The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor

By Haitao Yang, Maojun Yang, Yi Ding, Yiwei Liu, Z. Lou, Zhe Zhou, Lei Sun, L. Mo, S. Ye, H. Pang and 5 more. Proceedings of the National Academy of Sciences of the United States of America, 2003

933 citations recorded by the source corpus.

Subfields: Animal Science and Zoology, Infectious Diseases

View Paper: https://www.semanticscholar.org/paper/b77f5ee571bcc1a44663db2c185a931ebac4b38a

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Citations in the corpus

Coronavirus Pathogenesis and the Emerging Pathogen Severe Acute Respiratory Syndrome Coronavirus (2005, background): “The use of antiviral antibodies (discussed above and below), entry inhibitors (22, 193), proteinase inhibitors (194, 195, 347), calpain inhibitors (9), human immunodeficiency virus type 1 protease inhibitors (53), nucleoside analogues (such as ribavirin), interferons, and short interfering RNAs has ”
Novel 2019 coronavirus structure, mechanism of action, antiviral drug promises and rule out against its treatment (2020, background): “The second region of the COVID-19 M pro is the favorable position for the inhibitors binding(Yang et al., 2003; Zhao et al., 2008).”
Structural basis of SARS-CoV-2 3CLpro and anti-COVID-19 drug discovery from medicinal plants (2020, positive): “Among these screened phytochemicals, 5,7,30,40-tetrahydroxy-2’-(3,3dimethylallyl) isoflavone is an isoflavone extracted from Psorothamnus arborescens [38] that exhibited the highest binding affinity ( 29.57 kcal/mol) and docking score (S ¼ 16.35), and formed strong hydrogen bonds with the catalytic ”
Boceprevir, GC-376, and calpain inhibitors II, XII inhibit SARS-CoV-2 viral replication by targeting the viral main protease (2020, background): “Previously, SARS-CoV M and SARS-CoV-2 M crystal structures have been solved most frequently as one protomer per ASU, and occasionally a dimer.(8,10,11,21,22) In its native state, M requires dimerization to become catalytically active(23,24), which is supported by our native MS data (Supplementary in”
Structure-based design of antiviral drug candidates targeting the SARS-CoV-2 main protease (2020, methodology): “Recombinant SARS-CoV-2 M pro was expressed and purified from Escherichia coli (E. coli) (18, 25) .”
Severe Acute Respiratory Syndrome Coronavirus as an Agent of Emerging and Reemerging Infection (2007, neutral): “Orf1a/b nsp1 (180) Expression promoted degradation of host endogenous mRNAs, which may inhibit host protein synthesis and prevented endogenous IFN- mRNA accumulation (167) Induce CCL5, CXCL10 (IP10), and CCL3 expression in human lung epithelial cells via activation of NFB; increases cellular RNA deg”
The SARS-CoV-2 main protease as drug target (2020, positive): “Amongst the coronaviral targets that have been studied in the past, the main protease (Mpro, 3CLpro, nsp5) received major attention,25,56 particularly following the first SARS-CoV outbreak in the early 2000s.(23,57) Alternative coronaviral targets include the spike protein (S), RNA-de-”
Nidovirales: Evolving the largest RNA virus genome (2006, background): “The crystal structures of oronavirus and arterivirus 3CLpros revealed that both groups f enzymes have a three-domain structure, with domains I and I forming a (chymotrypsin-like) two-ß-barrel fold consisting f 12 or 13 ß-strands (Anand et al., 2002, 2003; Barrette-Ng t al., 2002; Yang et al., 2003).”
The Molecular Biology of Coronaviruses (2006, background): “Crystal structures have been solved for M pro for HCoV-229E (Anand et al., 2002) , TGEV , and SARS-CoV (Yang et al., 2003) .”
Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors (2020, result): “This phenomenon has also been observed with the SARS-CoV M (12) and is consistent with the halfsite activity described for this enzyme (13).”
Computational studies of drug repurposing and synergism of lopinavir, oseltamivir and ritonavir binding with SARS-CoV-2 protease against COVID-19 (2020, background): “Mpro is highly conserved among Coronaviridae members such as SARS-CoV and MERS-CoV, exhibiting 40 – 44% of sequence homology (Yang et al., 2003).”
From SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug design (2014, background): “The first structure of the free SARS-CoV M pro [36] was determined from crystals that had been grown at acidic pH (around 6.0); in this structure, one monomer of the M pro dimer was in the active state and the other one in a catalytically incompetent conformation in which the S1 specificity pocket a”