pubmed-article:15084137 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15084137 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
pubmed-article:15084137 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:15084137 | lifeskim:mentions | umls-concept:C0674428 | lld:lifeskim |
pubmed-article:15084137 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:15084137 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:15084137 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
pubmed-article:15084137 | lifeskim:mentions | umls-concept:C0121925 | lld:lifeskim |
pubmed-article:15084137 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:15084137 | pubmed:dateCreated | 2004-4-15 | lld:pubmed |
pubmed-article:15084137 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:abstractText | The effect of the K103N mutation of HIV-1 reverse transcriptase (RT) on the activity of efavirenz analogues was studied via Monte Carlo/free energy perturbation calculations. The relative fold resistance energies indicate that efavirenz binds to K103N RT in a manner similar to the wild-type enzyme. The improved performance of the quinazolinones against the mutant enzyme is attributed to formation of a more optimal hydrogen-bonding network with bridging water molecules between the ligands and Glu138. | lld:pubmed |
pubmed-article:15084137 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:language | eng | lld:pubmed |
pubmed-article:15084137 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15084137 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15084137 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15084137 | pubmed:month | Apr | lld:pubmed |
pubmed-article:15084137 | pubmed:issn | 0022-2623 | lld:pubmed |
pubmed-article:15084137 | pubmed:author | pubmed-author:JorgensenWill... | lld:pubmed |
pubmed-article:15084137 | pubmed:author | pubmed-author:Udier-Blagovi... | lld:pubmed |
pubmed-article:15084137 | pubmed:author | pubmed-author:Tirado-RivesJ... | lld:pubmed |
pubmed-article:15084137 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15084137 | pubmed:day | 22 | lld:pubmed |
pubmed-article:15084137 | pubmed:volume | 47 | lld:pubmed |
pubmed-article:15084137 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15084137 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15084137 | pubmed:pagination | 2389-92 | lld:pubmed |
pubmed-article:15084137 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
pubmed-article:15084137 | pubmed:meshHeading | pubmed-meshheading:15084137... | lld:pubmed |
pubmed-article:15084137 | pubmed:meshHeading | pubmed-meshheading:15084137... | lld:pubmed |
pubmed-article:15084137 | pubmed:meshHeading | pubmed-meshheading:15084137... | lld:pubmed |
pubmed-article:15084137 | pubmed:meshHeading | pubmed-meshheading:15084137... | lld:pubmed |
pubmed-article:15084137 | pubmed:meshHeading | pubmed-meshheading:15084137... | lld:pubmed |
pubmed-article:15084137 | pubmed:meshHeading | pubmed-meshheading:15084137... | lld:pubmed |
pubmed-article:15084137 | pubmed:meshHeading | pubmed-meshheading:15084137... | lld:pubmed |
pubmed-article:15084137 | pubmed:meshHeading | pubmed-meshheading:15084137... | lld:pubmed |
pubmed-article:15084137 | pubmed:meshHeading | pubmed-meshheading:15084137... | lld:pubmed |
pubmed-article:15084137 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15084137 | pubmed:articleTitle | Structural and energetic analyses of the effects of the K103N mutation of HIV-1 reverse transcriptase on efavirenz analogues. | lld:pubmed |
pubmed-article:15084137 | pubmed:affiliation | Department of Chemistry, Yale University, New Haven, Connecticut 06520-8107, USA. | lld:pubmed |
pubmed-article:15084137 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15084137 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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