| pubmed-article:10089882 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10089882 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:10089882 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:10089882 | lifeskim:mentions | umls-concept:C1332700 | lld:lifeskim |
| pubmed-article:10089882 | lifeskim:mentions | umls-concept:C0597538 | lld:lifeskim |
| pubmed-article:10089882 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
| pubmed-article:10089882 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
| pubmed-article:10089882 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
| pubmed-article:10089882 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:10089882 | pubmed:dateCreated | 1999-4-22 | lld:pubmed |
| pubmed-article:10089882 | pubmed:abstractText | Chemokine receptors and related seven-transmembrane-segment (7TMS) receptors serve as coreceptors for entry of human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV) into target cells. Each of these otherwise diverse coreceptors contains an N-terminal region that is acidic and tyrosine rich. Here, we show that the chemokine receptor CCR5, a principal HIV-1 coreceptor, is posttranslationally modified by O-linked glycosylation and by sulfation of its N-terminal tyrosines. Sulfated tyrosines contribute to the binding of CCR5 to MIP-1 alpha, MIP-1 beta, and HIV-1 gp120/CD4 complexes and to the ability of HIV-1 to enter cells expressing CCR5 and CD4. CXCR4, another important HIV-1 coreceptor, is also sulfated. Tyrosine sulfation may contribute to the natural function of many 7TMS receptors and may be a modification common to primate immunodeficiency virus coreceptors. | lld:pubmed |
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| pubmed-article:10089882 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10089882 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10089882 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10089882 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:10089882 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:10089882 | pubmed:author | pubmed-author:GerardCC | lld:pubmed |
| pubmed-article:10089882 | pubmed:author | pubmed-author:WyattRR | lld:pubmed |
| pubmed-article:10089882 | pubmed:author | pubmed-author:SodroskiJJ | lld:pubmed |
| pubmed-article:10089882 | pubmed:author | pubmed-author:CayabyabMM | lld:pubmed |
| pubmed-article:10089882 | pubmed:author | pubmed-author:GerardN PNP | lld:pubmed |
| pubmed-article:10089882 | pubmed:author | pubmed-author:ChoiLL | lld:pubmed |
| pubmed-article:10089882 | pubmed:author | pubmed-author:MirzabekovTT | lld:pubmed |
| pubmed-article:10089882 | pubmed:author | pubmed-author:FarzanMM | lld:pubmed |
| pubmed-article:10089882 | pubmed:author | pubmed-author:KolchinskyPP | lld:pubmed |
| pubmed-article:10089882 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10089882 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:10089882 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:10089882 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10089882 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10089882 | pubmed:pagination | 667-76 | lld:pubmed |
| pubmed-article:10089882 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:10089882 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10089882 | pubmed:articleTitle | Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry. | lld:pubmed |
| pubmed-article:10089882 | pubmed:affiliation | Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA. farzan@mbcrr.harvard.edu | lld:pubmed |
| pubmed-article:10089882 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10089882 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:10089882 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10089882 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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