The DOI matches its Crossref record; 99 of the 99 references it cites were found in a registry or an index.
Phosphopeptide fragmentation and analysis by mass spectrometry
Abstract
Reversible phosphorylation is a key event in many biological processes and is therefore a much studied phenomenon. The mass spectrometric (MS) analysis of phosphorylation is challenged by the substoichiometric levels of phosphorylation and the lability of the phosphate group in collision‐induced dissociation (CID). Here, we review the fragmentation behaviour of phosphorylated peptides in MS and discuss several MS approaches that have been developed to improve and facilitate the analysis of phosphorylated peptides. CID of phosphopeptides typically results in spectra dominated by a neutral loss of the phosphate group. Several proposed mechanisms for this neutral loss and several factors affecting the extent at which this occurs are discussed. Approaches are described to interpret such neutral loss‐dominated spectra to identify the phosphopeptide and localize the phosphorylation site. Methods using additional activation, such as MS 3 and multistage activation (MSA), have been designed to generate more sequence‐informative fragments from the ion produced by the neutral loss. The characteristics and benefits of these methods are reviewed together with approaches using phosphopeptide derivatization or specific MS scan modes. Additionally, electron‐driven dissociation methods by electron capture dissociation (ECD) or electron transfer dissociation (ETD) and their application in phosphopeptide analysis are evaluated. Finally, these techniques are put into perspective for their use in large‐scale phosphoproteomics studies. Copyright © 2009 John Wiley & Sons, Ltd.
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Cites
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A tissue-specific atlas of mouse protein phosphorylation and expression
Huttlin, E. L., Jedrychowski, M. P., Elias, J. E., Goswami, T., Rad, R., Beausoleil, S. A., Villén, J., Haas, W., Sowa, M. E., & Gygi, S. P. (2010) · Cell · doi:10.1016/j.cell.2010.12.001 · Cited by 1,778
Protein Analysis by Shotgun/Bottom-up Proteomics
Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491
Universal and Confident Phosphorylation Site Localization Using phosphoRS
Taus, T., Köcher, T., Pichler, P., Paschke, C., Schmidt, A., Henrich, C., & Mechtler, K. (2011) · Journal of Proteome Research · doi:10.1021/pr200611n · Cited by 870
Toward a comprehensive characterization of a human cancer cell phosphoproteome
Zhou, H., Di Palma, S., Preisinger, C., Peng, M., Polat, A. N., Heck, A. J. R., & Mohammed, S. (2013) · Journal of Proteome Research · doi:10.1021/pr300630k · Cited by 438
Self-citationA large-scale method to measure absolute protein phosphorylation stoichiometries
Wu, R., Haas, W., Dephoure, N., Huttlin, E. L., Zhai, B., Sowa, M. E., & Gygi, S. P. (2011) · Nature Methods · doi:10.1038/nmeth.1636 · Cited by 276
Metadata
- Authors
- Boersema, P. J., Mohammed, S., & Heck, A. J. R.
- Venue
- Journal of Mass Spectrometry
- Publisher
- Wiley
- Published
- 2009-06
- Volume
- 44
- Issue
- 6
- Pages
- 861-878
- ISSN
- 1076-5174 (ISSN-L)
- 1096-9888
- OpenAlex
- W2044620987
- Cited by
- 362
- References
- 99
- FWCI
- 17.72
- Type
- journal article
- Language
- en
- Open access
- closed
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