The SARS‐CoV‐2 main protease (Mpro): Structure, function, and emerging therapies for COVID‐19

Q Hu, Y Xiong, GH Zhu, YN Zhang, YW Zhang… - MedComm, 2022 - Wiley Online Library
The main proteases (Mpro), also termed 3‐chymotrypsin‐like proteases (3CLpro), are a
class of highly conserved cysteine hydrolases in β‐coronaviruses. Increasing evidence has …

Structural biology of SARS-CoV-2 Mpro and drug discovery

Y Duan, H Wang, Z Yuan, H Yang - Current Opinion in Structural Biology, 2023 - Elsevier
Since its outbreak in late 2019, the COVID-19 pandemic has drawn enormous attention
worldwide as a consequence of being the most disastrous infectious disease in the past …

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

GD Noske, E de Souza Silva, MO de Godoy… - Journal of Biological …, 2023 - ASBMB
SARS-CoV-2 is the causative agent of COVID-19. The main viral protease (M pro) is an
attractive target for antivirals. The clinically approved drug nirmatrelvir and the clinical …

Biocompatible wearable electrodes on leaves toward the on-site monitoring of water loss from plants

JA Barbosa, VMS Freitas, LHB Vidotto… - … Applied Materials & …, 2022 - ACS Publications
Impedimetric wearable sensors are a promising strategy for determining the loss of water
content (LWC) from leaves because they can afford on-site and nondestructive quantification …

Modulation of the monomer-dimer equilibrium and catalytic activity of SARS-CoV-2 main protease by a transition-state analog inhibitor

NT Nashed, A Aniana, R Ghirlando… - Communications …, 2022 - nature.com
The role of dimer formation for the onset of catalytic activity of SARS-CoV-2 main protease
(MProWT) was assessed using a predominantly monomeric mutant (MProM). Rates of …

The H163A mutation unravels an oxidized conformation of the SARS-CoV-2 main protease

N Tran, S Dasari, SAE Barwell, MJ McLeod… - Nature …, 2023 - nature.com
The main protease of SARS-CoV-2 (Mpro) is an important target for developing COVID-19
therapeutics. Recent work has highlighted Mpro's susceptibility to undergo redox-associated …

Autoprocessing and oxyanion loop reorganization upon GC373 and nirmatrelvir binding of monomeric SARS-CoV-2 main protease catalytic domain

NT Nashed, DW Kneller, L Coates, R Ghirlando… - Communications …, 2022 - nature.com
The monomeric catalytic domain (residues 1–199) of SARS-CoV-2 main protease (MPro1-
199) fused to 25 amino acids of its flanking nsp4 region mediates its autoprocessing at the …

Open Science Discovery of Potent Non-Covalent SARS-CoV-2 Main Protease Inhibitors

COVID Moonshot Consortium, H Achdout, A Aimon… - BioRxiv, 2020 - biorxiv.org
The COVID-19 pandemic is a stark reminder that a barren global antiviral pipeline has grave
humanitarian consequences. Future pandemics could be prevented by accessible, easily …

Structural and functional characterization of NEMO cleavage by SARS-CoV-2 3CLpro

MA Hameedi, E T. Prates, MR Garvin… - Nature …, 2022 - nature.com
In addition to its essential role in viral polyprotein processing, the SARS-CoV-2 3C-like
protease (3CLpro) can cleave human immune signaling proteins, like NF-κB Essential …

Biochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro

R Yadav, VV Courouble, SK Dey, JJEK Harrison… - Science …, 2022 - science.org
SARS-CoV-2, a human coronavirus, is the causative agent of the COVID-19 pandemic. Its
genome is translated into two large polyproteins subsequently cleaved by viral papain-like …