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Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains.

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Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains. / Dierck, Kevin; Machida, Kazuya; Voigt, Anja; Thimm, Julian; Horstmann, Martin; Fiedler, Walter; Mayer, Bruce J; Nollau, Peter.

in: NAT METHODS, Jahrgang 3, Nr. 9, 9, 2006, S. 737-744.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Dierck, K, Machida, K, Voigt, A, Thimm, J, Horstmann, M, Fiedler, W, Mayer, BJ & Nollau, P 2006, 'Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains.', NAT METHODS, Jg. 3, Nr. 9, 9, S. 737-744. https://doi.org/10.1038/nmeth917

APA

Dierck, K., Machida, K., Voigt, A., Thimm, J., Horstmann, M., Fiedler, W., Mayer, B. J., & Nollau, P. (2006). Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains. NAT METHODS, 3(9), 737-744. [9]. https://doi.org/10.1038/nmeth917

Vancouver

Dierck K, Machida K, Voigt A, Thimm J, Horstmann M, Fiedler W et al. Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains. NAT METHODS. 2006;3(9):737-744. 9. https://doi.org/10.1038/nmeth917

Bibtex

@article{ebb4184f4fa44653a1a62b406d31c084,
title = "Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains.",
abstract = "Deciphering global signaling networks is of great importance for the detailed understanding of cellular signaling processes controlling many important biological functions. Among signaling processes, tyrosine phosphorylation has a central role. At present, adequate techniques for the global characterization of the tyrosine phosphoproteome are lacking, particularly for the analysis of small amounts of protein. By combining the power of PCR amplification with the unique properties of Src homology region 2 (SH2) domains to specifically recognize tyrosine-phosphorylated proteins, we developed a new proteomic approach, termed oligonucleotide-tagged multiplex assay (OTM). For OTM, multiple SH2 domains are labeled by domain-specific oligonucleotide tags, applied as probes to complex protein mixtures in a multiplex reaction and phosphotyrosine-specific interactions are quantified by PCR. Using OTM we reproducibly quantified differential states of tyrosine phosphorylation with high sensitivity and specificity in small amounts of whole cellular extracts as demonstrated for various tumor cell lines and human leukemia samples.",
author = "Kevin Dierck and Kazuya Machida and Anja Voigt and Julian Thimm and Martin Horstmann and Walter Fiedler and Mayer, {Bruce J} and Peter Nollau",
year = "2006",
doi = "10.1038/nmeth917",
language = "Deutsch",
volume = "3",
pages = "737--744",
journal = "NAT METHODS",
issn = "1548-7091",
publisher = "NATURE PUBLISHING GROUP",
number = "9",

}

RIS

TY - JOUR

T1 - Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains.

AU - Dierck, Kevin

AU - Machida, Kazuya

AU - Voigt, Anja

AU - Thimm, Julian

AU - Horstmann, Martin

AU - Fiedler, Walter

AU - Mayer, Bruce J

AU - Nollau, Peter

PY - 2006

Y1 - 2006

N2 - Deciphering global signaling networks is of great importance for the detailed understanding of cellular signaling processes controlling many important biological functions. Among signaling processes, tyrosine phosphorylation has a central role. At present, adequate techniques for the global characterization of the tyrosine phosphoproteome are lacking, particularly for the analysis of small amounts of protein. By combining the power of PCR amplification with the unique properties of Src homology region 2 (SH2) domains to specifically recognize tyrosine-phosphorylated proteins, we developed a new proteomic approach, termed oligonucleotide-tagged multiplex assay (OTM). For OTM, multiple SH2 domains are labeled by domain-specific oligonucleotide tags, applied as probes to complex protein mixtures in a multiplex reaction and phosphotyrosine-specific interactions are quantified by PCR. Using OTM we reproducibly quantified differential states of tyrosine phosphorylation with high sensitivity and specificity in small amounts of whole cellular extracts as demonstrated for various tumor cell lines and human leukemia samples.

AB - Deciphering global signaling networks is of great importance for the detailed understanding of cellular signaling processes controlling many important biological functions. Among signaling processes, tyrosine phosphorylation has a central role. At present, adequate techniques for the global characterization of the tyrosine phosphoproteome are lacking, particularly for the analysis of small amounts of protein. By combining the power of PCR amplification with the unique properties of Src homology region 2 (SH2) domains to specifically recognize tyrosine-phosphorylated proteins, we developed a new proteomic approach, termed oligonucleotide-tagged multiplex assay (OTM). For OTM, multiple SH2 domains are labeled by domain-specific oligonucleotide tags, applied as probes to complex protein mixtures in a multiplex reaction and phosphotyrosine-specific interactions are quantified by PCR. Using OTM we reproducibly quantified differential states of tyrosine phosphorylation with high sensitivity and specificity in small amounts of whole cellular extracts as demonstrated for various tumor cell lines and human leukemia samples.

U2 - 10.1038/nmeth917

DO - 10.1038/nmeth917

M3 - SCORING: Zeitschriftenaufsatz

C2 - 16929320

VL - 3

SP - 737

EP - 744

JO - NAT METHODS

JF - NAT METHODS

SN - 1548-7091

IS - 9

M1 - 9

ER -