The main protease (M pro) of SARS-CoV-2 is an attractive target in anti-COVID-19 therapy
for its high conservation and major role in the virus life cycle. The covalent M pro inhibitor …

Emerging SARS-CoV-2 variants continue to threaten the effectiveness of COVID-19
vaccines, and small-molecule antivirals can provide an important therapeutic treatment …

The monomeric catalytic domain (residues 1–199) of SARS-CoV-2 main protease (MPro1-
199) fused to 25 amino acids of its flanking nsp4 region mediates its autoprocessing at the …

Viral proteases are an important target for drug development, since they can modulate vital
pathways in viral replication, maturation, assembly and cell entry. With the (re) appearance …

Abstract SARS‐CoV‐2 (SCoV2) and its variants of concern pose serious challenges to the
public health. The variants increased challenges to vaccines, thus necessitating for …

A critical step for SARS-CoV-2 assembly and maturation involves the autoactivation of the
main protease (MProWT) from precursor polyproteins. Upon expression, a model precursor …

Designing proteins with improved functions requires a deep understanding of how
sequence and function are related, a vast space that is hard to explore. The ability to …

Considering the significant impact of the recent COVID-19 outbreak, development of broad-
spectrum antivirals is a high priority goal to prevent future global pandemics. Antiviral …

Misfolding of antibody light chains can lead to systemic light chain amyloidosis, which is
associated with misfolding and aggregation. The antibody light chain may engage in 3D …

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 …