pubmed-article:20974843 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20974843 | lifeskim:mentions | umls-concept:C0019682 | lld:lifeskim |
pubmed-article:20974843 | lifeskim:mentions | umls-concept:C0019699 | lld:lifeskim |
pubmed-article:20974843 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:20974843 | lifeskim:mentions | umls-concept:C0558295 | lld:lifeskim |
pubmed-article:20974843 | lifeskim:mentions | umls-concept:C1332714 | lld:lifeskim |
pubmed-article:20974843 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
pubmed-article:20974843 | lifeskim:mentions | umls-concept:C1548789 | lld:lifeskim |
pubmed-article:20974843 | pubmed:issue | 52 | lld:pubmed |
pubmed-article:20974843 | pubmed:dateCreated | 2010-12-20 | lld:pubmed |
pubmed-article:20974843 | pubmed:abstractText | CD4 is a co-receptor for binding of T cells to antigen-presenting cells and the primary receptor for the human immunodeficiency virus type 1 (HIV). CD4 exists in three different forms on the cell surface defined by the state of the domain 2 cysteine residues: an oxidized monomer, a reduced monomer, and a covalent dimer linked through the domain 2 cysteines. The disulfide-linked dimer is the preferred immune co-receptor. The form of CD4 that is preferred by HIV was examined in this study. HIV entry and envelope-mediated cell-cell fusion were tested using cells expressing comparable levels of wild-type or disulfide bond mutant CD4 in which the domain 2 cysteines were mutated to alanine. Eliminating the domain 2 disulfide bond increased entry of HIV reporter viruses and enhanced HIV envelope-mediated cell-cell fusion 2-4-fold. These observations suggest that HIV enters susceptible cells preferably through monomeric reduced CD4, whereas dimeric CD4 is the preferred receptor for binding to antigen-presenting cells. Cleavage of the domain 2 disulfide bond is possibly involved in the conformational change in CD4 associated with fusion of the HIV and cell membranes. | lld:pubmed |
pubmed-article:20974843 | pubmed:language | eng | lld:pubmed |
pubmed-article:20974843 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20974843 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20974843 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20974843 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20974843 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20974843 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20974843 | pubmed:month | Dec | lld:pubmed |
pubmed-article:20974843 | pubmed:issn | 1083-351X | lld:pubmed |
pubmed-article:20974843 | pubmed:author | pubmed-author:HoggPhilip... | lld:pubmed |
pubmed-article:20974843 | pubmed:author | pubmed-author:MatthiasLisa... | lld:pubmed |
pubmed-article:20974843 | pubmed:author | pubmed-author:TabrettCather... | lld:pubmed |
pubmed-article:20974843 | pubmed:author | pubmed-author:AzimiImanI | lld:pubmed |
pubmed-article:20974843 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20974843 | pubmed:day | 24 | lld:pubmed |
pubmed-article:20974843 | pubmed:volume | 285 | lld:pubmed |
pubmed-article:20974843 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20974843 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20974843 | pubmed:pagination | 40793-9 | lld:pubmed |
pubmed-article:20974843 | pubmed:meshHeading | pubmed-meshheading:20974843... | lld:pubmed |
pubmed-article:20974843 | pubmed:meshHeading | pubmed-meshheading:20974843... | lld:pubmed |
pubmed-article:20974843 | pubmed:meshHeading | pubmed-meshheading:20974843... | lld:pubmed |
pubmed-article:20974843 | pubmed:meshHeading | pubmed-meshheading:20974843... | lld:pubmed |
pubmed-article:20974843 | pubmed:meshHeading | pubmed-meshheading:20974843... | lld:pubmed |
pubmed-article:20974843 | pubmed:meshHeading | pubmed-meshheading:20974843... | lld:pubmed |
pubmed-article:20974843 | pubmed:meshHeading | pubmed-meshheading:20974843... | lld:pubmed |
pubmed-article:20974843 | pubmed:meshHeading | pubmed-meshheading:20974843... | lld:pubmed |
pubmed-article:20974843 | pubmed:meshHeading | pubmed-meshheading:20974843... | lld:pubmed |
pubmed-article:20974843 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20974843 | pubmed:articleTitle | Reduced monomeric CD4 is the preferred receptor for HIV. | lld:pubmed |
pubmed-article:20974843 | pubmed:affiliation | Lowy Cancer Research Centre and Prince of Wales Clinical School, University of New South Wales, Sydney, New South Wales 2052, Australia. | lld:pubmed |
pubmed-article:20974843 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20974843 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:920 | entrezgene:pubmed | pubmed-article:20974843 | lld:entrezgene |
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