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Assistant Professor of Biology
Ph.D. (Computational and Structural Biology), University of Cambridge; M.S. (Mathematical Biology), University College London; Masters (Biochemistry/Molecular Biology), Jena, Germany.
Office Address:
| New York University |
| Department of Biology |
| Center for Genomics and Systems Biology |
| 12 Waverly Place, Room 403 |
| New York, NY 10003 |
Email:
Phone: 212-998-3976
List of Publications from Pubmed
List of citations from Google Scholar
Lab Homepage
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Research
My research revolves around proteins, their properties, evolution, and expression patterns. I am a systems biologist who uses statistical and computational tools, large-scale quantitative mass spectrometry, and molecular biology techniques to study the dynamics of the cellular proteome.
Quantitative shotgun proteomics
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Until recently, it was impossible to accurately estimate the absolute and relative concentrations of thousands of proteins in complex biological samples. Our quantitative proteomics technology called APEX (Absolute Protein Expression Index, Nature Biotech, 2007 25(1)) allows us to do so – for everything from bacteria to yeast and human. Mass spectrometry data is highly complex, and we continuously improve our data mining methods with respect to the identification and quantification of proteins. For example, in MSpresso and MSnet (Bioinformatics 2009a, b), we use mRNA expression data and protein functional network information, respectively, to increase the number of proteins that were identified by mass spectrometry analysis.
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The dynamics of protein expression
The expression levels of proteins are determined by transcription, translation, mRNA and protein stability, and these processes are regulated by a plethora of mechanisms. Thus, the relationship between protein and mRNA expression levels varies across organisms and sets of proteins (Mol BioSystems, 2009 5(12)). Using yeast and human cell lines, we characterize the proteome and transcriptome under normal conditions and in response to stimuli. Time course data allows us to describe cellular processes as dynamical systems and will enable us to better understand protein expression regulation – both mathematically and biologically.
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Proteomics characterization of translation regulators
The human genome encodes ~600 proteins with RNA-binding domains, and many of these proteins are putative translation regulators. Using quantitative proteomics approaches and complementary molecular biology techniques, we characterize the impact of RNA-binding proteins on the 'translation regulatory network'. One example is Musashi-1 which is a key regulator involved in brain tumor formation, and we analyze its impact on the human proteome and transcriptome. This project is carried out in collaboration with Luiz Penalva (UTexas San Antonio).
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Areas of Research/Interest
mass spectrometry, quantitative proteomics, dynamical systems, translation regulation, stress response, protein evolution
Fellowships/Honors
Human Frontier Science Program (2005-2008); Boehringer Ingelheim Fonds Pre-doctoral Fellowship (2001-2004); German National Merit Foundation (1998-2000)
Publications
Protein abundances are more conserved than mRNA abundances across diverse taxa.
Proteomics (2010 Dec)
Laurent JM, Vogel C, Kwon T, Craig SA, Boutz DR, Huse HK, Nozue K, Walia H, Whiteley M, Ronald PC, Marcotte EM |
Genomic analyses of musashi1 downstream targets show a strong association with cancer-related processes.
J Biol Chem (2009 May 1)
de Sousa Abreu R, Sanchez-Diaz PC, Vogel C, Burns SC, Ko D, Burton TL, Vo DT, Chennasamudaram S, Le SY, Shapiro BA, Penalva LO |
The APEX Quantitative Proteomics Tool: generating protein quantitation estimates from LC-MS/MS proteomics results.
BMC Bioinformatics (2008)
Braisted JC, Kuntumalla S, Vogel C, Marcotte EM, Rodrigues AR, Wang R, Huang ST, Ferlanti ES, Saeed AI, Fleischmann RD, Peterson SN, Pieper R |
Email update requests to
fas.bio.computing@nyu.edu
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