Allosteric Inhibition of the SARS‐CoV‐2 Main Protease: Insights from Mass Spectrometry Based Assays**-Reference-Cited by-同舟云学术

Allosteric Inhibition of the SARS‐CoV‐2 Main Protease: Insights from Mass Spectrometry Based Assays**

Published:2020-10-15 Issue:52 Volume:59 Page:23544-23548
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

El‐Baba Tarick J.¹^ORCID,Lutomski Corinne A.¹^ORCID,Kantsadi Anastassia L.²,Malla Tika R.³,John Tobias³,Mikhailov Victor³,Bolla Jani R.¹,Schofield Christopher J.³,Zitzmann Nicole²,Vakonakis Ioannis²^ORCID,Robinson Carol V.¹^ORCID

Affiliation:

1. Physical and Theoretical Chemistry Laboratory University of Oxford South Parks Rd. OX1 3QZ Oxford UK

2. Department of Biochemistry University of Oxford South Parks Rd. OX1 3QU Oxford UK

3. Chemistry Research Laboratory University of Oxford 12 Mansfield Rd OX1 3TA Oxford UK

Funder

Research Councils UK

Wellcome Trust

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.202010316

Reference20 articles.

1. Values taken from:https://coronavirus.jhu.edu.

2. Structure of the RNA-dependent RNA polymerase from COVID-19 virus

4. Structure of Mpro from SARS-CoV-2 and discovery of its inhibitors

5. Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors

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