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Updated: Jun 19, 2026

06:17
Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay
Published on: February 28, 2025
Discovery of covalent inhibitors for MIF tautomerase via cocrystal structures with phantom hits from virtual
Larry R McLean1, Ying Zhang, Hua Li
1Discovery Research, sanofi-aventis, Bridgewater, NJ 08807, USA. Larry.Mclean@sanofi-aventis.com
Bioorganic & Medicinal Chemistry Letters
|October 20, 2009
Abstract:
Biochemical and X-ray crystallographic studies confirmed that hydroxyquinoline derivatives identified by virtual screening were actually covalent inhibitors of the MIF tautomerase. Adducts were formed by N-alkylation of the Pro-1 at the catalytic site with a loss of an amino group of the inhibitor.

