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Rahimi, N

We show (i) that PfGrx-catalyzed redox reactions outcompete uncatalyzed reactions between roGFP2 and GSH or GSSG by several orders of magnitude, (ii) that the PfGrx-catalyzed reduction and oxidation of roGFP2 occur via a mono- and not a dithiol mechanism, and (iii) that the reduction of roGFP2(S 2 ) as a model non-glutathione disulfide substrate most likely involves a rate-limiting glutathionylation in a ternary complex with a GSH molecule that is activated at the 1st glutathione-interaction site of PfGrx

Immunohistochemistry of GGT1 protein expression in Gclc WT and KO orthotopic and flank tumors (n = 4 animals representative of 2 independent experiments)

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