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Proteomic analysis of phosphorylation, oxidation and nitrosylation in signal transduction

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
Volume 1764, Issue 12, Pages 1823-1841

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbapap.2006.09.013

Keywords

signal transduction; proteomics; phosphorylation; oxidation; nitrosylation

Funding

  1. Biotechnology and Biological Sciences Research Council [BB/C511572/1] Funding Source: Medline
  2. Wellcome Trust Funding Source: Medline
  3. Biotechnology and Biological Sciences Research Council [BB/C511572/1] Funding Source: researchfish

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Signal transduction pathways control cell fate, survival and function. They are organized as intricate biochemical networks which enable biochemical protein activities, crosstalk and subcellular localization to be integrated and tuned to produce highly specific biological responses in a robust and reproducible manner. Post translational Modifications (PTMs) play major roles in regulating these processes through a wide variety of mechanisms that include changes in protein activities, interactions, and subcellular localizations. Determining and analyzing PTMs poses enormous challenges. Recent progress in mass spectrometry (MS) based proteomics have enhanced our capability to map and identify many PTMs. Here we review the current state of proteomic PTM analysis relevant for signal transduction research, focusing on two areas: phosphorylation, which is well established as a widespread key regulator of signal transduction; and oxidative modifications, which from being primarily viewed as protein damage now start to emerge as important regulatory mechanisms. (c) 2006 Elsevier B.V. All rights reserved.

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