literature

HIV mutation literature information.

Drug resistance mutations in HIV type 1 isolates from patients failing antiretroviral therapy in Morocco.

PMID: 21919803 2012 AIDS research and human retroviruses

Abstract: The prevalence of protease inhibitor (PI) mutations was 22%, with major mutations V82A and M46I seen in 16% and 11% of viruses from PI-exposed individuals, respectively.

Drug resistance mutations in HIV pol sequences from Argentinean patients under antiretroviral treatment: subtype, gender, and age issues.

PMID: 21936717 2012 AIDS research and human retroviruses

Abstract: The most common DRMs were L10I, I54V, L90M, V82A, A71V, L10V, M46I, M184V, M41L, T215Y, D67N, L210W, K70R, N348I, V118I, K103N, Y181C, G190A, K101E, V108I, L100I, V90I, K101Q, and

PMID: 22258921 2012 The Journal of antimicrobial chemotherapy

Abstract: One or more protease mutations were detected in 32 (11%) patients; the most frequent were I54V (n = 12), M46I (n = 11), V82A (n = 7) and L76V (n = 3).

Potent antiviral HIV-1 protease inhibitor GRL-02031 adapts to the structures of drug resistant mutants with its P1'-pyrrolidinone ring.

PMID: 22401672 2012 Journal of medicinal chemistry

Abstract: Crystal structures at resolutions of 1.25-1.55 A were analyzed for complexes of 1 with the PR containing major drug resistant mutations, PR(I47V), PR(L76V), PR(V82A), and PR(N88D).

Abstract: Mutations of I47V and V82A alter residues in the inhibitor-binding site, while L76V and N88D are distal mutations having no direct contact with the inhibitor.

Abstract: Substitution of a smaller amino acid in PR(I47V) and PR(

HIV-1 protease with 20 mutations exhibits extreme resistance to clinical inhibitors through coordinated structural rearrangements.

PMID: 22404139 2012 Biochemistry

Result: Similarly, mutations in the active site cavity of PR20 (D30N, V32I, I47V and I84V) alter the charge and increase the distance between the flaps and the base of the cavity relative to the values in MDR769 (V82A and I84V).

Prevalence of HIV drug resistance mutation in the northern Indian population after failure of the first line antiretroviral therapy.

PMID: 22716105 2012 Current HIV research

Abstract: PI DRMs were observed in 14/128 (10.9%) patients, with L10I, V82A and L89V being the commonest.

HIV-1 Protease and Substrate Coevolution Validates the Substrate Envelope As the Substrate Recognition Pattern.

PMID: 24348205 2012 Journal of chemical theory and computation

Abstract: In this study, three coevolved protease-substrate complexes (AP2VNC-p1V82A, LP1'Fp1-p6D30N/N88D, and SP3'Np1-p6D30N/N88D) were investigated for structural and dynamic properties by molecular modeling and dynamics simulations.

Conclusion: In this study, structural properties of two drug resistant PR variants (V82A and D30N/N88D) and the substrates that coevolved with these two variants (AP2VNC-p1 and LP1'Fp1-p6/SP3'Np1-p6, respectively) were investigated in conformational ensembles obtained from

HIV-1 integrase resistance among antiretroviral treatment naive and experienced patients from Northwestern Poland.

PMID: 23259737 2012 BMC infectious diseases

Result: It must be noted, that three of the patients with developed drug resistance were heavily experienced with reverse transcriptase (RT) and protease (PR) mutations (patient 1: RT: M41L, K103N, M184V, T215S; PR: L10I; patient 2: PR: M41L, V118I, K103N, M184V, L210W, T215S, RT: L10I,

Low prevalence of transmitted drug resistance in patients newly diagnosed with HIV-1 infection in Sweden 2003-2010.

PMID: 22448246 2012 PloS one

Table: V82A

Differential Flap Dynamics in Wild-type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR Relaxation.

PMID: 23144597 2012 Journal of chemical theory and computation

Abstract: Flap+ is a multi-drug-resistant variant of HIV-1 protease with a combination of mutations at the edge of the active site, within the active site, and in the flaps (L10I, G48V, I54V, V82A).

Introduction: Flap+ is a multi-drug-resistant HIV-1 protease variant with a combination of flap and active site mutations (L10I, G48V, I54V, and V82A) that occur simultaneously in sequences of patients undergoing drug therapy (Figure 1).

Method: As described above, Flap+ contains additional mutations of L10I, G48V, I54V, and

Browser Board

Co-occurred Entities

Filtrator