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The N-terminal region of GHRH engages a particularly broad set of specific interactions within the transmembrane binding pocket

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Studied in preclinical models of tissue repair and gastrointestinal research

Gpxs exist in multiple isoforms, with different cellular localization and different substrate specificity ( 2 O 2 , Prxs seem to be more active, given their higher intracellular concentration and rate constant ( GSH, exploiting the redox-active thiol residue (-SH) of cysteine, exerts its antioxidant function mainly via Gpxs-mediated reactions, which result in peroxide buffering with simultaneous oxidation of GSH to GSSG ( Besides the neutralization of free radicals produced in phase 1 liver metabolism of chemical toxins, GSH also participates in the protection from the resulting electrophilic substrates through the intervention of glutathione-S-transferases (GSTs)