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Redox regulation in photosynthetic organisms: focus on glutathionylation

Tipo de material: TextoTextoSeries ; Antioxidants and Redox Signaling, 16(6), p.567-586, 2012Trabajos contenidos:
  • Zaffagnini M
  • Bedhomme M
  • Marchand Ch
  • Morisse S
  • Trost P
  • Lemaire Sd
Tema(s): Recursos en línea: Resumen: In photosynthetic organisms, besides the well-established disulfide/dithiol exchange reactions specifically controlled by thioredoxins (TRXs), protein S-glutathionylation is emerging as an alternative redox modification occurring under stress conditions. This modification, consisting of the formation of a mixed disulfide between glutathione and a protein cysteine residue, can not only protect specific cysteines from irreversible oxidation but also modulate protein activities and appears to be specifically controlled by small disulfide oxidoreductases of the TRX superfamily named glutaredoxins (GRXs).
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Documentos solicitados Documentos solicitados CICY Documento préstamo interbibliotecario Ref1 B-16816 (Browse shelf(Opens below)) Available

In photosynthetic organisms, besides the well-established disulfide/dithiol exchange reactions specifically controlled by thioredoxins (TRXs), protein S-glutathionylation is emerging as an alternative redox modification occurring under stress conditions. This modification, consisting of the formation of a mixed disulfide between glutathione and a protein cysteine residue, can not only protect specific cysteines from irreversible oxidation but also modulate protein activities and appears to be specifically controlled by small disulfide oxidoreductases of the TRX superfamily named glutaredoxins (GRXs).

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