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J Proteome Res. 2008 Apr;7(4):1675-82. doi: 10.1021/pr700696a. Epub 2008 Mar 8.

Phosphoproteome analysis of Drosophila melanogaster embryos.

Author information

1
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.

Abstract

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.

PMID:
18327897
PMCID:
PMC3063950
DOI:
10.1021/pr700696a
[Indexed for MEDLINE]
Free PMC Article

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