Structures of two coronavirus main proteases: implications for substrate binding and antiviral drug design

X Xue, H Yu, H Yang, F Xue, Z Wu, W Shen, J Li… - Journal of …, 2008 - Am Soc Microbiol
Coronaviruses (CoVs) can infect humans and multiple species of animals, causing a wide
spectrum of diseases. The coronavirus main protease (Mpro), which plays a pivotal role in …

A Patent Review on SARS Coronavirus Main Protease (3CLpro) Inhibitors

CSB Chia, W Xu, P Shuyi Ng - ChemMedChem, 2022 - Wiley Online Library
The severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) pandemic is an
unprecedented global health emergency causing more than 4.2 million fatalities as of 30 …

Substrate Specificity Profiling and Identification of a New Class of Inhibitor for the Major Protease of the SARS Coronavirus,

DH Goetz, Y Choe, E Hansell, YT Chen… - Biochemistry, 2007 - ACS Publications
Severe acute respiratory syndrome (SARS) is an emerging infectious disease associated
with a high rate of mortality. The SARS-associated coronavirus (SARS-CoV) has been …

High-throughput screening identifies inhibitors of the SARS coronavirus main proteinase

JE Blanchard, NH Elowe, C Huitema, PD Fortin… - Chemistry & biology, 2004 - cell.com
The causative agent of severe acute respiratory syndrome (SARS) has been identified as a
novel coronavirus, SARS-CoV. The main proteinase of SARS-CoV, 3CL pro, is an attractive …

Design, synthesis, and evaluation of inhibitors for severe acute respiratory syndrome 3C-like protease based on phthalhydrazide ketones or heteroaromatic esters

J Zhang, HI Pettersson, C Huitema, C Niu… - Journal of medicinal …, 2007 - ACS Publications
The 3C-like protease (3CLpro), which controls the severe acute respiratory syndrome
(SARS) coronavirus replication, has been identified as a potential target for drug design in …

Cinanserin is an inhibitor of the 3C-like proteinase of severe acute respiratory syndrome coronavirus and strongly reduces virus replication in vitro

L Chen, C Gui, X Luo, Q Yang, S Günther… - Journal of …, 2005 - Am Soc Microbiol
ABSTRACT The 3C-like proteinase (3CLpro) of severe acute respiratory syndrome-
associated coronavirus (SARS-CoV) is one of the most promising targets for anti-SARS-CoV …

Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization: biochemical and …

S Chen, L Chen, J Tan, J Chen, L Du, T Sun… - Journal of Biological …, 2005 - ASBMB
Severe acute respiratory syndrome (SARS) coronavirus is a novel human coronavirus and is
responsible for SARS infection. SARS coronavirus 3C-like proteinase (SARS 3CL pro) plays …

Binding mechanism of coronavirus main proteinase with ligands and its implication to drug design against SARS

KC Chou, DQ Wei, WZ Zhong - Biochemical and biophysical research …, 2003 - Elsevier
In order to stimulate the development of drugs against severe acute respiratory syndrome
(SARS), based on the atomic coordinates of the SARS coronavirus main proteinase …

Peptide aldehyde inhibitors challenge the substrate specificity of the SARS-coronavirus main protease

L Zhu, S George, MF Schmidt, SI Al-Gharabli… - Antiviral research, 2011 - Elsevier
SARS coronavirus main protease (SARS-CoV Mpro) is essential for the replication of the
virus and regarded as a major antiviral drug target. The enzyme is a cysteine protease, with …

Inhibitor recognition specificity of MERS-CoV papain-like protease may differ from that of SARS-CoV

H Lee, H Lei, BD Santarsiero, JL Gatuz… - ACS chemical …, 2015 - ACS Publications
The Middle East Respiratory Syndrome coronavirus (MERS-CoV) papain-like protease
(PLpro) blocking loop 2 (BL2) structure differs significantly from that of SARS-CoV PLpro …