Y. R. Alugubelli

This paper develops first-in-class PROTAC degraders of SARS-CoV-2 main protease, showing they reduce MPro levels and exhibit anti-SARS-CoV-2 activity.

This study develops an azapeptide platform with covalent warheads to identify potent SARS-CoV-2 MPro inhibitors, including MPI89 with a 10 nM EC50 and high selectivity.

This study systematically evaluates dipeptidyl inhibitors of SARS-CoV-2 main protease, identifying compounds with high antiviral potency and low cytotoxicity.

This paper develops PADLE, a phage-assisted method to evolve potent HDAC8 inhibitors, identifying two highly selective and potent inhibitors with sub-nanomolar Ki values.

This study constructs and validates a phage-displayed macrocyclic peptide library using regioselective chemical reactions and identifies a potent SARS-CoV-2 neutralizing peptide through epitope-directed selection.

This paper identifies that a P4 N-terminal carbamate in boceprevir-based inhibitors is crucial for high antiviral potency against SARS-CoV-2.

The paper evaluates MPro inhibitors for SARS-CoV-2, finding MPI8 selectively inhibits both MPro and host cathepsin L, enhancing antiviral efficacy with reduced toxicity.

This paper evaluates the cellular potency of SARS-CoV-2 MPro inhibitors using a fluorescent flow cytometry assay, revealing that most inhibitors have weak cellular activity despite strong antiviral effects.

This study designs and synthesizes potent SARS-CoV-2 main protease inhibitors, with some showing IC50 values below 100 nM and high virus inhibition potency in cell assays.