Proteomics strategy for quantitative protein interaction profiling in cell extracts
Research output: Contribution to journal › Journal article › Research › peer-review
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.
Original language | English |
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Journal | Nature Methods |
Volume | 6 |
Issue number | 10 |
Pages (from-to) | 741-4 |
Number of pages | 3 |
ISSN | 1548-7091 |
DOIs | |
Publication status | Published - 2009 |
Externally published | Yes |
Bibliographical note
Keywords: Cell Extracts; Chromatography, Affinity; Mass Spectrometry; Protein Interaction Mapping; Proteome; Proteomics
ID: 19160448