Article

Distal Protein-Protein Interactions Contribute to SARS-CoV-2 Main Protease Substrate Binding and Nirmatrelvir Resistance

2024-04-02

Abstract excerpt

SARS-CoV-2 main protease, M pro , is responsible for the processing of the viral polyproteins into individual proteins, including the protease itself. M pro is a key target of anti-COVID-19 therapeutics such as nirmatrelvir (the active component of Paxlovid). Resistance mutants identified clinically and in viral passage assays contain a combination of active site mutations (e.g. E166V, E166A, L167F), which reduc...

Topics

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

Identifiers and source

Literature Corpus work: 8ee4683f-5dd7-56f4-8ffc-201e73092fb6
DOI: 10.1101/2024.04.01.587566

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Distal Protein-Protein Interactions Contribute to SARS-CoV-2 Main Protease Substrate Binding and Nirmatrelvir ResistanceDOI 10.1101/2024.04.01.587566Read

Molecular mechanisms of drug resistance and compensation in SARS-CoV-2 main protease: the interplay between E166 and L50.Semantic 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

A yeast-based system to study SARS-CoV-2 M <sup>pro</sup> structure and to identify nirmatrelvir resistant mutationsSemantic proximity Read

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

Structural basis for varying drug resistance of SARS-CoV-2 Mpro E166 variants.Semantic proximity Read

Effects of SARS-CoV-2 Main Protease Mutations at Positions L50, E166, and L167 Rendering Resistance to Covalent and Noncovalent Inhibitors.Semantic proximity Read

Evolutionary and Structural Insights about Potential SARS-CoV-2 Evasion of NirmatrelvirSemantic 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

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

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

Structural basis of nirmatrelvir and ensitrelvir activity against naturally occurring polymorphisms of the SARS-CoV-2 main proteaseSemantic proximity Read