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Open AccessJournal ArticleDOI

Zinc2+ ion inhibits SARS-CoV-2 main protease and viral replication in vitro.

TLDR
In this article, the first crystal structure of the Mpro-Zn2+ complex at 1.9 A was presented and provided the structural basis of viral replication inhibition, which showed that zinc not only inhibits the SARS-CoV-2 main protease (Mpro) with nanomolar affinity, but also viral replication.
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This article is published in Chemical Communications.The article was published on 2021-09-30 and is currently open access. It has received 27 citations till now. The article focuses on the topics: Viral replication & Protease.

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Inhibition of the main protease of SARS-CoV-2 (Mpro) by repurposing/designing drug-like substances and utilizing nature’s toolbox of bioactive compounds

TL;DR: The main protease (Mpro) of the virus is an appealing target for the development of inhibitors, due to its importance in the viral life cycle and its high conservation among different coronaviruses as mentioned in this paper .
Journal ArticleDOI

Advances in the Development of SARS-CoV-2 Mpro Inhibitors

TL;DR: A huge effort was then carried out by the scientific community to design, synthesize and test new small molecules acting as inactivators of SARS-CoV-2 Mpro as mentioned in this paper .
Journal ArticleDOI

The Effect of Circulating Zinc, Selenium, Copper and Vitamin K1 on COVID-19 Outcomes: A Mendelian Randomization Study

TL;DR: In this article , the authors employed a two-sample Mendelian Randomization (MR) analysis to test whether genetically predicted zinc, selenium, copper and vitamin K1 levels have a causal effect on COVID-19 related outcomes, including risk of infection, hospitalization and critical illness.
Journal ArticleDOI

The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (M<sup>pro</sup>)

- 17 Aug 2022 - 
TL;DR: In this paper , a series of high-resolution crystal structures of unliganded SARS-CoV-2 main protease, or Mpro, were obtained at different tem-per-atures from cryogenic to physiological.
Posted ContentDOI

The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (M pro )

TL;DR: X-ray crystallography at variable temperature for SARS-CoV-2 M pro reveals a complex conformational landscape, including mobile solvent at the catalytic dyad, mercurial conformational heterogeneity in a key substrate-binding loop, and an intramolecular network bridging the active site and dimer interface.
References
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Journal ArticleDOI

A new coronavirus associated with human respiratory disease in China.

TL;DR: Phylogenetic and metagenomic analyses of the complete viral genome of a new coronavirus from the family Coronaviridae reveal that the virus is closely related to a group of SARS-like coronaviruses found in bats in China.
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Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors

TL;DR: The pharmacokinetic characterization of the optimized inhibitor reveals a pronounced lung tropism and suitability for administration by the inhalative route and work that may provide a basis for development of anticoronaviral drugs.
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Zn2+ inhibits coronavirus and arterivirus RNA polymerase activity in vitro and zinc ionophores block the replication of these viruses in cell culture

TL;DR: It is demonstrated that the combination of Zn2+ and PT at low concentrations reduces the replication of SARS-coronavirus (SARS-CoV) and equine arteritis virus (EAV) in cell culture and efficiently inhibits the RNA-synthesizing activity of the RTCs of both viruses.
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Boceprevir, GC-376, and calpain inhibitors II, XII inhibit SARS-CoV-2 viral replication by targeting the viral main protease.

TL;DR: This study reports the discovery of inhibitors targeting the SARS-CoV-2 main protease (M pro) using the FRET-based enzymatic assay, and indicates that boceprevir, GC-376, and calpain inhibitors II, and XII represent novel chemotypes that are distinct from known substrate-based peptidomimetic M pro inhibitors.
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