Proteomics strategy for quantitative protein interaction profiling in cell extracts. Export

@article{citeulike:5998182, 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 = {Sharma, Kirti and Weber, Christoph and Bairlein, Michaela and Greff, Zolt\'{a}n and K\'{e}ri, Gy\"{o}rgy and Cox, J\"{u}rgen and Olsen, Jesper V. and Daub, Henrik}, citeulike-article-id = {5998182}, citeulike-linkout-0 = {http://dx.doi.org/10.1038/nmeth.1373}, citeulike-linkout-1 = {http://www.f1000.com/article/id/1165810}, citeulike-linkout-2 = {http://dx.doi.org/10.1038/nmeth.1373}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19749761}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19749761}, day = {13}, doi = {10.1038/nmeth.1373}, issn = {1548-7105}, journal = {Nature methods}, keywords = {interaction, methods, proteomics}, month = {October}, number = {10}, pages = {741--744}, posted-at = {2009-11-07 00:37:06}, priority = {2}, publisher = {Nature Publishing Group}, title = {Proteomics strategy for quantitative protein interaction profiling in cell extracts.}, url = {http://dx.doi.org/10.1038/nmeth.1373}, volume = {6}, year = {2009} }

TY - JOUR ID - citeulike:5998182 L3 - citeulike-article-id:5998182 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. IS - 10 JF - Nature methods SN - 1548-7105 EP - 744 TI - Proteomics strategy for quantitative protein interaction profiling in cell extracts. PB - Nature Publishing Group VL - 6 SP - 741 KW - interaction KW - methods KW - proteomics AU - Sharma, Kirti AU - Weber, Christoph AU - Bairlein, Michaela AU - Greff, Zoltán AU - Kéri, György AU - Cox, Jürgen AU - Olsen, Jesper AU - Daub, Henrik PY - 2009/10/13/ UR - http://dx.doi.org/10.1038/nmeth.1373 ER -