''Mapping the Cysteine Redoxome''

Prof Jing Yang

National Center for Protein Sciences      

CHINA

Thursday, December 22, 2022
11:00

The nucleophilic thiol group (Cys-SH) allows cysteine to undergo a broad range of redox modifications, such as sulfenylation (Cys-SOH), sulfinylation (Cys-SO2H). Emerging evidence suggests that cysteine redox modifications are well-controlled, site-specific cellular events, which play important roles in regulating many biological processes, such as autophagy, cellular metabolism, inflammation, cell cycle and cell death under physiological and pathological contexts. Efforts to understand their underlying mechanisms have been hampered due to limitations of methods for globally analyzing site-specific protein targets and redox dynamics. We have recently developed several chemoproteomic approaches to globally map and to quantify Cys-SH, Cys-SOH and Cys-SO2H in complex proteomes, providing versatile opportunities to study cysteine-mediated redox networks in a range of biological processes and adaptive responses in physiology and pathophysiology.

Jozef Schell seminar room
Technologiepark 71 - 9052 

Genome editing, cutting-edge technology for a sustainable agriculture