Crystal structures of HIV-1 reverse transcriptase mutated at codons 100, 106 and 108 show nevirapine resistance is mediated via perturbation of interactions with Tyr181 or Tyr188

ग्रंथसूची विवरण
मुख्य लेखकों:	Stammers, D, Ren, J, Nichols, C, Chamberlain, P, Weaver, K, Short, SA, Stuart, D
स्वरूप:	Journal article
प्रकाशित:	2002

Crystal structures of HIV-1 reverse transcriptases mutated at codons 100, 106 and 108 and mechanisms of resistance to non-nucleoside inhibitors.
द्वारा: Ren, J, और अन्य
प्रकाशित: (2004)

Structural mechanisms of drug resistance for mutations at codons 181 and 188 in HIV-1 reverse transcriptase and the improved resilience of second generation non-nucleoside inhibitors.
द्वारा: Ren, J, और अन्य
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Relationship of potency and resilience to drug resistant mutations for GW420867X revealed by crystal structures of inhibitor complexes for wild-type, Leu100Ile, Lys101Glu, and Tyr188Cys mutant HIV-1 reverse transcriptases.
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Mutational analysis of Tyr-318 within the non-nucleoside reverse transcriptase inhibitor binding pocket of human immunodeficiency virus type I reverse transcriptase.
द्वारा: Pelemans, H, और अन्य
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Structural insights into mechanisms of non-nucleoside drug resistance for HIV-1 reverse transcriptases mutated at codons 101 or 138.
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Structural basis for drug resistance mechanisms for non-nucleoside inhibitors of HIV reverse transcriptase.
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Intrapartum single-dose carbamazepine reduces nevirapine levels faster and may decrease resistance after a single dose of nevirapine for perinatal HIV prevention.
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द्वारा: Herzmann, C, और अन्य
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Crystal structures of HIV-1 reverse transcriptase mutated at codons 100, 106 and 108 show nevirapine resistance is mediated via perturbation of interactions with Tyr181 or Tyr188

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