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Article type: Research Article
Authors: Pineda-Molina, Estela | Lamas, Santiago
Affiliations: Centro de Investigaciones Biológicas, Instituto "Reina Sofía" de Investigaciones Nefrológicas, CSIC, Madrid, Spain
Abstract: Both oxidative and nitrosative stresses may result in the inactivation of the binding to DNA of redox-sensitive transcription factors. The underlying biochemical mechanisms may involve oxidation or nitrosylation of critical thiols within the DNA binding domains of these proteins. However, S-glutahionylation, the formation of a mixed disulfide between glutathione and the redox-sensitive cysteine residues, has been shown to occur under NO exposure and pro-oxidative conditions in c-Jun, one of the AP-1 constituents [1,2]. This modification may be functionally important as it is reversible and has been detected in other transcription factors, such as NF-κB, by using covalent chromatography with a modified S-nitrosoglutathione sepharose [3].
Journal: BioFactors, vol. 15, no. 2-4, pp. 113-115, 2001
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