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 HIV mutation literature information.


  Genetic variation and susceptibilities to protease inhibitors among subtype B and F isolates in Brazil.
 PMID: 9925514       1999       Antimicrobial agents and chemotherapy
Abstract: The frequency of critical PI resistance substitutions (amino acid changes D30N, V82A/F/T, I84V, N88D, and L90M) among Brazilian isolates is very low (mean, 2.5%), and the associated secondary substitutions (amino acid positions 10L, 20K, 36M, 46M, 48G, 54I, 63P, 71A, and 77A) are infrequent.


  Virologic responses to a ritonavir--saquinavir-containing regimen in patients who had previously failed nelfinavir.
 PMID: 10202820       1999       AIDS (London, England)
Abstract: The most frequent baseline mutations in the protease gene prior to switching were D30N (13 out of 18), N88D (eight out of 18) and M36I (eight out of 18).


  Structural and kinetic analysis of drug resistant mutants of HIV-1 protease.
 PMID: 10429209       1999       European journal of biochemistry
Abstract: Mutant V82S is the least active (2-20% of wild-type protease), mutants N88D, R8Q, and L90M exhibit activities ranging from 20 to 40% and G48V from 50 to 80% of the wild-type activity.
Abstract: Mutants of HIV-1 protease that are commonly selected on exposure to different drugs, V82S, G48V, N88D and L90M, showed reduced catalytic activity compared to the wild-type protease on cleavage site peptides, CA-p2, p6pol-PR and PR-RT, c


  A mutation in human immunodeficiency virus type 1 protease at position 88, located outside the active site, confers resistance to the hydroxyethylurea inhibitor SC-55389A.
 PMID: 9055985       1997       Antimicrobial agents and chemotherapy
Abstract: In contrast, SC-52151-resistant variants selected from the monocytotropic strain SF162 had multiple substitutions in the protease gene (I11V, M461, F53L, A71V, and N88D), and the N88D mutation, re-created by oligonucleotide-mediated site-directed mutagenesis in HXB2, did not confer resistance to SC-52151.
Abstract: The potencies of L735,524 and Ro31-8959 were not reduced when these compounds were assayed against variants with either the N88S or N88D substitution.



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