pubmed-article:17696515 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C0003451 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C0013227 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C0332325 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C1883559 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C2348205 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C0917721 | lld:lifeskim |
pubmed-article:17696515 | lifeskim:mentions | umls-concept:C0205198 | lld:lifeskim |
pubmed-article:17696515 | pubmed:issue | 18 | lld:pubmed |
pubmed-article:17696515 | pubmed:dateCreated | 2007-8-30 | lld:pubmed |
pubmed-article:17696515 | pubmed:abstractText | The potent new antiviral inhibitor GRL-98065 (1) of HIV-1 protease (PR) has been studied with PR variants containing the single mutations D30N, I50V, V82A, and I84V that provide resistance to the major clinical inhibitors. Compound 1 had inhibition constants of 17-fold, 8-fold, 3-fold, and 3-fold, respectively, for PR(D30N), PR(I50V), PR(V82A), and PR(I84V) relative to wild type PR. The chemically related darunavir had similar relative inhibition, except for PR(D30N), where inhibitor 1 was approximately 3-fold less potent. The high resolution (1.11-1.60 Angstrom) crystal structures of PR mutant complexes with inhibitor 1 showed small changes relative to the wild type enzyme. PR(D30N) and PR(V82A) showed compensating interactions with inhibitor 1 relative to those of PR, while reduced hydrophobic contacts were observed with PR(I50V) and PR(I84V). Importantly, inhibitor 1 complexes showed fewer changes relative to wild type enzyme than reported for darunavir complexes. Therefore, inhibitor 1 is a valuable addition to the antiviral inhibitors with high potency against resistant strains of HIV. | lld:pubmed |
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pubmed-article:17696515 | pubmed:language | eng | lld:pubmed |
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pubmed-article:17696515 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:17696515 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17696515 | pubmed:month | Sep | lld:pubmed |
pubmed-article:17696515 | pubmed:issn | 0022-2623 | lld:pubmed |
pubmed-article:17696515 | pubmed:author | pubmed-author:GhoshArun KAK | lld:pubmed |
pubmed-article:17696515 | pubmed:author | pubmed-author:HarrisonRober... | lld:pubmed |
pubmed-article:17696515 | pubmed:author | pubmed-author:WangYuan-Fang... | lld:pubmed |
pubmed-article:17696515 | pubmed:author | pubmed-author:TozserJozsefJ | lld:pubmed |
pubmed-article:17696515 | pubmed:author | pubmed-author:WeberIrene... | lld:pubmed |
pubmed-article:17696515 | pubmed:author | pubmed-author:TieYunfengY | lld:pubmed |
pubmed-article:17696515 | pubmed:author | pubmed-author:BorossPeter... | lld:pubmed |
pubmed-article:17696515 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17696515 | pubmed:day | 6 | lld:pubmed |
pubmed-article:17696515 | pubmed:volume | 50 | lld:pubmed |
pubmed-article:17696515 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17696515 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17696515 | pubmed:pagination | 4509-15 | lld:pubmed |
pubmed-article:17696515 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
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pubmed-article:17696515 | pubmed:meshHeading | pubmed-meshheading:17696515... | lld:pubmed |
pubmed-article:17696515 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17696515 | pubmed:articleTitle | Potent new antiviral compound shows similar inhibition and structural interactions with drug resistant mutants and wild type HIV-1 protease. | lld:pubmed |
pubmed-article:17696515 | pubmed:affiliation | Department of Biology, Molecular Basis of Disease, Georgia State University, Atlanta, Georgia 30303, USA. | lld:pubmed |
pubmed-article:17696515 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17696515 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:17696515 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:17696515 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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