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Integrated proteomic analysis of post-translational modifications by serial enrichment
Open accessAbstract
We report a mass spectrometry–based method for the integrated analysis of protein expression, phosphorylation, ubiquitination and acetylation by serial enrichments of different post-translational modifications (SEPTM) from the same biological sample. This technology enabled quantitative analysis of nearly 8,000 proteins and more than 20,000 phosphorylation, 15,000 ubiquitination and 3,000 acetylation sites per experiment, generating a holistic view of cellular signal transduction pathways as exemplified by analysis of bortezomib-treated human leukemia cells.
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Metadata
- Authors
- Mertins, P., Qiao, J. W., Patel, J., Udeshi, N. D., Clauser, K. R., Mani, D. R., Burgess, M. W., Gillette, M. A., Jaffe, J. D., & Carr, S. A.
- Venue
- Nature Methods
- Published
- 2013-06-09
- Volume
- 10
- Issue
- 7
- Pages
- 634-637
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W1974515407
- Cited by
- 618
- References
- 1
- FWCI
- 21.70
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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