Tulsi Upadhyay

This paper identifies a covalent irreversible inhibitor, Z34, that binds to ALDH1A3 in two distinct conformations at the active-site cysteine, showing promise for anticancer drug development.

This study develops a covalent probe for imaging S. aureus biofilms in vitro and in vivo, showing high specificity for the serine hydrolase FphE.

The paper characterizes the structural and ligand-binding properties of Staphylococcus aureus FphE, revealing its unique dimeric structure and substrate engagement mechanisms.

The paper develops fluorescent probes for FphB, a Staphylococcus aureus enzyme, using mRNA display with a genetically encoded electrophile, achieving nanomolar selectivity.

This paper develops a fluorogenic substrate for Chikungunya virus protease (nsP2) that improves signal-to-noise ratio and specificity for inhibitor screening.

The paper develops oxadiazolone-based probes targeting FphE to specifically detect S. aureus infections through covalent modification of the enzyme's active site.