The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Technologies and challenges in large‐scale phosphoproteomics
Abstract
Phosphorylation, the reversible addition of a phosphate group to amino acid side chains of proteins, is a fundamental regulator of protein activity, stability, and molecular interactions. Most cellular processes, such as inter‐ and intracellular signaling, protein synthesis, degradation, and apoptosis, rely on phosphorylation. This PTM is thus involved in many diseases, rendering localization and assessment of extent of phosphorylation of major scientific interest. MS‐based phosphoproteomics, which aims at describing all phosphorylation sites in a specific type of cell, tissue, or organism, has become the main technique for discovery and characterization of phosphoproteins in a nonhypothesis driven fashion. In this review, we describe methods for state‐of‐the‐art MS‐based analysis of protein phosphorylation as well as the strategies employed in large‐scale phosphoproteomic experiments with focus on the various challenges and limitations this field currently faces.
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Cited by
Phosphoproteomics in the Age of Rapid and Deep Proteome Profiling
Riley, N. M., & Coon, J. J. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04123 · Cited by 265
Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications
Doll, S., & Burlingame, A. L. (2015) · ACS Chemical Biology · doi:10.1021/cb500904b · Cited by 261
Kauko, O., Laajala, T. D., Jumppanen, M., Hintsanen, P., Suni, V., Haapaniemi, P., Corthals, G., Aittokallio, T., Westermarck, J., & Imanishi, S. Y. (2015) · Scientific Reports · doi:10.1038/srep13099 · Cited by 61
Metadata
- Authors
- Engholm‐Keller, K., & Larsen, M. R.
- Venue
- PROTEOMICS
- Publisher
- Wiley
- Published
- 2013-03
- Volume
- 13
- Issue
- 6
- Pages
- 910-931
- ISSN
- 1615-9853 (ISSN-L)
- 1615-9861
- OpenAlex
- W2060747252
- Cited by
- 166
- References
- 15
- FWCI
- 12.14
- Type
- journal article
- Language
- en
- Open access
- closed
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