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

Computational mutation scanning and drug resistance mechanisms of HIV-1 protease inhibitors.

The journal of physical chemistry. B - 29 Jul 2010

Hao Ge-Fei, Yang Guang-Fu, Zhan Chang-Guo

Abstract excerpt

The drug resistance of various clinically available HIV-1 protease inhibitors has been studied using a new computational protocol, that is, computational mutation scanning (CMS), leading to valuable insights into the resistance mechanisms and structure-resistance correction of the HIV-1 protease inhibitors associated with a variety of active site and nonactive site mutations. By using the CMS method, the...

Read the complete abstract on PubMed

Topics

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

Share to Computational Biology
Share to Drug Resistance, Viral
Share to HIV-1

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Protease

Share to HIV Protease Inhibitors

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 20604558
DOI: 10.1021/jp102546s
PMCID: PMC2916083

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Computational mutation scanning and drug resistance mechanisms of HIV-1 protease inhibitors.PMID 20604558Read ↗

Drug resistance mechanisms of three mutations V32I, I47V and V82I in HIV-1 protease toward inhibitors probed by molecular dynamics simulations and binding free energy predictionsSemantic proximity Read ↗

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

Assessment of a Computational Approach to Predict Drug Resistance Mutations for HIV, HBV and SARS-CoV-2.Semantic proximity Read ↗

Structural analyses of 2015-updated drug-resistant mutations in HIV-1 protease: an implication of protease inhibitor cross-resistance.Semantic proximity Read ↗

Computational Estimation of Residues Involving Resistance to the SARS-CoV-2 Main Protease Inhibitor Ensitrelvir Based on Virtual Alanine Scan of the Active Site.Semantic proximity Read ↗

Characterizing drug resistance using geometric ensembles from HIV protease dynamicsSemantic proximity Read ↗

Prediction and molecular field view of drug resistance in HIV-1 protease mutants.Semantic proximity Read ↗

Computational study of protein specificity: the molecular basis of HIV-1 protease drug resistance.Semantic proximity Read ↗

A Comparative Insight into Amprenavir Resistance of Mutations V32I, G48V, I50V, I54V, and I84V in HIV-1 Protease Based on Thermodynamic Integration and MM-PBSA Methods.Semantic 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 ↗

Some insights into mechanism for binding and drug resistance of wild type and I50V V82A and I84V mutations in HIV-1 protease with GRL-98065 inhibitor from molecular dynamic simulations.Semantic proximity Read ↗

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

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