Discovery, Synthesis, And Structure-Based Optimization of a Series of N-(tert-Butyl)-2-(N-arylamido)-2-(pyridin-3-yl) Acetamides (ML188) as Potent Noncovalent …

J Jacobs, V Grum-Tokars, Y Zhou… - Journal of medicinal …, 2013 - ACS Publications
A high-throughput screen of the NIH molecular libraries sample collection and subsequent
optimization of a lead dipeptide-like series of severe acute respiratory syndrome (SARS) …

Mechanism of the maturation process of SARS-CoV 3CL protease*[boxs]

MF Hsu, CJ Kuo, KT Chang, HC Chang… - Journal of Biological …, 2005 - ASBMB
Severe acute respiratory syndrome (SARS) is an emerging infectious disease caused by a
novel human coronavirus. Viral maturation requires a main protease (3CL pro) to cleave the …

Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase

K Fan, P Wei, Q Feng, S Chen, C Huang, L Ma… - Journal of Biological …, 2004 - ASBMB
The 3C-like proteinase of severe acute respiratory syndrome (SARS) coronavirus has been
proposed to be a key target for structural-based drug design against SARS. In order to …

Overview of antiviral drug candidates targeting coronaviral 3C‐like main proteases

CC Chen, X Yu, CJ Kuo, J Min, S Chen, L Ma… - The FEBS …, 2021 - Wiley Online Library
Coronaviruses (CoVs) are positive single‐stranded RNA viruses that cause severe
respiratory syndromes in humans, including severe acute respiratory syndrome (SARS) and …

Identification of Novel Inhibitors of the SARS Coronavirus Main Protease 3CLpro

U Bacha, J Barrila, A Velazquez-Campoy… - Biochemistry, 2004 - ACS Publications
SARS (severe acute respiratory syndrome) is caused by a newly discovered coronavirus. A
key enzyme for the maturation of this virus and, therefore, a target for drug development is …

Evaluating the 3C-like protease activity of SARS-Coronavirus: recommendations for standardized assays for drug discovery

V Grum-Tokars, K Ratia, A Begaye, SC Baker… - Virus research, 2008 - Elsevier
Although the initial outbreaks of the deadly coronavirus that causes severe acute respiratory
syndrome (SARS-CoV) were controlled by public health measures, the development of …

The catalysis of the SARS 3C‐like protease is under extensive regulation by its extra domain

J Shi, J Song - The FEBS journal, 2006 - Wiley Online Library
The 3C‐like protease of the severe acute respiratory syndrome (SARS) coronavirus has a C‐
terminal extra domain in addition to the chymotrypsin‐fold adopted by piconavirus 3C …

[HTML][HTML] Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure

T Hu, Y Zhang, L Li, K Wang, S Chen, J Chen, J Ding… - Virology, 2009 - Elsevier
The 3C-like protease of SARS coronavirus (SARS-CoV 3CLpro) is vital for SARS-CoV
replication and is a promising drug target. It has been extensively proved that only the …

Crystal structures reveal an induced-fit binding of a substrate-like Aza-peptide epoxide to SARS coronavirus main peptidase

TW Lee, MM Cherney, J Liu, KE James… - Journal of molecular …, 2007 - Elsevier
The SARS coronavirus main peptidase (SARS-CoV Mpro) plays an essential role in the life-
cycle of the virus and is a primary target for the development of anti-SARS agents. Here, we …

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 …