High-resolution functional proteomics by active-site peptide profiling.

by: ES Okerberg, J Wu, B Zhang, B Samii, K Blackford, DT Winn, KR Shreder, JJ Burbaum, MP Patricelli

Proc Natl Acad Sci U S A, Vol. 102, No. 14. (5 April 2005), pp. 4996-5001.

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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.

@article{citeulike:1902577, 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.}, address = {ActivX Biosciences, 11025 North Torrey Pines Road, Suite 120, La Jolla, CA 92037, USA.}, author = {Okerberg, E. S. and Wu, J. and Zhang, B. and Samii, B. and Blackford, K. and Winn, D. T. and Shreder, K. R. and Burbaum, J. J. and Patricelli, M. P. }, citeulike-article-id = {1902577}, doi = {http://dx.doi.org/10.1073/pnas.0501205102}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, keywords = {method, proteomics, targetbeads}, month = {April}, number = {14}, pages = {4996--5001}, posted-at = {2007-11-12 12:20:53}, priority = {0}, title = {High-resolution functional proteomics by active-site peptide profiling.}, url = {http://dx.doi.org/10.1073/pnas.0501205102}, volume = {102}, year = {2005} }

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TY - JOUR ID - citeulike:1902577 L3 - citeulike-article-id:1902577 N2 - 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. IS - 14 JF - Proc Natl Acad Sci U S A SN - 0027-8424 AD - ActivX Biosciences, 11025 North Torrey Pines Road, Suite 120, La Jolla, CA 92037, USA. EP - 5001 TI - High-resolution functional proteomics by active-site peptide profiling. VL - 102 SP - 4996 KW - method KW - proteomics KW - targetbeads AU - Okerberg, ES AU - Wu, J AU - Zhang, B AU - Samii, B AU - Blackford, K AU - Winn, DT AU - Shreder, KR AU - Burbaum, JJ AU - Patricelli, MP PY - 2005/04/05/ UR - http://dx.doi.org/10.1073/pnas.0501205102 ER -

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