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

Sequence Characterization and Molecular Modeling of Clinically Relevant Variants of the SARS-CoV-2 Main Protease.

Biochemistry - 6 Oct 2020

Cross Thomas J, Takahashi Gemma R, Diessner Elizabeth M, Crosby Marquise G, Farahmand Vesta, Zhuang Shannon, Butts Carter T, Martin Rachel W

Abstract excerpt

The SARS-CoV-2 main protease (Mpro) is essential to viral replication and cleaves highly specific substrate sequences, making it an obvious target for inhibitor design. However, as for any virus, SARS-CoV-2 is subject to constant neutral drift and selection pressure, with new Mpro mutations arising over time. Identification and structural characterization of Mpro variants is thus critical for robust inhibitor...

Read the complete abstract on PubMed

Topics

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

Share to Betacoronavirus
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Drug Discovery

Share to Molecular Structure

Share to Protease Inhibitors

Share to SARS-CoV-2

Share to Sequence Analysis, Protein

Share to Viral Nonstructural Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 32931703
DOI: 10.1021/acs.biochem.0c00462
PMCID: PMC7518256

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

Sequence Characterization and Molecular Modeling of Clinically Relevant Variants of the SARS-CoV-2 Main Protease.PMID 32931703Read ↗

Sequence characterization and molecular modeling of clinically relevant variants of the SARS-CoV-2 main proteaseSemantic proximity Read ↗

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

Evolution of the SARS-CoV-2 main protease under fitness constraints imposed by folding stability and activitySemantic proximity Read ↗

Mutation Effects on Structure and Dynamics: Adaptive Evolution of the SARS-CoV-2 Main Protease.Semantic proximity Read ↗

Identification of mutation resistance coldspots for targeting the SARS-CoV2 main protease.Semantic proximity Read ↗

Defining the substrate envelope of SARS-CoV-2 main protease to predict and avoid drug resistanceSemantic 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 ↗

A systematic mutation analysis of 13 major SARS-CoV-2 variants.Semantic proximity Read ↗

SARS-CoV-2 NSP14 governs mutational instability and assists in making new SARS-CoV-2 variants.Semantic proximity Read ↗

High Throughput Virtual Screening and Validation of a SARS-CoV-2 Main Protease Non-Covalent InhibitorSemantic proximity Read ↗

SARS-CoV-2 NSP14 governs mutational instability and assists in making new SARS-CoV-2 variantsSemantic proximity Read ↗

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

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