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Phospho‐proteomic analysis of cellular signaling
Author(s) -
de Graauw Marjo,
Hensbergen Paul,
van de Water Bob
Publication year - 2006
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200600018
Subject(s) - proteomics , signal transduction , phosphorylation , biology , protein phosphorylation , mechanism (biology) , computational biology , apoptosis , toxicant , microbiology and biotechnology , proteome , bioinformatics , chemistry , biochemistry , protein kinase a , gene , philosophy , organic chemistry , epistemology , toxicity
Reversible protein phosphorylation plays an important role in the regulation of many different processes, such as cell growth, differentiation, migration, metabolism, and apoptosis. Identification of differentially phosphorylated proteins by means of phospho‐proteomic analysis provides insight into signal transduction pathways that are activated in response to, for example, growth factor stimulation or toxicant‐induced apoptosis. This review summarizes recent advances made in the field of phospho‐proteomics and provides examples of how phospho‐proteomic techniques can be combined to quantitatively investigate the dynamic changes in protein phosphorylation in time. By linking experimental data to clinical data ( e.g. , disease progression or response to therapy) new disease markers could be identified, which could then be validated for applications in disease diagnosis and progression or prediction of a response to drugs.