C. Alicia Padilla

TL;DR: Analysis of the purified recombinant c‐Jun DNA binding domain for redox‐dependent thiol modifications and concomitant changes in DNA binding activity shows that changes in the ratio of reduced to oxidized glutathione provide the potential to oxidize c‐ Jun sulfhydryls by mechanisms that include both protein disulfide formation and S‐glutathiolation.

TL;DR: A shotgun redox proteomic technique has allowed new redox regulated proteins (DAHP and carbamoylphosphate synthases, Doa1p) and to precisely identify target cysteines in a number of known ones.

TL;DR: It is shown that yGrX2 has a specific activity 15 times higher than that of yGrx1, although these two oxidoreductases share 64% identity and 85% similarity with respect to their amino acid sequences, and hypothesize that the substitutions of Ser23 and Gln52 in y Grx1 by Ala23 and Glu52 in YGrx2 modify the capability of the active-site C-terminal cysteine to attack the mixed disulfide

TL;DR: Results indicate that GRX2 contains two in-frame start codons, and that translation from the first AUG results in a product that is targeted to mitochondria.

TL;DR: The results show that a plethora of GrX2 subcellular localizations could spread its antioxidant functions all over the cell, but one single Ala to Gly mutation converts Grx2 into a typical protein of the mitochondrial matrix.