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Phosphoproteome Analysis of Drosophila melanogaster Embryos
Open accessAbstract
Protein phosphorylation is a key regulatory event in most cellular processes and development. Mass spectrometry-based proteomics provides a framework for the large-scale identification and characterization of phosphorylation sites. Here, we used a well-established phosphopeptide enrichment and identification strategy including the combination of strong cation exchange chromatography, immobilized metal affinity chromatography, and high-accuracy mass spectrometry instrumentation to study phosphorylation in developing Drosophila embryos. In total, 13,720 different phosphorylation sites were discovered from 2702 proteins with an estimated false-discovery rate (FDR) of 0.63% at the peptide level. Because of the large size of the data set, both novel and known phosphorylation motifs were extracted using the Motif-X algorithm, including those representative of potential ordered phosphorylation events.
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Metadata
- Authors
- Zhai, B., Villén, J., Beausoleil, S. A., Mintseris, J., & Gygi, S. P.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-03-08
- Volume
- 7
- Issue
- 4
- Pages
- 1675-1682
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W2018732798
- Cited by
- 270
- References
- 38
- FWCI
- 12.23
- Type
- journal article
- Language
- en
- Open access
- green
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