Proteomics strategy for quantitative protein interaction profiling in cell extracts

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

Standard

Proteomics strategy for quantitative protein interaction profiling in cell extracts. / Sharma, Kirti; Weber, Christoph; Bairlein, Michaela; Greff, Zoltán; Kéri, György; Cox, Jürgen; Olsen, Jesper V; Daub, Henrik.

In: Nature Methods, Vol. 6, No. 10, 2009, p. 741-4.

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

Harvard

Sharma, K, Weber, C, Bairlein, M, Greff, Z, Kéri, G, Cox, J, Olsen, JV & Daub, H 2009, 'Proteomics strategy for quantitative protein interaction profiling in cell extracts', Nature Methods, vol. 6, no. 10, pp. 741-4. https://doi.org/10.1038/nmeth.1373

APA

Sharma, K., Weber, C., Bairlein, M., Greff, Z., Kéri, G., Cox, J., Olsen, J. V., & Daub, H. (2009). Proteomics strategy for quantitative protein interaction profiling in cell extracts. Nature Methods, 6(10), 741-4. https://doi.org/10.1038/nmeth.1373

Vancouver

Sharma K, Weber C, Bairlein M, Greff Z, Kéri G, Cox J et al. Proteomics strategy for quantitative protein interaction profiling in cell extracts. Nature Methods. 2009;6(10):741-4. https://doi.org/10.1038/nmeth.1373

Author

Sharma, Kirti ; Weber, Christoph ; Bairlein, Michaela ; Greff, Zoltán ; Kéri, György ; Cox, Jürgen ; Olsen, Jesper V ; Daub, Henrik. / Proteomics strategy for quantitative protein interaction profiling in cell extracts. In: Nature Methods. 2009 ; Vol. 6, No. 10. pp. 741-4.

Bibtex

@article{964d97a0457211df928f000ea68e967b,
title = "Proteomics strategy for quantitative protein interaction profiling in cell extracts",
abstract = "We report a proteomics strategy to both identify and quantify cellular target protein interactions with externally introduced ligands. We determined dissociation constants for target proteins interacting with the ligand of interest by combining quantitative mass spectrometry with a defined set of affinity purification experiments. We demonstrate the general utility of this methodology in interaction studies involving small-molecule kinase inhibitors, a tyrosine-phosphorylated peptide and an antibody as affinity ligands.",
author = "Kirti Sharma and Christoph Weber and Michaela Bairlein and Zolt{\'a}n Greff and Gy{\"o}rgy K{\'e}ri and J{\"u}rgen Cox and Olsen, {Jesper V} and Henrik Daub",
note = "Keywords: Cell Extracts; Chromatography, Affinity; Mass Spectrometry; Protein Interaction Mapping; Proteome; Proteomics",
year = "2009",
doi = "10.1038/nmeth.1373",
language = "English",
volume = "6",
pages = "741--4",
journal = "Nature Methods",
issn = "1548-7091",
publisher = "nature publishing group",
number = "10",

}

RIS

TY - JOUR

T1 - Proteomics strategy for quantitative protein interaction profiling in cell extracts

AU - Sharma, Kirti

AU - Weber, Christoph

AU - Bairlein, Michaela

AU - Greff, Zoltán

AU - Kéri, György

AU - Cox, Jürgen

AU - Olsen, Jesper V

AU - Daub, Henrik

N1 - Keywords: Cell Extracts; Chromatography, Affinity; Mass Spectrometry; Protein Interaction Mapping; Proteome; Proteomics

PY - 2009

Y1 - 2009

N2 - We report a proteomics strategy to both identify and quantify cellular target protein interactions with externally introduced ligands. We determined dissociation constants for target proteins interacting with the ligand of interest by combining quantitative mass spectrometry with a defined set of affinity purification experiments. We demonstrate the general utility of this methodology in interaction studies involving small-molecule kinase inhibitors, a tyrosine-phosphorylated peptide and an antibody as affinity ligands.

AB - We report a proteomics strategy to both identify and quantify cellular target protein interactions with externally introduced ligands. We determined dissociation constants for target proteins interacting with the ligand of interest by combining quantitative mass spectrometry with a defined set of affinity purification experiments. We demonstrate the general utility of this methodology in interaction studies involving small-molecule kinase inhibitors, a tyrosine-phosphorylated peptide and an antibody as affinity ligands.

U2 - 10.1038/nmeth.1373

DO - 10.1038/nmeth.1373

M3 - Journal article

C2 - 19749761

VL - 6

SP - 741

EP - 744

JO - Nature Methods

JF - Nature Methods

SN - 1548-7091

IS - 10

ER -

ID: 19160448