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glutathione disulfide reductase oxyr Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with for protein reduction The thiol-disulfide-switch model of E.

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Neurosci Lett (2010) 468(3):17882

glutathione disulfide reductase oxyr Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with for protein reduction The thiol-disulfide-switch model of E.

Control of taNK-binding kinase 1-mediated signaling by the 1 34.5 protein of herpes simplex virus 1

glutathione disulfide reductase oxyr Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with for protein reduction The thiol-disulfide-switch model of E.

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glutathione disulfide reductase oxyr Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with for protein reduction The thiol-disulfide-switch model of E.

[DOI] [PubMed] [Google Scholar] Chuang S

glutathione disulfide reductase oxyr Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with for protein reduction The thiol-disulfide-switch model of E.

In: Adam MP, Ardinger HH, Pagon RA, et al., eds

glutathione disulfide reductase oxyr Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with for protein reduction The thiol-disulfide-switch model of E.

These compounds were described not only as substrates for glutathione production but also as metabolically active participants in pathways related to methylation and redox signaling

glutathione disulfide reductase oxyr Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with for protein reduction The thiol-disulfide-switch model of E.

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