literature

HIV mutation literature information.

Insights into the mechanism of drug resistance: X-ray structure analysis of G48V/C95F tethered HIV-1 protease dimer/saquinavir complex.

PMID: 20471372 2010 Biochemical and biophysical research communications

Abstract: Recently, G48V mutation is found to co-exist with the mutation C95F in AIDS patients treated with saquinavir.

Abstract: The mutation G48V in HIV-1 protease is a major resistance mutation against the drug saquinavir.

Abstract: The present structure also provides a rationale for the clinical observation that the resistance mutations C95F/G48V/V82A occur as a cluster in AIDS patients.

Decomposing the energetic impact of drug resistant mutations in HIV-1 protease on binding DRV.

PMID: 20543885 2010 Journal of chemical theory and computation

Abstract: Two drug-resistant protease variants FLAP+ (L10I, G48V, I54V, V82A) and ACT (V82T, I84V) decrease the binding affinity with DRV by 1.0 kcal/mol and 1.6 kcal/mol respectively.

Introduction: In this study, the binding of DRV was investigated with wild-type HIV-1 protease and two drug-resistant variants: FLAP+ (Figure 1B) with L10I, G48V, I54V, V82A which are a combination of flap and active site mutations, and ACT (Figure 1C) with V82T, I84V which are active site mutations.

Discussion: In this st

Comparison of protease inhibitor (PI) resistance-associated mutations between PI-naive and PI-experienced HIV-1 infected patients in Thailand where subtype A/E is predominant.

PMID: 20636277 2010 Current HIV research

Abstract: The most common primary PI-RAMs in the latter group were V82A (10%), I54V (7%) and G48V (4.8%).

HIV-1 protease mutations and protease inhibitor cross-resistance.

PMID: 20660676 2010 Antimicrobial agents and chemotherapy

Abstract: Of the mutations with the greatest effect on PI susceptibility, I84AV was associated with decreased susceptibility to eight PIs; V32I, G48V, I54ALMSTV, V82F, and L90M were associated with decreased susceptibility to six to seven PIs; I47A, G48M, I50V, L76V, V82ST, and N88S were associated with decreased susceptibility to four to five PIs; and D30N,

PMID: 20695887 2010 The FEBS journal

Discussion: Also, the structure of PRG48V-DRV showed reduced volume of the active site cavity relative to the wild type complex, consistent with a major effect of the G48V rather than the L90M mutation in reducing the S1/S1' volume in PRG48V/L90M-SQV.

Human immunodeficiency virus type 1 protease inhibitor drug-resistant mutants give discordant results when compared in single-cycle and multiple-cycle fitness assays.

PMID: 20826651 2010 Journal of clinical microbiology

Abstract: Five protease mutants showed statistically different fitness values by the MCA versus the SCA: the D30N, G48V, I50V, I54L, and I54M mutants.

Distinct resistance mutation and polymorphism acquisition in HIV-1 protease of subtypes B and F1 from children and adult patients under virological failure.

PMID: 18992847 2009 Infection, genetics and evolution

Method: Mutations D30N (NFV), V32I (LPV), M46I/L (IDV/RTV), I47V/A (LPV/RTV), G48V (SQV), I50L/V (APV), V82A/F/T/S (LPV/IDV/RTV), I84V (APV/IDV/RTV) and L90M (SQV/NFV) were considered as major resistance mutations and were analyzed separately for each PI as well as quantitatively all together.

Table: G48V

Proteochemometric modeling of drug resistance over the mutational space for multiple HIV protease variants and multiple protease inhibitors.

PMID: 19391634 2009 Journal of chemical information and modeling

Abstract: The model revealed the most deleterious mutations in the protease to be D30N, V32I, G48V, I50V, I54V, V82A, I84V, and L90M.

Role of atazanavir in the treatment of HIV infection.

PMID: 19436623 2009 Therapeutics and clinical risk management

Introduction: Mutations more significant to be included in the GIQ model are the following: L10F/I/V, K20M/R, L24I, D30N, V32I, L33F, M36I/L, I47V/A, G48V, I50V, I50L, F53L, I54V/L/A/M/T/S, L63P, A71V/T, G73S, V77I, V82A/F/T, I84V, N88D/S and

Rapid and accurate prediction of binding free energies for saquinavir-bound HIV-1 proteases.

PMID: 18225901 2008 Journal of the American Chemical Society

Abstract: A detailed analysis of the enthalpic/entropic balance of drug-protease interactions explains resistance in L90M in terms of a higher vibrational entropy than in the WT complex, while G48V disrupts critical hydrogen bonds at the inhibitor's binding site and produces an altered, more unfavorable balance of Coulomb and polar desolvation energies.

Abstract: Herein we report an application of the molecular mechanics Poisson-Boltzmann surface area (MM/PBSA) technique to the ranking of binding affinities of the inhibitor saquinavir with the wild type (WT) and three resistant mutants of HIV-1 protease: L90M, G48V, and G48V/L90M.

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