“Proteomics is essential for deciphering how molecules interact as a system and for understanding the functions of cellular systems in human disease; however, the unique characteristics of the human proteome, which include a high dynamic range of protein expression and extreme complexity due to a plethora of PTMs and sequence variations, make such analyses challenging. An emerging “top-down” MS-based proteomics approach, which provides a “bird’s eye” view of all proteoforms, has unique advantages for the assessment of PTMs and sequence variations. ”

Recent Publications

Fornelli L, Toby TK, Schachner LF, Doubleday PF, Srzentić K, et al. 2017. Top-down proteomics: Where we are, where we are going? Journal of Proteomics
Tran BQ, Barton C, Feng J, Sandjong A, Yoon SH, et al. 2016. Comprehensive glycosylation profiling of IgG and IgG-fusion proteins by top-down MS with multiple fragmentation techniques. Journal of Proteomics. 134:93–101
Dang X, Scotcher J, Wu S, Chu RK, Tolić N, et al. 2014. The first pilot project of the consortium for top-down proteomics: A status report. Proteomics. 14(10):1130–40
Gregorich ZR, Ge Y. 2014. Top-down proteomics in health and disease: Challenges and opportunities. Proteomics. 14(10):1195–1210
Smith LM, Kelleher NL, Proteomics TC for TD. 2013. Proteoform: a single term describing protein complexity. Nat Meth. 10(3):186–87
Tran JC, Zamdborg L, Ahlf DR, Lee JE, Catherman AD, et al. 2011. Mapping intact protein isoforms in discovery mode using top-down proteomics. Nature. 480(7376):254–58