Source:http://linkedlifedata.com/resource/entrezgene/hivinteraction/155971-10332
| Predicate | Object |
|---|---|
| rdf:type | |
| entrezgene:pubmed |
pubmed-article:11257134,
pubmed-article:11384997,
pubmed-article:11739956,
pubmed-article:12152166,
pubmed-article:1518869,
pubmed-article:15215692,
pubmed-article:15795245,
pubmed-article:16365436,
pubmed-article:1736938,
pubmed-article:17632570,
pubmed-article:19514109,
pubmed-article:20152818,
pubmed-article:21277928,
pubmed-article:22842622
|
| entrezgene:interactant | |
| entrezgene:geneRifText |
Crystal structures of carbohydrate-recognition domains of DC-SIGN and of DC-SIGNR in combination with binding studies reveal that these receptors selectively recognize endogenous high-mannose oligosaccharides of HIV-1 gp120,
HIV-1 gp120 binds to a membrane-associated mannose-binding lectin in a CD4-independent manner,
L-SIGN behaves similarly to DC-SIGN in that it has a high affinity for ICAM-3, captures HIV-1 through gp120 binding, and enhances HIV-1 infection of T cells in trans
|
| entrezgene:keyphrase |
binds
|