Proteomics strategy for quantitative protein interaction profiling in cell extracts.

Full 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 information

Author/s: Sharma, Kirti (K); Weber, Christoph (C); Bairlein, Michaela (M); Greff, Zoltán (Z); Kéri, György (G); Cox, Jürgen (J); Olsen, Jesper V (JV); Daub, Henrik (H);

Affiliation: Cell Signaling Group, Department of Molecular Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Nature methods (Nat Methods), published in United States. (Language: eng)

Reference: 2009-Oct; vol 6 (issue 10) : pp 741-4

Dates: Created 2009/09/30; Completed 2009/10/21;

PMID: 19749761, status: MEDLINE (last retrieval date: 10/21/2009, IMS Date: )

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