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Identification of Tyrosine Phosphorylated Proteins by SH2 Domain Affinity Purification and Mass Spectrometry

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Identification of Tyrosine Phosphorylated Proteins by SH2 Domain Affinity Purification and Mass Spectrometry. / Buhs, Sophia; Gerull, Helwe; Nollau, Peter.

In: Methods Mol Biol, Vol. 1555, 2017, p. 407-418.

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

Harvard

Buhs, S, Gerull, H & Nollau, P 2017, 'Identification of Tyrosine Phosphorylated Proteins by SH2 Domain Affinity Purification and Mass Spectrometry', Methods Mol Biol, vol. 1555, pp. 407-418. https://doi.org/10.1007/978-1-4939-6762-9_23

APA

Buhs, S., Gerull, H., & Nollau, P. (2017). Identification of Tyrosine Phosphorylated Proteins by SH2 Domain Affinity Purification and Mass Spectrometry. Methods Mol Biol, 1555, 407-418. https://doi.org/10.1007/978-1-4939-6762-9_23

Vancouver

Buhs S, Gerull H, Nollau P. Identification of Tyrosine Phosphorylated Proteins by SH2 Domain Affinity Purification and Mass Spectrometry. Methods Mol Biol. 2017;1555:407-418. https://doi.org/10.1007/978-1-4939-6762-9_23

Bibtex

@article{2edea2dc25bb4609ac1bfcaed418c447,
title = "Identification of Tyrosine Phosphorylated Proteins by SH2 Domain Affinity Purification and Mass Spectrometry",
abstract = "Phosphotyrosine signaling plays a major role in the control of many important biological functions such as cell proliferation and apoptosis. Deciphering of phosphotyrosine-dependent signaling is therefore of great interest paving the way for the understanding of physiological and pathological processes of signal transduction. On the basis of the specific binding of SH2 domains to phosphotyrosine residues, we here present an experimental workflow for affinity purification and subsequent identification of tyrosine phosphorylated proteins by mass spectrometry. In combination with SH2 profiling, a broadly applicable platform for the characterization of phosphotyrosine profiles in cell extracts, our pull down strategy enables researchers by now to identify proteins in signaling cascades which are differentially phosphorylated and selectively recognized by distinct SH2 domains.",
author = "Sophia Buhs and Helwe Gerull and Peter Nollau",
year = "2017",
doi = "10.1007/978-1-4939-6762-9_23",
language = "English",
volume = "1555",
pages = "407--418",
journal = "Methods Mol Biol",
issn = "1064-3745",
publisher = "Humana Press",

}

RIS

TY - JOUR

T1 - Identification of Tyrosine Phosphorylated Proteins by SH2 Domain Affinity Purification and Mass Spectrometry

AU - Buhs, Sophia

AU - Gerull, Helwe

AU - Nollau, Peter

PY - 2017

Y1 - 2017

N2 - Phosphotyrosine signaling plays a major role in the control of many important biological functions such as cell proliferation and apoptosis. Deciphering of phosphotyrosine-dependent signaling is therefore of great interest paving the way for the understanding of physiological and pathological processes of signal transduction. On the basis of the specific binding of SH2 domains to phosphotyrosine residues, we here present an experimental workflow for affinity purification and subsequent identification of tyrosine phosphorylated proteins by mass spectrometry. In combination with SH2 profiling, a broadly applicable platform for the characterization of phosphotyrosine profiles in cell extracts, our pull down strategy enables researchers by now to identify proteins in signaling cascades which are differentially phosphorylated and selectively recognized by distinct SH2 domains.

AB - Phosphotyrosine signaling plays a major role in the control of many important biological functions such as cell proliferation and apoptosis. Deciphering of phosphotyrosine-dependent signaling is therefore of great interest paving the way for the understanding of physiological and pathological processes of signal transduction. On the basis of the specific binding of SH2 domains to phosphotyrosine residues, we here present an experimental workflow for affinity purification and subsequent identification of tyrosine phosphorylated proteins by mass spectrometry. In combination with SH2 profiling, a broadly applicable platform for the characterization of phosphotyrosine profiles in cell extracts, our pull down strategy enables researchers by now to identify proteins in signaling cascades which are differentially phosphorylated and selectively recognized by distinct SH2 domains.

U2 - 10.1007/978-1-4939-6762-9_23

DO - 10.1007/978-1-4939-6762-9_23

M3 - SCORING: Journal article

C2 - 28092046

VL - 1555

SP - 407

EP - 418

JO - Methods Mol Biol

JF - Methods Mol Biol

SN - 1064-3745

ER -