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Nevertheless, the most prominent groups of proteins under both conditions were those involved in the metabolism of xenobiotics, and thus, the study provides a clear rationale for the role of Nrf2 in protection against chemical toxins following both acute and chronic exposure. The definition of the Nrf2 inducible proteome in all organs, from a qualitative and quantitative perspective, would provide a useful platform for the development of Nrf2 inducers as therapeutic agents for the treatment of diseases which have aetiologies based on either chemical stress or chemical exposure. Furthermore, such proteomic analysis should provide a basis for the discovery ABT-263 purchase of biomarkers which can be used to facilitate the translation of basic biochemical science into clinical practice. The following are the supplementary data related to this article. Supplementary Table?1. ? iTRAQ-based proteomic comparison of liver proteins in Nrf2(?/?) and wild type mice. Proteins whose expression was different (P?Endonuclease a common pool are given for n?=?4�C6 animals. Proteins are ordered according to the ratio between wild type and Nrf2(?/?) mice (Nrf2(+/+)/Nrf2(?/?); highest to lowest) such that proteins whose expression is most markedly reduced in Nrf2(?/?) animals appear at the top of the list. Transparency Document. This work was supported by The Wellcome Trust (094128/Z/10/Z) and forms part of a BBSRC-funded PhD undertaken by JW, with further support from AstraZeneca Pharmaceuticals. We are grateful to Jitesh Poonan (Liverpool Cancer Trials Unit, University of Liverpool) for statistical advice and support. We thank Professor Masayuki Yamamoto for providing breeding stock for the Nrf2 knockout mouse colony. ""Protein phosphorylation is the most studied post-translational modifications and it regulates most biological processes. A large proportion of genomes encode proteins that regulate protein phosphorylation (kinases and phosphatases) http://www.selleckchem.com/EGFR(HER).html as well as many classes of protein domains that recognize it as a regulated epitope. The analysis of protein phosphorylation has been transformed in recent years with the development of methods to enrich phosphopeptides from complex mixtures [1], [2], [3], [4]?and?[5], soft peptide fragmentation techniques such as electron transfer dissociation [6], as well as advances in the sensitivity and specificity of mass spectrometry instrumentation. Protein phosphorylation was the first PTM studied on a proteome scale and since then protein acetylation [7], ubiquitination [8] and O-GlcNAcylation [9], amongst others have benefitted from similar technological developments. CID fragmentation is generally the method of choice for peptide fragmentation and its implementation in ion trap and Q-ToF type devices allows rapid and sensitive peptide identification.