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Cited by 270

The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.

Phosphoproteome Analysis of Drosophila melanogaster Embryos

Open access
Zhai, Bo, Villén, Judit, Beausoleil, Sean A., Mintseris, Julian, Gygi, Steven P.·2008·Journal of Proteome Research

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.

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Metadata

Authors
Zhai, B., Villén, J., Beausoleil, S. A., Mintseris, J., & Gygi, S. P.
Venue
Journal of Proteome Research
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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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.