@article{783080e3d5e54923a5984d8b0a1c08db,
title = "A protease for 'middle-down' proteomics",
abstract = "We developed a method for restricted enzymatic proteolysis using the outer membrane protease T (OmpT) to produce large peptides (>6.3 kDa on average) for mass spectrometry-based proteomics. Using this approach to analyze prefractionated high-mass HeLa proteins, we identified 3,697 unique peptides from 1,038 proteins. We demonstrated the ability of large OmpT peptides to differentiate closely related protein isoforms and to enable the detection of many post-translational modifications.",
author = "Cong Wu and Tran, {John C.} and Leonid Zamdborg and Durbin, {Kenneth R.} and Mingxi Li and Ahlf, {Dorothy R.} and Early, {Bryan P.} and Thomas, {Paul M.} and Sweedler, {Jonathan V.} and Kelleher, {Neil L.}",
note = "Funding Information: We sincerely thank current and former members of the Kelleher and Sweedler research groups, especially B. Evans, P. Chu, P. Compton, A. Catherman, S. Sweet, I. Ntai, J. Lee, A. Vellaichamy and K. Catherman, for technical support and insightful suggestions, P. Yau and B. Imai from the Protein Sciences Facility at the University of Illinois for the synthesis of the fluorogenic substrate and M. Burke for the access to a fluorimeter. The project was supported by the US National Institutes of Health through awards R01 GM067193, P30 DA018310 and F30 DA026672, by the National Science Foundation through award DMS 0800631 and by the Chicago Biomedical Consortium with support from the Searle Funds at the Chicago Community Trust.",
year = "2012",
month = aug,
doi = "10.1038/nmeth.2074",
language = "English (US)",
volume = "9",
pages = "822--824",
journal = "Molecular Pharmaceutics",
issn = "1543-8384",
publisher = "American Chemical Society",
number = "8",
}