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  Quantitative interaction proteomics using mass spectrometry

Wepf, A., Glatter, T., Schmidt, A., Aebersold, R., & Gstaiger, M. (2009). Quantitative interaction proteomics using mass spectrometry. NATURE METHODS, 6(3), 203-205. doi:10.1038/NMETH.1302.

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 Creators:
Wepf, Alexander1, Author
Glatter, Timo2, Author                 
Schmidt, Alexander1, Author
Aebersold, Ruedi1, Author
Gstaiger, Matthias1, Author
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1external, ou_persistent22              
2ETH, Inst Mol Syst Biol, Dept Biol, Zurich, Switzerland, ou_persistent22              

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 Abstract: We present a mass spectrometry-based strategy for the absolute quantification of protein complex components isolated through affinity purification. We quantified bait proteins via isotope-labeled reference peptides corresponding to an affinity tag sequence and prey proteins by label-free correlational quantification using the precursor ion signal intensities of proteotypic peptides generated in reciprocal purifications. We used this method to quantitatively analyze interaction stoichiometries in the human protein phosphatase 2A network.

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 Dates: 2009
 Publication Status: Issued
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 Identifiers: ISI: 000263723300013
DOI: 10.1038/NMETH.1302
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Title: NATURE METHODS
Source Genre: Journal
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Pages: - Volume / Issue: 6 (3) Sequence Number: - Start / End Page: 203 - 205 Identifier: ISSN: 1548-7091