Rebecca A. Scheck

This study discovers a new type of glycation crosslink, MIDAL, formed by methylglyoxal in Arg-Arg sites, and presents a platform for studying crosslinking AGEs.

This study identifies a chemical mechanism for argpyrimidine formation from methylglyoxal, showing phosphorylated residues promote APY formation and linking glycation to phosphorylation.

This paper introduces dialAGE, a method to control site-specific glycation in proteins, showing it works in vitro and in living cells.

This study identifies a cyclic arginine adduct as the primary glyoxal-derived AGE, challenging prior assumptions about lysine modification and highlighting experimental condition impacts.

This paper demonstrates the incorporation of two noncanonical amino acids into yeast proteins, enabling chemoselective modification at two distinct sites for applications in biology and drug discovery.