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. (http://dx.doi.org/10.1016/j.bbapap.2006.09.013)
Full text not available in this repository.Request a copyAbstract
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 Dates: DateEventDecember 2006PublishedSubjects: Science > Chemistry
Science > Natural history > BiologyDepartment: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Faculty of Science > Pure and Applied ChemistryDepositing user: Strathprints Administrator Date deposited: 06 May 2010 14:15 Last modified: 08 Apr 2024 17:30 URI: https://strathprints.strath.ac.uk/id/eprint/17198