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

Contributions of Hyperactive Mutations in Mpro from SARS-CoV-2 to Drug Resistance.

ACS infectious diseases - 12 Apr 2024

Flynn Julia M, Zvornicanin Sarah N, Tsepal Tenzin, Shaqra Ala M, Kurt Yilmaz Nese, Jia Weiping, Moquin Stephanie, Dovala Dustin, Schiffer Celia A, Bolon Daniel N A

Abstract excerpt

The appearance and spread of mutations that cause drug resistance in rapidly evolving diseases, including infections by the SARS-CoV-2 virus, are major concerns for human health. Many drugs target enzymes, and resistance-conferring mutations impact inhibitor binding or enzyme activity. Nirmatrelvir, the most widely used inhibitor currently used to treat SARS-CoV-2 infections, targets the main protease (Mpro)...

Read the complete abstract on PubMed

Topics

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

Share to COVID-19
Share to Drug Resistance

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lactams

Share to Leucine

Share to Mutation

Share to Nitriles

Share to Saccharomyces cerevisiae

Share to SARS-CoV-2

Source

Open in PubMed Open full text

Identifiers

PMID: 38472113
DOI: 10.1021/acsinfecdis.3c00560
PMCID: PMC11179160

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Contributions of Hyperactive Mutations in Mpro from SARS-CoV-2 to Drug Resistance.PMID 38472113Read ↗

Contributions of hyperactive mutations in M <sup>pro</sup> from SARS-CoV-2 to drug resistanceSemantic proximity Read ↗

Functional and Structural Characterization of Treatment-Emergent Nirmatrelvir Resistance Mutations at Low Frequencies in the Main Protease (Mpro) Reveals a Unique Evolutionary Route for SARS-CoV-2 to Gain ResistanceSemantic proximity Read ↗

Naturally Occurring Mutations of SARS-CoV-2 Main Protease Confer Drug Resistance to NirmatrelvirSemantic proximity Read ↗

Molecular mechanisms of SARS-CoV-2 resistance to nirmatrelvir.Semantic proximity Read ↗

Comprehensive fitness landscape of SARS-CoV-2 Mpro reveals insights into viral resistance mechanismsSemantic proximity Read ↗

Hotspot residues and resistance mutations in the nirmatrelvir-binding site of SARS-CoV-2 main protease: Design, identification, and correlation with globally circulating viral genomes.Semantic proximity Read ↗

A yeast-based system to study SARS-CoV-2 Mpro structure and to identify nirmatrelvir resistant mutations.Semantic proximity Read ↗

Comprehensive fitness landscape of SARS-CoV-2 M <sup>pro</sup> reveals insights into viral resistance mechanismsSemantic proximity Read ↗

A yeast-based system to study SARS-CoV-2 Mpro structure and to identify nirmatrelvir resistant mutationsSemantic proximity Read ↗

A SARS-CoV-2 Mpro mutation conferring ensitrelvir resistance paradoxically increases nirmatrelvir susceptibilitySemantic proximity Read ↗

Naturally occurring mutations of SARS-CoV-2 main protease confer drug resistance to nirmatrelvirSemantic proximity Read ↗

Systematic analyses of the resistance potential of drugs targeting SARS-CoV-2 main proteaseSemantic proximity Read ↗

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