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Scanning for Phosphotyrosine

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Science's STKE  15 Jan 2002:
Vol. 2002, Issue 115, pp. tw28
DOI: 10.1126/stke.2002.115.tw28

Steen et al. report identification of tyrosine phosphorylated peptides and the specific phosphorylated residues using a new method called phosphotyrosine-specific immonium ion (PSI) scanning. Cells treated or not treated with epidermal growth factor (EGF) provided models in which to test the technique. Steen et al. identified tyrosine-phosphorylated proteins and residues already implicated in EGF signaling. In addition, they discovered novel proteins and residues phosphorylated in response to EGF. To their surprise, several of these novel residues were not predicted to be phosphorylated by any of several phosphorylation detection algorithms [Scansite (http://scansite.mit.edu/), ProSite (www.expasy.ch/prosite/), and NetPhos (www.cbs.dtu.dk/)]. Thus, this technique has the power to uncover unexpected and presently unpredictable phosphorylation events.

H. Steen, B. Kuster, M. Fernandez, A. Pandey, M. Mann, Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. J. Biol. Chem. 277, 1031-1039 (2002). [Abstract] [Full Text]

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