Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.

@article{Christensen2005PosttranslationallyMR,
  title={Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.},
  author={Brian Christensen and Mette Slot Nielsen and Kim F Haselmann and Torben Ellebaek Petersen and Esben Skipper S\orensen},
  journal={The Biochemical journal},
  year={2005},
  volume={390 Pt 1},
  pages={285-92}
}
OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival. A significant regulation of OPN function is mediated through PTM (post-translational modification). Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of… CONTINUE READING
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