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Regarding intracellular roGFP2-based structure-function analysis of glutaredoxins, we now showed that the GSSG-dependent oxidation of the fused glutaredoxin moiety (and not the glutathionylation of the roGFP2 moiety) is rate-limiting unless saturating GSSG concentrations are present

The unexpected activity can be explained by the formation of variable amounts of disulfide-bridged PfGrx C32S/C88S homodimers and potential Diamide-modified monomers, summarized as PfGrx C32S/C88S (SX), as revealed by non-reducing SDS-PAGE (Fig

Educational content must avoid prescriptive language and clearly indicate experimental status

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Evidence of oxidative stress in full-term healthy infants