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

Cooperative effects of drug-resistance mutations in the flap region of HIV-1 protease.

ACS chemical biology - 15 Mar 2013

Foulkes-Murzycki Jennifer E, Rosi Christina, Kurt Yilmaz Nese, Shafer Robert W, Schiffer Celia A

Abstract excerpt

Understanding the interdependence of multiple mutations in conferring drug resistance is crucial to the development of novel and robust inhibitors. As HIV-1 protease continues to adapt and evade inhibitors while still maintaining the ability to specifically recognize and efficiently cleave its substrates, the problem of drug resistance has become more complicated. Under the selective pressure of therapy,...

Read the complete abstract on PubMed

Topics

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

Share to Calorimetry
Share to Drug Resistance, Viral
Share to HIV Protease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutation

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 23252515
DOI: 10.1021/cb3006193
PMCID: PMC3805267

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cooperative effects of drug-resistance mutations in the flap region of HIV-1 protease.PMID 23252515Read ↗

A synergy of activity, stability, and inhibitor-interaction of HIV-1 protease mutants evolved under drug-pressure.Semantic proximity Read ↗

Extreme entropy-enthalpy compensation in a drug-resistant variant of HIV-1 protease.Semantic proximity Read ↗

Differential Flap Dynamics in Wild-Type and a Drug Resistant Variant of HIV-1 Protease Revealed by Molecular Dynamics and NMR RelaxationSemantic proximity Read ↗

An inhibitor-interaction intermediate of HIV-1 protease, revealed by Isothermal Titration Calorimetry and NMR spectroscopySemantic proximity Read ↗

Quantized water access to the HIV-1 protease active site as a proposed mechanism for cooperative mutations in drug affinity.Semantic proximity Read ↗

Evolution of drug resistance drives progressive destabilizations in functionally conserved molecular dynamics of the flap region of the HIV-1 proteaseSemantic proximity Read ↗

Dynamical Network of HIV-1 Protease Mutants Reveals the Mechanism of Drug Resistance and Unhindered Activity.Semantic proximity Read ↗

Highly drug-resistant HIV-1 protease reveals decreased intra-subunit interactions due to clusters of mutations.Semantic proximity Read ↗

Effects of the V82A and I54V mutations on the dynamics and ligand binding properties of HIV-1 protease.Semantic proximity Read ↗

Structural Studies of a Rationally Selected Multi-Drug Resistant HIV-1 Protease Reveal Synergistic Effect of Distal Mutations on Flap Dynamics.Semantic proximity Read ↗

Structural and Thermodynamic Basis of Resistance to HIV-1 Protease Inhibition: Implications for Inhibitor DesignSemantic proximity Read ↗

A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV-1 protease.Semantic proximity Read ↗

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