Article

Sequence characterization and molecular modeling of clinically relevant variants of the SARS-CoV-2 main protease

2020-05-15

Abstract excerpt

The SARS-CoV-2 main protease (M pro ) 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 selection pressure, with new M pro mutations arising over time. Identification and structural characterization of M pro variants is thus critical for robust inhibitor design. Here we...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 52441906-a424-5fee-9f01-28f21a09fe95
DOI: 10.1101/2020.05.15.097493

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Sequence characterization and molecular modeling of clinically relevant variants of the SARS-CoV-2 main proteaseDOI 10.1101/2020.05.15.097493Read

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

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

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

Structural Basis of the Main Proteases of Coronavirus Bound to Drug Candidate PF-07321332Semantic proximity Read

Structural basis for the inhibition of coronaviral main proteases by PF-00835231Semantic proximity Read

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

Structural basis for the inhibition of coronaviral main proteases by PF-00835231.Semantic proximity Read

Amino acid variants of SARS-CoV-2 papain-like protease have impact on drug bindingSemantic proximity Read

Structure-Based Virtual Screening to Discover Potential Lead Molecules for the SARS-CoV‑2 Main ProteaseSemantic proximity Read

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