Irreversible inhibitors of serine, cysteine, and threonine proteases.

By J. Powers, Juliana L. Asgian, O. Ekici, K. James. 2002

948 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Plant Science

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In Molecular Biology

1. Paul V. Fish

Citations in the corpus

• Designed switch from covalent to non-covalent inhibitors of carboxylesterase Notum activity (2023, background): “A number of ‘warheads ’ have been created that react selectively with the activated, catalytic serine residue in either a reversible or irreversible covalent manner and usually mimic a substrate transition state [18,20].”
• Strategies for Tuning the Selectivity of Chemical Probes that Target Serine Hydrolases (2020, background): “For example, a P1 tyrosine or phenylalanine biases selectivity of the diphenyl phosphonate toward chymotrypsinlike proteases, while a P1 arginine results in labeling of trypsinlike proteases (Powers et al., 2002).”