Abstract
Characterization and functional annotation of the large number of proteins predicted from genome sequencing projects poses a major scientific challenge. Whereas several proteomics techniques have been developed to quantify the abundance of proteins, these methods provide little information regarding protein function. Here, we present a gel-free platform that permits ultrasensitive, quantitative, and high-resolution analyses of protein activities in proteomes, including highly problematic samples such as undiluted plasma. We demonstrate the value of this platform for the discovery of both disease-related enzyme activities and specific inhibitors that target these proteins. © 2005 by The National Academy of Sciences of the USA.
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Okerberg, E. S., Wu, J., Zhang, B., Samii, B., Blackford, K., Winn, D. T., … Patricelli, M. P. (2005). High-resolution functional proteomics by active-site peptide profiling. Proceedings of the National Academy of Sciences of the United States of America, 102(14), 4996–5001. https://doi.org/10.1073/pnas.0501205102
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