Ching-Cheng Hsueh

TL;DR: This study presents the structure of IDO1 in complex with 24, a NLG919 analogue with potent activity and demonstrates that extensive hydrophobic interactions and the unique hydrogen bonding network contribute to the great potency of imidazoleisoindole derivatives.

TL;DR: A structure-activity relationship study of this compound resulted in the potent IDO1 inhibitor 1-(4-cyanophenyl)-3-(3-(cyclopropylethynyl)imidazo[2,1-b]thiazol-5-yl)thiourea 47 (hIDO IC50 = 16.4 nM).

TL;DR: To the best of the knowledge, it is the first structural evidence demonstrating how a compound can inhibit the activated c-KIT by switching back to its inactive state through a sequence of conformational changes.

TL;DR: In this article, the structure of MTHFD2 in complex with xanthine derivative 15, which allosterically binds to the enzyme and coexists with the substrate analogue, was presented.

TL;DR: A multitargeted tyrosine kinase inhibitor, compound 15a, with potent inhibition against single or double mutations of c-KIT developed in GISTs is discovered, and crystal structure analysis revealed the unique binding mode of 15a with c- KIT and may elucidate its high potency in inhibiting c-kIT kinase activity.