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Denaturation and reactivation of dimeric human glutathione reductase: an assay for folding inhibitors

Nordhoff, A. ; Tziatzios, C. ; van den Broek, J. A. ; Schott, M. K. ; Kalbitzer, Hans Robert ; Becker, K. ; Schubert, D. ; Schirmer, R. H.


Human glutathione reductase (GR; which catalyzes the reaction NADPH + GSSG + H+ --> 2 GSH + NADP+) is an obligatory FAD-containing homodimer of known geometry. Native human GR, a potential target of antimalarial and cytostatic agents, cannot be dissociated by dilution or by means of subunit-interface mimetics, similarly to well-studied viral dimeric proteins. However, ab initio folding and/or ...


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