Robert L. Moritz
Ph.D., University of Melbourne, Australia


Phone: 206-732-1244
Office: 123

Email: rmoritz@systemsbiology.org

Dr. Robert Moritz, a native of Australia, joined the ISB faculty in late 2008 as Associate Professor and Director of Proteomics. Dr. Moritz began his work in 1983 in the Joint Protein Structure laboratory of Prof. Richard J. Simpson (JPSL-Ludwig Institute for Cancer Research, and The Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia). During his 25 years at JPSL, Dr. Moritz designed and implemented a number of technologies currently used in many proteomics laboratories across the globe. Examples include technologies such as the development of micro-chromatography for proteomics from the late 1980's to its current day implementation, a micro-fractionation technique widely used by many laboratories worldwide. His collaborative research into cytokine biochemistry, protein-receptor chemistry and cellular biochemistry culminated in the novel identification of a number of proteins (e.g., IL-6, IL-9 A33 ligand, DIABLO, as well as several others), their interacting partners, and 3-dimensional structures of their cell surface receptors important in human health concerns such as cancer and inflammation. During his time at JPSL, Dr. Moritz progressed through the ranks whilst obtaining his Bachelor's degree in Biochemistry with first-class Honors, and his Ph.D., from the University of Melbourne.

Dr. Moritz has brought wide-ranging skills and expertise to ISB, much of it drawn from his Australian experience. There, in 2005, he conceptualized a shared proteomics high-performance computing system, organized a consortia of proteomic scientists from all states in Australia, and proposed a computational system specifically for proteomics data analysis for all Australian researchers to access. For this work, in 2006, he was awarded an enabling grant from the Australian National Health and Medical Research Council worth AUS$2M. With that award, he established a bioinformatics center in Australia that enabled proteomic researchers anywhere in the country to analyze mass spectrometry data. It was the first effort on a national scale to bring proteomic data analysis and algorithms to any researcher in the whole country without the need for them to build their own bioinformatics group. In late 2006, the Australian Proteomics Computational Facility (APCF, www.apcf.edu.au) was inaugurated, and Dr. Moritz remains as Director of the APCF. The dedicated proteomics data analysis facility is equipped with a 1000 CPU high-performance computing cluster, and full-time software engineers for the continued development of proteomics algorithms and data validation. This facility serves all researchers in Australia and others regardless of their global geographical location. He is continuing that work at ISB by expanding the ISB proteomics centre into a national facility with online tools for data analysis.

Dr. Moritz collaborates with a wide variety of researchers on specific human diseases. For example, when mass spectrometry replaced earlier techniques such as Edman degradation for protein identification, he embarked on several projects to find proteins that are shed into the blood by colorectal cancers. As part of these projects, Dr. Moritz developed a series of tools to separate particular classes of proteins from complex samples, tools that he will implement and further develop at ISB. Specifically, Dr. Moritz concentrates on development of quantitative analytical protein chemistry and proteomic techniques for the purpose of profiling cellular protein diseases such as atherosclerosis, inflammation and colorectal cancer. By the discovery of organ specific markers for these diseases, early detection strategies can be employed to benefit human health and wellbeing.

Dr. Moritz has authored more than 140 peer-reviewed papers, and is a holder of several patents on his research interests in discovery protein science and the relationship of aberrant protein expression and its function in human disease.

Key publications:

Boddey, J.A., Moritz, R.L., Simpson R.J and Cowman, A.F. Role of the Plasmodium Export Element in trafficking parasite proteins to the infected erythrocyte. (2009) Traffic 10:285-299

Simpson RJ, Bernhard OK, Greening DW, Moritz RL. 2008. Proteomics-driven cancer biomarker discovery: looking to the future. Current Opinion in Chemical Biology 12:72-77.

Greening DW, Glenister KM, Kapp EA, Moritz RL, Sparrow RL, Lynch GW, Simpson RJ. 2008. Comparison of human platelet membrane-cytoskeletal proteins with the plasma proteome: towards understanding of the platelet-plasma nexus. Proteomics - Clinical Applications 2:63-77.

Moritz R.L., Skandarajah AR, Ji H, Simpson RJ. 2005. Proteomic analysis of colorectal cancer: prefractionation strategies using two-dimensional free-flow electrophoresis. Comparative and Functional Genomics 6:236-243.

Moritz, R.L., Ji, H., Schütz, F., Connolly, L.M. Kapp E.A., Speed, T.P. and Simpson R.J A Proteome fractionation strategy using continuous free-flow electrophoresis coupled off-line to rapid reversed-phase high-performance liquid chromatography. (2004) Anal. Chem., 76, 4811-4824.

Varghese, J.N., Moritz, R.L., Lou, M-Z, vanDonkelaar, A., Ji, H., Ivancic, N., Branson, K.M., Hall, N.E., Simpson, R.J. Structure of the extra-cellular domains of the human Interleukin-6 Receptor α Chain. (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 15959-15964.

Moritz, R.L., Hall N.E., Connolly L.M., and Simpson, R.J. (2001) Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130. J Biol Chem. 276: 8244-8253.

Verhagen, A., Ehert, P.G., Silke, J., Pakusch, M., Connolly, L.M., Reid, G.E., Moritz, R.L., Simpson, R.J., and Vaux, D.L. (2000) Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to an antagonizing inhibitor of apoptosis (IAP) protein. Cell. 102:43-53.

Moritz, R. L., Ward, L. D., Tu, G-F, Fabri, L. J., Ji, H. Yasukawa, K. and Simpson, R.J. (1999) The N-terminus of gp130 is critical for the formation of the high affinity interleukin-6 receptor. Growth Factors. 16:265-278