Faculty
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Research Interests (Taken from Kelleher's current website) Our laboratory has three main areas of research: custom instrumentation for Fourier Transform Mass Spectrometry (FTMS), Nuclear Signaling and Natural Products. More specifically, our main interests lie in the enzymology of natural product biosynthesis, mass spectrometric-based studies of the "Histone Code," and development of Fourier Transform Mass Spectrometry (FTMS) for Top Down Proteomics (i.e. analyzing intact proteins directly; no proteases). A core activity is measuring chemical modifications to proteins in both hypothesis-driven and discovery modes. Our pioneering efforts in "Top Down" proteomics involve fragmenting intact protein ions in the gas phase and developing custom bioinformatics to characterize unexpected post-translational modifications (PTMs) in methane-producing microbes, yeast, and human cancer cells. In both human cell biology and antibiotic biosynthesis, key proteins harbor over 20 PTMs that present a "code" of biological logic written in the language of protein modifications. We construct, automate, and apply custom mass spectrometry and algorithms to detect and decode this logic.
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Selected Publications Endogenous peptide discovery of the rat circadian clock: a focused study of the suprachiasmatic nucleus by ultra-high performance tandem mass spectrometry. Lee JE, Atkins N Jr, Hatcher NG, Zamdborg L, Gillette MU, Sweedler JV, Kelleher NL. Mol Cell Proteomics. 2009 Nov 10. [Epub ahead of print] A proteomics approach to discovering natural products and their biosynthetic pathways. Bumpus SB, Evans BS, Thomas PM, Ntai I, Kelleher NL. Nat Biotechnol. 2009 Oct;27(10):951-6. Epub 2009 Sep 20.PMID: 19767731 [PubMed - in process] View all publications by Neil L. Kelleher listed in the National Library of Medicine (PubMed). Past and current IBiS students in blue |