A novel method for analyzing phosphoproteins using SELDI‐TOF MS in combination with a series of recombinant proteins
- 10 July 2007
- journal article
- technology
- Published by Wiley in Proteomics
- Vol. 7 (14) , 2350-2354
- https://doi.org/10.1002/pmic.200700157
Abstract
A novel SELDI-TOF MS-based method for analyzing phosphoproteins was developed using a series of recombinant wild-type and mutant ribosomal P2 proteins. We demonstrated that the phosphorylation status of the overexpressed proteins in cells was easily and rapidly confirmed using this method. The ribosomal P2 protein contained two phosphorylation sites, which were sequentially phosphorylated in vivo. We also quantitatively detected the phosphoprotein by using SELDI-TOF MS.Keywords
This publication has 19 references indexed in Scilit:
- Proteomic analysis of fast and slow muscles from normal and kyphoscoliotic mice using protein arrays, 2-DE and MSProteomics, 2006
- Phosphorylation Analysis by Mass SpectrometryMolecular & Cellular Proteomics, 2006
- Quantitative Phosphoproteomics Applied to the Yeast Pheromone Signaling PathwayMolecular & Cellular Proteomics, 2005
- Immunoaffinity profiling of tyrosine phosphorylation in cancer cellsNature Biotechnology, 2005
- Mass spectrometry-based proteomicsNature, 2003
- β2-Adrenergic Receptor Stimulated, G Protein-Coupled Receptor Kinase 2 Mediated, Phosphorylation of Ribosomal Protein P2Biochemistry, 2002
- A Mass Spectrometry-based Proteomic Approach for Identification of Serine/Threonine-phosphorylated Proteins by Enrichment with Phospho-specific AntibodiesMolecular & Cellular Proteomics, 2002
- Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiaeNature Biotechnology, 2002
- Tyrosine Phosphorylation Mapping of the Epidermal Growth Factor Receptor Signaling PathwayJournal of Biological Chemistry, 2002
- Proteins P1, P2, and P0, components of the eukaryotic ribosome stalk. New structural and functional aspectsBiochemistry and Cell Biology, 1995