J.A. Bárcena

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: This work presents a generally applicable model that accurately explains the behavior of data obtained using current SIL approaches, including (18)O, iTRAQ, and SILAC labeling, and different MS instruments, and decomposes the total technical variance into the spectral, peptide, and protein variance components.

TL;DR: The sequence of human glutaredoxin was compared to that of Escherichia coli with known three-dimensional structure in solution to identify conserved residues and predict a structure from alignment, and in particular the GSH-binding site of glutared toxin was conserved between all molecules.

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