Exploring oxidative modifications of tyrosine: An update on mechanisms of formation, advances in analysis and biological consequences

@article{HoueLvin2015ExploringOM,
  title={Exploring oxidative modifications of tyrosine: An update on mechanisms of formation, advances in analysis and biological consequences},
  author={Chantal Hou{\'e}e-L{\'e}vin and Krzysztof Bobrowski and Lubica Horakova and Betul Karademir and Christian Sch{\"o}neich and Michael Jonathan Davies and Corinne M. Spickett},
  journal={Free Radical Research},
  year={2015},
  volume={49},
  pages={347 - 373}
}
Abstract Protein oxidation is increasingly recognised as an important modulator of biochemical pathways controlling both physiological and pathological processes. While much attention has focused on cysteine modifications in reversible redox signalling, there is increasing evidence that other protein residues are oxidised in vivo with impact on cellular homeostasis and redox signalling pathways. A notable example is tyrosine, which can undergo a number of oxidative post-translational… 
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The sulfur-containing amino acids cysteine and methionine are prominent protein targets of redox modification during conditions of oxidative stress and are equally prone to one-electron pathways, generating intermediary radicals and/or radial ions.
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Recent advances in investigation of mechanisms of protein redox modifications and adaptive redox switches such as MAPK/PI3K/PTEN, Nrf2/Keap1, and NF-κB/IκB, powerful regulators of numerous physiological processes, also implicated in various diseases are discussed.
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Using the radiolytic generation of specific oxidizing radicals to form tyrosine phenoxyl radicals in an aqueous solution at a known rate, the products in the absence and presence of nitric oxide or oxygen are compared.
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