Nature Cell Biology 7, 750 - 757 (2005)
doi:10.1038/ncb0805-750
Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomicsDonald S. Kirkpatrick1, Carilee Denison1
& Steven P. Gygi21
Donald S. Kirkpatrick and Carilee Denison are in the Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. 2
Steven P. Gygi is in the Department of Cell Biology and the Taplin Biological Mass Spectrometry Facility, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. Steven_Gygi@hms.harvard.edu
Mass-spectrometry-based proteomics has become an essential tool for the qualitative and quantitative analysis of cellular systems. The biochemical complexity and functional diversity of the ubiquitin system are well suited to proteomic studies. This review summarizes advances involving the identification of ubiquitinated proteins, the elucidation of ubiquitin-modification sites and the determination of polyubiquitin chain linkages, as well as offering a perspective on the application of emerging technologies for mechanistic and functional studies of protein ubiquitination.
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