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glutathione interactions Aromatic Residue F443 Modulates the Dimer Interface and Activity of Pseudomonas mandelii Glutathione Reductase
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glutathione interactions Aromatic Residue F443 Modulates the Dimer Interface and Activity of Pseudomonas mandelii Glutathione Reductase
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Detection of ProteinProtein Interactions Using Glutathione S Transferase (GST) Pull Down Assay Technique Springer Nature Experiments The dithiol mechanism of class I glutaredoxins promotes specificity for glutathione as a reducing agent ScienceDirect Deciphering the mechanism of glutaredoxin catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction Nature Communications The dithiol mechanism of class I glutaredoxins promotes specificity for glutathione as a reducing agent ScienceDirect
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glutathione interactions Aromatic Residue F443 Modulates the Dimer Interface and Activity of Pseudomonas mandelii Glutathione Reductase
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