Phosphoproteome analysis of the pathogenic bacterium Helicobacter pylori reveals over-representation of tyrosine phosphorylation and multiply phosphorylated proteins.

@article{Ge2011PhosphoproteomeAO,
  title={Phosphoproteome analysis of the pathogenic bacterium Helicobacter pylori reveals over-representation of tyrosine phosphorylation and multiply phosphorylated proteins.},
  author={Ruiguang Ge and Xuesong Sun and Chuanle Xiao and Xingfeng Yin and Weiran Shan and Zhuo Chen and Qing-Yu He},
  journal={Proteomics},
  year={2011},
  volume={11 8},
  pages={1449-61}
}
Increasing evidence shows that protein phosphorylation on serine (Ser), threonine (Thr) and tyrosine (Tyr) residues is a major regulatory post-translational modification in the bacteria. To reveal the phosphorylation state in the Gram-negative pathogenic bacterium Helicobacter pylori, we carried out a global and site-specific phosphoproteomic analysis based on TiO(2) -phosphopeptide enrichment and high-accuracy LC-MS/MS determination. Eighty-two phosphopeptides from 67 proteins were identified… CONTINUE READING
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