Unknown

Dataset Information

0

Phosphoproteome analysis of Drosophila melanogaster embryos.


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.

SUBMITTER: Zhai B 

PROVIDER: S-EPMC3063950 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Phosphoproteome analysis of Drosophila melanogaster embryos.

Zhai Bo B   Villén Judit J   Beausoleil Sean A SA   Mintseris Julian J   Gygi Steven P SP  

Journal of proteome research 20080308 4


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 phosphory  ...[more]

Similar Datasets

| S-EPMC5123040 | biostudies-literature
| S-EPMC5293093 | biostudies-literature
| S-EPMC9232161 | biostudies-literature
| S-EPMC2947467 | biostudies-literature
2016-12-23 | PXD004753 | Pride
| S-EPMC2865133 | biostudies-literature
| S-EPMC6154878 | biostudies-literature
| EMPIAR-10679 | biostudies-other
2024-09-29 | PXD026049 | Pride
2014-11-21 | GSE63323 | GEO