Targeting the dimerization of the main protease of coronaviruses: a potential broad-spectrum therapeutic strategy
A new coronavirus (CoV) caused a pandemic named COVID-19, which has become a
global health care emergency in the present time. The virus is referred to as SARS-CoV-2 …
global health care emergency in the present time. The virus is referred to as SARS-CoV-2 …
Feline coronavirus drug inhibits the main protease of SARS-CoV-2 and blocks virus replication
The main protease, Mpro (or 3CLpro) in SARS-CoV-2 is a viable drug target because of its
essential role in the cleavage of the virus polypeptide. Feline infectious peritonitis, a fatal …
essential role in the cleavage of the virus polypeptide. Feline infectious peritonitis, a fatal …
Mutation of Glu-166 blocks the substrate-induced dimerization of SARS coronavirus main protease
SC Cheng, GG Chang, CY Chou - Biophysical journal, 2010 - cell.com
The maturation of SARS coronavirus involves the autocleavage of polyproteins 1a and 1ab
by the main protease (Mpro) and a papain-like protease; these represent attractive targets …
by the main protease (Mpro) and a papain-like protease; these represent attractive targets …
Characterization of alternate encounter assemblies of SARS-CoV-2 main protease
A Aniana, NT Nashed, R Ghirlando, VN Drago… - Journal of Biological …, 2024 - jbc.org
The assembly of two monomeric constructs spanning segments 1-199 (MPro 1-199) and 10-
306 (MPro 10-306) of SARS-CoV-2 main protease (MPro) was examined to assess the …
306 (MPro 10-306) of SARS-CoV-2 main protease (MPro) was examined to assess the …
SARS-CoV-2 Mpro responds to oxidation by forming disulfide and NOS/SONOS bonds
PYA Reinke, R Schubert, D Oberthür… - Nature …, 2024 - nature.com
The main protease (Mpro) of SARS-CoV-2 is critical for viral function and a key drug target.
Mpro is only active when reduced; turnover ceases upon oxidation but is restored by re …
Mpro is only active when reduced; turnover ceases upon oxidation but is restored by re …
Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode
The main protease (M pro) plays a vital role in proteolytic processing of the polyproteins in
the replicative cycle of SARS coronavirus (SARS-CoV). Dimerization of this enzyme has …
the replicative cycle of SARS coronavirus (SARS-CoV). Dimerization of this enzyme has …
Domain swapping: a mathematical model for quantitative assessment of structural effects
I Roterman, K Stapor, D Dułak, L Konieczny - FEBS Open Bio, 2024 - Wiley Online Library
The domain‐swapping mechanism involves the exchange of structural elements within a
secondary or supersecondary structure between two (or more) proteins. The present paper …
secondary or supersecondary structure between two (or more) proteins. The present paper …
Three-dimensional domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main protease
Proteolytic processing of viral polyproteins is indispensible for the lifecycle of coronaviruses.
The main protease (M pro) of SARS-CoV is an attractive target for anti-SARS drug …
The main protease (M pro) of SARS-CoV is an attractive target for anti-SARS drug …
Dynamically-driven inactivation of the catalytic machinery of the SARS 3C-like protease by the N214A mutation on the extra domain
J Shi, N Han, L Lim, S Lua, J Sivaraman… - PLoS computational …, 2011 - journals.plos.org
Despite utilizing the same chymotrypsin fold to host the catalytic machinery, coronavirus 3C-
like proteases (3CLpro) noticeably differ from picornavirus 3C proteases in acquiring an …
like proteases (3CLpro) noticeably differ from picornavirus 3C proteases in acquiring an …