubmed-article:19812165 | pubmed:meshHeading | pubmed-meshheading:19812165... | lld:pubmed |
pubmed-article:19812165 | pubmed:meshHeading | pubmed-meshheading:19812165... | lld:pubmed |
pubmed-article:19812165 | pubmed:meshHeading | pubmed-meshheading:19812165... | lld:pubmed |
pubmed-article:19812165 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19812165 | pubmed:articleTitle | Binding of herpes simplex virus glycoprotein B (gB) to paired immunoglobulin-like type 2 receptor alpha depends on specific sialylated O-linked glycans on gB. | lld:pubmed |
pubmed-article:19812165 | pubmed:affiliation | Laboratory of Immunochemistry, WPI Immunology Frontier Research Center, Osaka University, Suita, Osaka 565-0871, Japan. | lld:pubmed |
pubmed-article:19812165 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19812165 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:19812165 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:2703455 | entrezgene:pubmed | pubmed-article:19812165 | lld:entrezgene |
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