Phosphoproteome Analysis |
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Authors: | Roberto Raggiaschi Stefano Gotta Georg C Terstappen |
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Institution: | (1) Sienabiotech S.p.A., Discovery Research, Via Fiorentina 1, 53100 Siena, Italy |
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Abstract: | Protein phosphorylation is directly or indirectly involved in all important cellular events. The understanding of its regulatory
role requires the discovery of the proteins involved in these processes and how, where and when protein phosphorylation takes
place. Investigation of the phosphoproteome of a cell is becoming feasible today although it still represents a very difficult
task especially if quantitative comparisons have to be made. Several different experimental strategies can be employed to
explore phosphoproteomes and this review will cover the most important ones such as incorporation of radiolabeled phosphate
into proteins, application of specific antibodies against phosphorylated residues and direct staining of phosphorylated proteins
in polyacrylamide gels. Moreover, methods to enrich phosphorylated proteins such as affinity chromatography (IMAC) and immunoprecipitation
as well as mass spectrometry for identification of phosphorylated peptides and phosphorylation sites are also described. |
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Keywords: | Phosphorylation phosphoprotein detection strategies phosphoprotein enrichment methods mass spectrometry analysis |
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