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

Dynamical Nonequilibrium Molecular Dynamics Simulations Identify Allosteric Sites and Positions Associated with Drug Resistance in the SARS-CoV-2 Main Protease

7 Jun 2023

Abstract excerpt

High Resolution Image Download MS PowerPoint Slide The SARS-CoV-2 main protease (M pro ) plays an essential role in the coronavirus lifecycle by catalyzing hydrolysis of the viral polyproteins at specific sites. M pro is the target of drugs, such as nirmatrelvir, though resistant mutants have emerged that threaten drug efficacy. Despite its importance, questions remain on the mechanism of how M pro binds its...

Read the complete abstract on PubMed

Topics

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

Share to Computational Drug Discovery Methods
Share to SARS-CoV-2 and COVID-19 Research
Share to thermodynamics and calorimetric analyses

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 37384148
DOI: 10.1021/jacsau.3c00185

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dynamical Nonequilibrium Molecular Dynamics Simulations Identify Allosteric Sites and Positions Associated with Drug Resistance in the SARS-CoV-2 Main ProteasePMID 37384148Read ↗

A dynamical-nonequilibrium molecular dynamics (D-NEMD) alanine scanning approach for identifying allosteric positions in proteinsSemantic proximity Read ↗

Computational Analysis of Dynamic Allostery and Control in the three SARS-CoV-2 non-structural proteinsSemantic proximity Read ↗

Mutation-Induced Resistance of SARS-CoV-2 Mpro to WU-04 Revealed by Multi-Scale Modeling.Semantic proximity Read ↗

Drug Resistance Mutations Alter Dynamics of Inhibitor-Bound HIV-1 ProteaseSemantic proximity Read ↗

Molecular dynamics and in silico mutagenesis on the reversible inhibitor-bound SARS-CoV-2 Main Protease complexes reveal the role of a lateral pocket in enhancing the ligand affinitySemantic proximity Read ↗

Unveiling Mutation Effects on the Structural Dynamics of the Main Protease from SARS-CoV-2 with Hybrid Simulation MethodsSemantic proximity Read ↗

SARS-CoV-2 main protease mutation analysis via a kinematic method.Semantic proximity Read ↗

Impact of emerging mutations on the dynamic properties the SARS-CoV-2 main protease: an <i>in silico</i> investigationSemantic proximity Read ↗

An Integrative Approach to Dissect the Drug Resistance Mechanism of the H172Y Mutation of SARS-CoV-2 Main ProteaseSemantic proximity Read ↗

Visualizing the Active Site Oxyanion Loop Transition Upon Ensitrelvir Binding and Transient Dimerization of SARS-CoV-2 Main Protease.Semantic proximity Read ↗

Structural Differences In 3C-like protease (Mpro) From SARS-CoV and SARS-CoV-2: Molecular Insights For Drug Repurposing Against COVID-19 Revealed by Molecular Dynamics SimulationsSemantic proximity Read ↗

Dynamical Responses Predict a Distal Site that Modulates Activity in an Antibiotic Resistance EnzymeSemantic proximity Read ↗

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