Inhibitor binding influences the protonation states of histidines in SARS-CoV-2 main protease
Inhibitor binding influences the protonation states of histidines in SARS-CoV-2 main protease
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Author / Creator
Pavlova, Anna , Lynch, Diane L , Daidone, Isabella , Zanetti-Polzi, Laura , Smith, Micholas Dean , Chipot, Chris , Kneller, Daniel W , Kovalevsky, Andrey , Coates, Leighton , Golosov, Andrei A , Dickson, Callum J , Velez-Vega, Camilo , Duca, José S , Vermaas, Josh V , Pang, Yui Tik , Acharya, Atanu , Parks, Jerry M , Smith, Jeremy C and Gumbart, James C
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
Journal title
Language
English
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Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Contents
Abstract The main protease (Mpro) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is an attractive target for antiviral therapeutics. Recently, many high-resolution apo and inhibitor-bound structures of Mpro, a cysteine protease, have been determined, facilitating structure-based drug design. Mpro plays a central role in the viral l...
Alternative Titles
Full title
Inhibitor binding influences the protonation states of histidines in SARS-CoV-2 main protease
Authors, Artists and Contributors
Author / Creator
Lynch, Diane L
Daidone, Isabella
Zanetti-Polzi, Laura
Smith, Micholas Dean
Chipot, Chris
Kneller, Daniel W
Kovalevsky, Andrey
Coates, Leighton
Golosov, Andrei A
Dickson, Callum J
Velez-Vega, Camilo
Duca, José S
Vermaas, Josh V
Pang, Yui Tik
Acharya, Atanu
Parks, Jerry M
Smith, Jeremy C
Gumbart, James C
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Primary Identifiers
Record Identifier
TN_cdi_proquest_journals_2508259887
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2508259887
Other Identifiers
ISSN
2692-8205
E-ISSN
2692-8205
DOI
10.1101/2020.09.07.286344
