References
- Owens T, Cess CD, Ramanathan A. Enhanced carbon dioxide greenhouse to compensate for reduced solar luminosity on early Earth. Nature277, 640–641 (1979).
- Davies MJ. The oxidative environment and protein damage. Biochim. Biophys. Acta1703, 93–109 (2005).
- Winterbourn CC. Reconciling the chemistry and biology of reactive oxygen species. Nat. Chem. Biol.4, 278–286 (2008).
- Halliwell B, Gutteridge J. Free Radicals in Biology and Medicine (4th Edition). Oxford University Press, Oxford, UK (2007).
- Oktyabrsky ON, Smirnova GV. Redox regulation of cellular function. Biochemistry72(2), 32–145 (2007).
- Chiarugi P, Buricchi F. Protein tyrosine phosphorylation and reversible oxidation: two cross-talking posttranslational modifications. Antioxid. Redox Signal.9, 1–24 (2007).
- Görg A, Weiss W, Dunn MJ. Current two-dimensional electrophoresis technology for proteomics. Proteomics4, 3665–3685 (2004).
- Rabilloud T, Heller M, Gasnier F et al. Proteomics analysis of cellular response to oxidative stress – evidence for in vivo overoxidation of peroxiredoxins at their active site. J. Biol. Chem.277, 19396–19401 (2002).
- Kanamoto T, Hellman U, Heldin CH et al. Functional proteomics of transforming growth factor-β 2-stimulated My1Lu epithelial cells: Rad51 as a target of TGFβ 1-dependent regulation of DNA repair. EMBO J.21, 1219–1230 (2002).
- Sheehan D. Detection of redox-based modification in two dimensional electrophoresis proteomic separations. Biochem. Biophys. Res. Commun.349, 455–462 (2006).
- Noda Y, Berlett BS, Stadtman ER et al. Identification of enzymes and regulatory proteins in Escherichia coli that are oxidized under nitrogen, carbon or phosphate starvation. Proc. Natl Acad. Sci. USA104, 18456–18460 (2007).
- Tyther R, Ahmeda A, Johns E et al. Proteomic identification of tyrosine nitration targets in kidney of spontaneously hypertensive rats. Proteomics7, 4555–4564 (2007).
- Newman SF, Sultana R, Perluigi M et al. An increase in S-glutathionylated proteins in the Alzheimer’s disease inferior parietal lobule, a proteomics approach. J. Neurosci. Res.85, 1506–1514 (2009).
- Lind C, Gerdes R, Hamnell Y et al. Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis. Arch. Biochem. Biophys.406, 229–240 (2002).
- Baty JW, Hampton MB, Winterbourn CC. Detection of oxidant sensitive thiol proteins by fluorescence labelling and two dimensional electrophoresis. Proteomics2, 1261–1266 (2002).
- Leichert LI, Jakob U. Protein thiol modifications visualized in vivo. PLOS Biol.2, 1723–1737 (2004).
- Levine RL, Moskovitz J, Stadtman ER. Oxidation of methionines in proteins: roles in antioxidant defense and cellular regulation. IUBMB Life50, 301–307 (2000).
- Hansen RE, Roth JR, Winther JR. Quantifying the global cellular thiol-disulfide status. Proc. Natl Acad. Sci. USA106, 422–427 (2009).
- Saurin AT, Neubert H, Brennan JP et al. Widespread sulfenic acid formation in tissues in response to hydrogen peroxide. Proc. Natl Acad. Sci. USA101, 17982–17987 (2004).
- Jaffrey SR, Erdjument-Bromage H, Ferris CD et al. Protein S-nitrosylation: a physiological signal for neuronal nitric oxide. Nat. Cell. Biol.3, 193–197 (2001).
- Malmstrom J, Lee H, Aebersold R. Advances in proteomic workflows for systems biology. Curr. Opin. Biotechnol.18, 378–384 (2007).
- McDonagh B, Ogueta S, Lasarte G et al. Shotgun redox proteomics identifies specifically modified cysteines in key metabolic enzymes under oxidative stress in Saccharomyces cerevisiae. J. Proteomics72, 677–689 (2009).
- Hashemy SI, Johansson C, Berndt C et al. Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: effects on structure and activity. J. Biol. Chem.282, 14428–14436 (2007).
- Gygi SP, Rist B, Gerber SA et al. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol.17(10), 994–999 (1999).
- Ong SE, Blagoev B, Kratchmarova I et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics1, 376–386 (2002).
- Ross PL, Huang YN, Marchese JN et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics.3(12), 1154–1169 (2004).
- Nelson KJ, Day AE, Zeng BB et al. Isotope-coded, iodoacetamide-based reagent to determine individual cysteine pK(a) values by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Biochem.375, 187–195 (2008).
- Sethuraman M, McComb ME, Huang H et al. Isotope-coded affinity tag (ICAT) approach to redox proteomics: identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res.3, 1228–1233 (2004).
- Liechert LI, Gehrke F, Gudiseva HV et al. Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. Proc. Natl Acad. Sci. USA105, 8197–8202 (2008).
- Fu C, Wu C, Liu T et al. Elucidation of thioredoxin target protein networks in mouse. Mol. Cell. Proteomics.8, 1674–1687 (2009).
- Mann M. Functional and quantitative proteomics using SILAC. Nat. Rev. Mol. Cell Biol.7, 952–958 (2006).