S. Munshi

This study identifies novel SIRT3 activators that restore catalytic activity under NAD+ depletion, offering potential therapeutic applications for age-related diseases.

The paper identifies a thermally accessible folded excited state in the intrinsically disordered bacterial transcription factor CytR, showing it binds DNA via a folding-before-binding conformational selection mechanism.

The paper tests small-molecule ligands against -1 PRF in coronaviruses, finding nafamostat inhibits frameshifting in multiple bat CoVs and SARS-CoV-2 but not other viruses.

The paper investigates the structural dynamics of the SARS-CoV-2 frameshift-stimulatory pseudoknot under tension, revealing multiple conformers and their folding mechanisms.

This study reveals that Fn1 fibrils are composed of nanodomains rather than continuous fibers, using live imaging and SMLM to challenge the traditional view.

The paper examines how natural mutations in the SARS-CoV-2 pseudoknot affect −1 PRF efficiency and the activity of anti-frameshifting ligands, finding that ligand activity remains resistant to most mutations.

The paper characterizes small molecules that nonallosterically activate SIRT3, identifying honokiol as a hit compound through computational and biochemical methods.

This paper identifies a general mechanism-based approach for activating sirtuin enzymes, challenges existing activation modes, and evaluates reported compounds for validity.