pubmed-article:11551937 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11551937 | lifeskim:mentions | umls-concept:C0521026 | lld:lifeskim |
pubmed-article:11551937 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:11551937 | lifeskim:mentions | umls-concept:C0128897 | lld:lifeskim |
pubmed-article:11551937 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:11551937 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:11551937 | pubmed:issue | 46 | lld:pubmed |
pubmed-article:11551937 | pubmed:dateCreated | 2001-11-12 | lld:pubmed |
pubmed-article:11551937 | pubmed:abstractText | Monocyte chemoattractant protein-1 (MCP-1) is a chemotactic cytokine mainly acting on monocytes and T cells that elicits its biological effects by interacting with the seven-transmembrane helix receptor CCR2B. The vaccinia virus strain Lister and many other poxviruses express soluble proteins (vCCI) that bind MCP-1 and other CC chemokines and inhibit their function. In order to define the interaction site of MCP-1 with vCCI from vaccinia, surface exposed residues of MCP-1 were identified and mutated to alanine. The MCP-1 variants were expressed, purified, and their interaction with vCCI was characterized. The site on MCP-1 for vCCI binding is dominated by arginine 18 with important additional contributions from tyrosine 13 and arginine 24. These residues define a binding site that largely overlaps with the CCR2B receptor interaction site. The viral chemokine-binding protein vCCI thus inhibits the biological function of MCP-1 by directly masking its CCR2B receptor-binding site. | lld:pubmed |
pubmed-article:11551937 | pubmed:language | eng | lld:pubmed |
pubmed-article:11551937 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11551937 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11551937 | pubmed:month | Nov | lld:pubmed |
pubmed-article:11551937 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:11551937 | pubmed:author | pubmed-author:UrferRR | lld:pubmed |
pubmed-article:11551937 | pubmed:author | pubmed-author:ZuberJ FJF | lld:pubmed |
pubmed-article:11551937 | pubmed:author | pubmed-author:ManninoMM | lld:pubmed |
pubmed-article:11551937 | pubmed:author | pubmed-author:StuderCC | lld:pubmed |
pubmed-article:11551937 | pubmed:author | pubmed-author:BeckC GCG | lld:pubmed |
pubmed-article:11551937 | pubmed:author | pubmed-author:DemangeB JBJ | lld:pubmed |
pubmed-article:11551937 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11551937 | pubmed:day | 16 | lld:pubmed |
pubmed-article:11551937 | pubmed:volume | 276 | lld:pubmed |
pubmed-article:11551937 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11551937 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11551937 | pubmed:pagination | 43270-6 | lld:pubmed |
pubmed-article:11551937 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:11551937 | pubmed:year | 2001 | lld:pubmed |
pubmed-article:11551937 | pubmed:articleTitle | The viral CC chemokine-binding protein vCCI inhibits monocyte chemoattractant protein-1 activity by masking its CCR2B-binding site. | lld:pubmed |
pubmed-article:11551937 | pubmed:affiliation | Department of Arthritis Biology, Novartis Pharma AG, CH-4002 Basel, Switzerland. | lld:pubmed |
pubmed-article:11551937 | pubmed:publicationType | Journal Article | lld:pubmed |
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