Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides

@article{Gevaert2003ExploringPA,
  title={Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides},
  author={K. Gevaert and M. Goethals and L. Martens and J. Damme and A. Staes and G. Thomas and J. Vandekerckhove},
  journal={Nature Biotechnology},
  year={2003},
  volume={21},
  pages={566-569}
}
Current non-gel techniques for analyzing proteomes rely heavily on mass spectrometric analysis of enzymatically digested protein mixtures. Prior to analysis, a highly complex peptide mixture is either separated on a multidimensional chromatographic system or it is first reduced in complexity by isolating sets of representative peptides. Recently, we developed a peptide isolation procedure based on diagonal electrophoresis and diagonal chromatography. We call it combined fractional diagonal… Expand
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References

SHOWING 1-10 OF 18 REFERENCES
Signature-peptide approach to detecting proteins in complex mixtures.
Large-scale analysis of the yeast proteome by multidimensional protein identification technology
Proteomics based on selecting and quantifying cysteine containing peptides by covalent chromatography.
Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
A systematic approach to the analysis of protein phosphorylation
...
1
2
...