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glutaredoxin glutathione disulfide bond formation by exported indicates glutathione's presence in the E. coli periplasm S-Glutathionylation: From Molecular Mechanisms to

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glutaredoxin glutathione disulfide bond formation by exported indicates glutathione's presence in the E. coli periplasm S-Glutathionylation: From Molecular Mechanisms to

doi: 10.1038/s41598-022-06412-3 285 ManamSTsakokTTillSFlohrC

glutaredoxin glutathione disulfide bond formation by exported indicates glutathione's presence in the E. coli periplasm S-Glutathionylation: From Molecular Mechanisms to

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glutaredoxin glutathione disulfide bond formation by exported indicates glutathione's presence in the E. coli periplasm S-Glutathionylation: From Molecular Mechanisms to

Food Biosci 106306

glutaredoxin glutathione disulfide bond formation by exported indicates glutathione's presence in the E. coli periplasm S-Glutathionylation: From Molecular Mechanisms to

Since the FDR sample size is small, these analyses were restricted to non-parametric tests, and the results should be interpreted with caution

glutaredoxin glutathione disulfide bond formation by exported indicates glutathione's presence in the E. coli periplasm S-Glutathionylation: From Molecular Mechanisms to

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glutaredoxin glutathione disulfide bond formation by exported indicates glutathione's presence in the E. coli periplasm S-Glutathionylation: From Molecular Mechanisms to

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