Regulation of the Dimerization and Activity of SARS-CoV-2 Main Protease through Reversible Glutathionylation of Cysteine 300
SARS-CoV-2 encodes main protease (Mpro), an attractive target for therapeutic interventions. We show Mpro is susceptible to glutathionylation leading to inhibition of dimerization and activity. Activity of glutathionylated Mpro could be restored with reducing agents or glutaredoxin. Analytical studi...
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Published in | bioRxiv |
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Main Authors | , , , , , , , , |
Format | Journal Article Paper |
Language | English Japanese |
Published |
United States
Cold Spring Harbor Laboratory
12.04.2021
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Edition | 1.2 |
Subjects | |
Online Access | Get full text |
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