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

A naturally occurring G11S mutation in the 3C-like protease from the SARS-CoV-2 virus dramatically weakens the dimer interface.

Protein science : a publication of the Protein Society - 1 Jan 2024

Wang Guanyu, Venegas Felipe A, Rueda Andres M, Weerasinghe Nuwani W, Uggowitzer Kevin A, Thibodeaux Christopher J, Moitessier Nicolas, Mittermaier Anthony K

Abstract excerpt

The 3C-like protease (3CLpro ) is crucial to the replication of SARS-CoV-2, the causative agent of COVID-19, and is the target of several successful drugs including Paxlovid and Xocova. Nevertheless, the emergence of viral resistance underlines the need for alternative drug strategies. 3CLpro only functions as a homodimer, making the protein-protein interface an attractive drug target. Dimerization is partly...

Read the complete abstract on PubMed

Topics

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

Share to Antiviral Agents
Share to COVID-19

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine Endopeptidases

Share to Mutation

Share to Peptide Hydrolases

Share to SARS-CoV-2

Source

Open in PubMed Open full text

Identifiers

PMID: 38058248
DOI: 10.1002/pro.4857
PMCID: PMC10731504

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

A naturally occurring G11S mutation in the 3C-like protease from the SARS-CoV-2 virus dramatically weakens the dimer interface.PMID 38058248Read ↗

Inhibitor-induced dimerization mediates lufotrelvir resistance in mutants of SARS-CoV-2 3C-like protease.Semantic proximity Read ↗

Mutation of Asn28 disrupts the dimerization and enzymatic activity of SARS 3CL(pro) .Semantic proximity Read ↗

Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure.Semantic proximity Read ↗

3-Chymotrypsin-like Protease (3CLpro): Validation as a Molecular Target, Proposal of a Novel Catalytic Mechanism, and Inhibitors in Preclinical and Clinical TrialsSemantic proximity Read ↗

Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations.Semantic proximity Read ↗

Targeting the Dimerization of the Main Protease of Coronaviruses: A Potential Broad-Spectrum Therapeutic Strategy.Semantic proximity Read ↗

Resistance mechanisms of SARS-CoV-2 3CLpro to the non-covalent inhibitor WU-04Semantic proximity Read ↗

Resistance mechanisms of SARS-CoV-2 3CLpro to the non-covalent inhibitor WU-04Semantic proximity Read ↗

Development of small molecule non-covalent coronavirus 3CL protease inhibitors from DNA-encoded chemical library screeningSemantic proximity Read ↗

Mechanistic Insights into the Mutational Landscape of the Main Protease/3CLPro and Its Impact on Long-Term COVID-19/SARS-CoV-2 ManagementSemantic proximity Read ↗

SARS-CoV-2 main protease (M-pro) mutational profiling: An insight into mutation coldspots.Semantic proximity Read ↗

Cooperativity and communication between the active sites of the dimeric SARS-CoV-2 main protease.Semantic proximity Read ↗

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