High confidence determination of specific protein-protein interactions using quantitative mass spectrometry.

@article{citeulike:2959649, abstract = {In recent years, interactions between proteins have successfully been determined by mass spectrometry. A limitation of this technology has been the need for extensive purification, which restricts throughput and implies a tradeoff between specificity and the ability to detect weak or transient interactions. Quantitative proteomics sidesteps this problem by directly comparing specific and control pull-downs. Specific interaction partners are revealed by their quantitative ratios rather than by gel-based visualization and can be retrieved from a vast excess of background proteins. This principle is revolutionizing the protein interaction field as demonstrated by recent applications in fields as diverse as tyrosine signaling pathways, cell adhesion, and chromatin biology.}, address = {Department of proteomics and signal transduction, Max-Planck Institute for Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.}, author = {Vermeulen, Michiel and Hubner, Nina C C. and Mann, Matthias }, citeulike-article-id = {2959649}, doi = {10.1016/j.copbio.2008.06.001}, issn = {0958-1669}, journal = {Current opinion in biotechnology}, keywords = {interaction, proteomics, quantitation}, month = {June}, posted-at = {2008-07-03 16:06:53}, priority = {2}, title = {High confidence determination of specific protein-protein interactions using quantitative mass spectrometry.}, url = {http://dx.doi.org/10.1016/j.copbio.2008.06.001}, year = {2008} }

TY - JOUR ID - citeulike:2959649 L3 - citeulike-article-id:2959649 TI - High confidence determination of specific protein-protein interactions using quantitative mass spectrometry. JF - Current opinion in biotechnology AD - Department of proteomics and signal transduction, Max-Planck Institute for Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany. SN - 0958-1669 N2 - In recent years, interactions between proteins have successfully been determined by mass spectrometry. A limitation of this technology has been the need for extensive purification, which restricts throughput and implies a tradeoff between specificity and the ability to detect weak or transient interactions. Quantitative proteomics sidesteps this problem by directly comparing specific and control pull-downs. Specific interaction partners are revealed by their quantitative ratios rather than by gel-based visualization and can be retrieved from a vast excess of background proteins. This principle is revolutionizing the protein interaction field as demonstrated by recent applications in fields as diverse as tyrosine signaling pathways, cell adhesion, and chromatin biology. KW - interaction KW - proteomics KW - quantitation AU - Vermeulen, Michiel AU - Hubner, Nina C AU - Mann, Matthias PY - 2008/06/27/ UR - http://dx.doi.org/10.1016/j.copbio.2008.06.001 ER -