Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Understanding the co-evolutionary molecular mechanisms of resistance in the HIV-1 Gag and protease.

Journal of biomolecular structure & dynamics - 1 Jan 2022

Marie Veronna, Gordon Michelle

Abstract excerpt

Due to high human immunodeficiency virus type 1 (HIV-1) subtype C infections coupled with increasing antiretroviral treatment failure, the elucidation of complex drug resistance mutational patterns arising through protein co-evolution is required. Despite the inclusion of potent protease inhibitors Lopinavir (LPV) and Darunavir (DRV) in second- and third-line therapies, many patients still fail treatment due to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Darunavir
Share to Drug Resistance, Viral
Share to HIV-1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Infections

Share to HIV Protease

Share to HIV Protease Inhibitors

Share to Mutation

Share to Peptide Hydrolases

Source

Identifiers

PMID: 34253143
DOI: 10.1080/07391102.2021.1950569

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Understanding the co-evolutionary molecular mechanisms of resistance in the HIV-1 Gag and protease.PMID 34253143Read ↗

Structural and dynamical aspects of HIV-1 protease and its role in drug resistance.Semantic proximity Read ↗

Integrative Computational Approaches for Understanding Drug Resistance in HIV-1 Protease Subtype CSemantic proximity Read ↗

Computational simulations of HIV-1 proteases--multi-drug resistance due to nonactive site mutation L90M.Semantic proximity Read ↗

Understanding The Mechanism of Mutant HIV-1 Protease Resistance Against Darunavir Using Molecular Dynamic StudySemantic proximity Read ↗

HIV-1 protease with 10 lopinavir and darunavir resistance mutations exhibits altered inhibition, structural rearrangements and extreme dynamics.Semantic proximity Read ↗

Acquired HIV-1 Protease Conformational Flexibility Associated with Lopinavir Failure May Shape the Outcome of Darunavir Therapy after Antiretroviral Therapy Switch.Semantic proximity Read ↗

An in silico pharmacological approach toward the discovery of potent inhibitors to combat drug resistance HIV‐1 protease variantsSemantic proximity Read ↗

Multiple Molecular Dynamics Simulations of the Inhibitor GRL-02031 Complex with Wild Type and Mutant HIV-1 Protease Reveal the Binding and Drug-Resistance Mechanism.Semantic proximity Read ↗

Evaluating the potency of HIV-1 protease drugs to combat resistance.Semantic proximity Read ↗

Predicting drug resistance of the HIV-1 protease using molecular interaction energy components.Semantic proximity Read ↗

Drug resistance conferred by mutations outside the active site through alterations in the dynamic and structural ensemble of HIV-1 protease.Semantic proximity Read ↗

Non-active site mutants of HIV-1 protease influence resistance and sensitisation towards protease inhibitors.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.