20643898

Source:http://linkedlifedata.com/resource/pubmed/id/20643898

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0019691, umls-concept:C0019704, umls-concept:C0028778, umls-concept:C0444669, umls-concept:C0913820, umls-concept:C0913822, umls-concept:C0913823, umls-concept:C1522492, umls-concept:C1550548, umls-concept:C1555714, umls-concept:C1705654
pubmed:issue	10
pubmed:dateCreated	2010-9-20
pubmed:abstractText	We had shown that virus resistance to ADS-J1 was associated with amino acid changes in the envelope glycoprotein, mostly located in the gp120 coding region. Time-of-addition and endocytic virus transfer assays clearly demonstrated that ADS-J1 behaved as a gp120 inhibitor. ADS-J1-resistant virus was cross-resistant to the polyanion dextran sulfate, and recombination of gp120 recovered only the ADS-J1-resistant phenotype. In summary, ADS-J1 blocks an early step of virus entry that appears to be driven by gp120 alone.
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0315061
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/ADS J1, http://linkedlifedata.com/resource/pubmed/chemical/Anti-HIV Agents, http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120, http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp41, http://linkedlifedata.com/resource/pubmed/chemical/Naphthalenesulfonates, http://linkedlifedata.com/resource/pubmed/chemical/Triazines
pubmed:status	MEDLINE
pubmed:month	Oct
pubmed:issn	1098-6596
pubmed:author	pubmed-author:BallanaEsterE, pubmed-author:ClotetBonaventuraB, pubmed-author:EstéJosé AJA, pubmed-author:González-OrtegaEmmanuelE, pubmed-author:MenaMaria-PauMP, pubmed-author:PermanyerMarcM
pubmed:issnType	Electronic
pubmed:volume	54
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	4487-92
pubmed:dateRevised	2011-7-27
pubmed:meshHeading	pubmed-meshheading:20643898-Anti-HIV Agents, pubmed-meshheading:20643898-Cell Line, pubmed-meshheading:20643898-HIV Envelope Protein gp120, pubmed-meshheading:20643898-HIV Envelope Protein gp41, pubmed-meshheading:20643898-HIV-1, pubmed-meshheading:20643898-Humans, pubmed-meshheading:20643898-Naphthalenesulfonates, pubmed-meshheading:20643898-Triazines, pubmed-meshheading:20643898-Virus Internalization
pubmed:year	2010
pubmed:articleTitle	ADS-J1 inhibits HIV-1 entry by interacting with gp120 and does not block fusion-active gp41 core formation.
pubmed:affiliation	Retrovirology Laboratory IrsiCaixa, Hospital Universitari Germans Trias i Pujol, Universitat Auto´noma de Barcelona, 08916 Barcelona, Spain.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't