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Proteomic analysis of phosphorylation, oxidation and nitrosylation in signal transduction

Spickett, C.M. and Pitt, A.R. and Morrice, N. and Kolch, W. (2006) Proteomic analysis of phosphorylation, oxidation and nitrosylation in signal transduction. BBA - Biochimica et Biophysica Acta, 1764 (12). pp. 1823-1841.

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Abstract

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.

Item type: Article
ID code: 17198
Keywords: signal transduction, proteomics, phosphorylation, oxidation, nitrosylation, post translational modifications, Chemistry, Biology
Subjects: Science > Chemistry
Science > Natural history > Biology
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Faculty of Science > Pure and Applied Chemistry
Related URLs:
    Depositing user: Strathprints Administrator
    Date Deposited: 06 May 2010 15:15
    Last modified: 17 Jul 2013 00:10
    URI: http://strathprints.strath.ac.uk/id/eprint/17198

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