N-terminal autoprocessing from its polyprotein precursor enables creating the mature-like
stable dimer interface of SARS-CoV-2 main protease (MPro), concomitant with the active site …

SARS-CoV-2 is the causative agent of COVID-19. The dimeric form of the viral M pro is
responsible for the cleavage of the viral polyprotein in 11 sites, including its own N and C …

The SARS‐CoV‐2 main protease (Mpro) cleaves along the two viral polypeptides to release
non‐structural proteins required for viral replication. MPro is an attractive target for antiviral …

We recently demonstrated that inhibitor binding reorganizes the oxyanion loop of a
monomeric catalytic domain of SARS CoV-2 main protease (MPro) from an unwound (E) to a …

SARS-CoV-2 constantly circulates and evolves worldwide, generating many variants and
posing a menace to global health. It is urgently needed to discover effective medicines to …

β-coronavirus (CoVs) alone has been responsible for three major global outbreaks in the
21st century. The current crisis has led to an urgent requirement to develop therapeutics …

The design of effective target-specific drugs for COVID-19 treatment has become an
intriguing challenge for modern science. The SARS-CoV-2 main protease, Mpro …

The SARS-CoV-2 pandemic has rapidly spread across the globe, posing an urgent health
concern. Many quests to computationally identify treatments against the virus rely on in silico …

Besides vaccines, the development of antiviral drugs targeting SARS-CoV-2 is critical for
stopping the current COVID-19 pandemic and preventing future outbreaks. The SARS-CoV …

The coronavirus main protease (Mpro) is required for viral replication and has enzymatical
activity as a homodimer. Thus, targeting its dimerization is an effective strategy for …