Identification of in vivo phosphorylation sites of lens proteins from porcine eye lenses by a gel-free phosphoproteomics approach

@inproceedings{Chiou2010IdentificationOI,
  title={Identification of in vivo phosphorylation sites of lens proteins from porcine eye lenses by a gel-free phosphoproteomics approach},
  author={S. P. Chiou and Chun-Hao Huang and I-Liang Lee and Yi-Ting Wang and Nai-yu Liu and Y S Tsay and Yu-Ju Chen},
  booktitle={Molecular vision},
  year={2010}
}
PURPOSE Phosphorylation is an important post-translational modification for the cellular regulation of various biosignaling pathways. We have identified in vivo phosphorylation sites of various lens proteins including especially the major structural proteins of the crystallin family from porcine eye lenses by means of two-dimensional gel electrophoresis (2-DE) or immobilized metal affinity chromatography (IMAC) followed by liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS… CONTINUE READING

Similar Papers

Citations

Publications citing this paper.
SHOWING 1-9 OF 9 CITATIONS

Novel roles for α-crystallins in retinal function and disease

  • Progress in Retinal and Eye Research
  • 2012
VIEW 2 EXCERPTS
CITES RESULTS & BACKGROUND

References

Publications referenced by this paper.
SHOWING 1-10 OF 33 REFERENCES

Phosphorylation-induced change of the oligomerization state of alpha B-crystallin.

  • The Journal of biological chemistry
  • 2001
VIEW 7 EXCERPTS
HIGHLY INFLUENTIAL