The SH2 domain interaction landscape

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

The SH2 domain interaction landscape. / Tinti, M.; Kiemer, Lars; Costa, Stefano; Miller, Martin Lee; Sacco, F.; Olsen, Jesper Velgaard; Carducci, M.; Paoluzi, S.; Langone, F.; Workman, Christopher; Blom, Nikolaj; Machida, K.; Thompson, C.M.; Schutkowski, M.; Brunak, Søren; Mann, Matthias; Mayer, B.J.; Castagnoli, L.; Cesareni, G.

In: Cell Reports, Vol. 3, No. 4, 2013, p. 1293-1305.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Tinti, M, Kiemer, L, Costa, S, Miller, ML, Sacco, F, Olsen, JV, Carducci, M, Paoluzi, S, Langone, F, Workman, C, Blom, N, Machida, K, Thompson, CM, Schutkowski, M, Brunak, S, Mann, M, Mayer, BJ, Castagnoli, L & Cesareni, G 2013, 'The SH2 domain interaction landscape', Cell Reports, vol. 3, no. 4, pp. 1293-1305. https://doi.org/10.1016/j.celrep.2013.03.001

APA

Tinti, M., Kiemer, L., Costa, S., Miller, M. L., Sacco, F., Olsen, J. V., Carducci, M., Paoluzi, S., Langone, F., Workman, C., Blom, N., Machida, K., Thompson, C. M., Schutkowski, M., Brunak, S., Mann, M., Mayer, B. J., Castagnoli, L., & Cesareni, G. (2013). The SH2 domain interaction landscape. Cell Reports, 3(4), 1293-1305. https://doi.org/10.1016/j.celrep.2013.03.001

Vancouver

Tinti M, Kiemer L, Costa S, Miller ML, Sacco F, Olsen JV et al. The SH2 domain interaction landscape. Cell Reports. 2013;3(4):1293-1305. https://doi.org/10.1016/j.celrep.2013.03.001

Author

Tinti, M. ; Kiemer, Lars ; Costa, Stefano ; Miller, Martin Lee ; Sacco, F. ; Olsen, Jesper Velgaard ; Carducci, M. ; Paoluzi, S. ; Langone, F. ; Workman, Christopher ; Blom, Nikolaj ; Machida, K. ; Thompson, C.M. ; Schutkowski, M. ; Brunak, Søren ; Mann, Matthias ; Mayer, B.J. ; Castagnoli, L. ; Cesareni, G. / The SH2 domain interaction landscape. In: Cell Reports. 2013 ; Vol. 3, No. 4. pp. 1293-1305.

Bibtex

@article{a28d13cd59994c3486fed6b6905a3473,
title = "The SH2 domain interaction landscape",
abstract = "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 high-density peptide chip technology that allows for probing of 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 putative SH2-peptide interactions for more than 70 different SH2 domains. By integrating this rich data set with orthogonal context-specific information, we have assembled an SH2-mediated probabilistic interaction network, which we make available as a community resource in the PepspotDB database. A predicted dynamic interaction between the SH2 domains of the tyrosine phosphatase SHP2 and the phosphorylated tyrosine in the extracellular signal-regulated kinase activation loop was validated by experiments in living cells.",
author = "M. Tinti and Lars Kiemer and Stefano Costa and Miller, {Martin Lee} and F. Sacco and Olsen, {Jesper Velgaard} and M. Carducci and S. Paoluzi and F. Langone and Christopher Workman and Nikolaj Blom and K. Machida and C.M. Thompson and M. Schutkowski and S{\o}ren Brunak and Matthias Mann and B.J. Mayer and L. Castagnoli and G. Cesareni",
year = "2013",
doi = "10.1016/j.celrep.2013.03.001",
language = "English",
volume = "3",
pages = "1293--1305",
journal = "Cell Reports",
issn = "2211-1247",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - The SH2 domain interaction landscape

AU - Tinti, M.

AU - Kiemer, Lars

AU - Costa, Stefano

AU - Miller, Martin Lee

AU - Sacco, F.

AU - Olsen, Jesper Velgaard

AU - Carducci, M.

AU - Paoluzi, S.

AU - Langone, F.

AU - Workman, Christopher

AU - Blom, Nikolaj

AU - Machida, K.

AU - Thompson, C.M.

AU - Schutkowski, M.

AU - Brunak, Søren

AU - Mann, Matthias

AU - Mayer, B.J.

AU - Castagnoli, L.

AU - Cesareni, G.

PY - 2013

Y1 - 2013

N2 - 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 high-density peptide chip technology that allows for probing of 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 putative SH2-peptide interactions for more than 70 different SH2 domains. By integrating this rich data set with orthogonal context-specific information, we have assembled an SH2-mediated probabilistic interaction network, which we make available as a community resource in the PepspotDB database. A predicted dynamic interaction between the SH2 domains of the tyrosine phosphatase SHP2 and the phosphorylated tyrosine in the extracellular signal-regulated kinase activation loop was validated by experiments in living cells.

AB - 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 high-density peptide chip technology that allows for probing of 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 putative SH2-peptide interactions for more than 70 different SH2 domains. By integrating this rich data set with orthogonal context-specific information, we have assembled an SH2-mediated probabilistic interaction network, which we make available as a community resource in the PepspotDB database. A predicted dynamic interaction between the SH2 domains of the tyrosine phosphatase SHP2 and the phosphorylated tyrosine in the extracellular signal-regulated kinase activation loop was validated by experiments in living cells.

UR - http://www.scopus.com/inward/record.url?scp=84876957035&partnerID=8YFLogxK

U2 - 10.1016/j.celrep.2013.03.001

DO - 10.1016/j.celrep.2013.03.001

M3 - Journal article

C2 - 23545499

AN - SCOPUS:84876957035

VL - 3

SP - 1293

EP - 1305

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 4

ER -

ID: 46440109