Cell Reports volume 3, issue 4, P1293-1305 2013 DOI: 10.1016/j.celrep.2013.03.001 View full text
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Michele Tinti, Lars Kiemer, Stefano Costa, Martin L. Miller, Francesca Sacco, Jesper V. Olsen, Martina Carducci, Serena Paoluzi, Francesca Langone, Christopher T. Workman, Nikolaj Blom, Kazuya Machida, Christopher M. Thompson, Mike Schutkowski et al.

Abstract: Summary Members of the SH2 domain family modulate signal transduction by binding to short peptides containing phosphorylated tyrosines. Each domain displays a distinct preference for the sequence context of the phosphorylated residue. We have developed a new high-density peptide chip technology that allows probing the affinity of most SH2 domains for a large fraction of the entire complement of tyrosine phosphopeptides in the human proteome. Using this technique we have experimentally identified thousands of …

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