Rini, James M. - University of Toronto - Department of Biochemistry

个人简介

Dr. James Rini obtained his Ph.D. from the department of Medical Biophysics at the University of Toronto where he determined one of the first x-ray crystal structures of a protein-carbohydrate complex. He then did postdoctoral research with Dr. Ian Wilson at the Research Institute of Scripps Clinic where his work on anti-viral antibodies led to the discovery of new principles of immune recognition. As an independent researcher Dr. Rini has established an international reputation for his contributions in the areas of protein-carbohydrate interactions, animal lectins and glycosyltransferase structure and mechanism. He has written a number of important reviews in these areas and he is a contributor to the popular textbook Essentials of Glycobiology.

研究领域

The membrane and secreted proteins/glycoproteins of mammalian cells play critical roles in processes ranging from cell-cell communication and signalling to the recognition of foreign antigens. Specifically, our research efforts are focused on the study of such proteins in three broad areas, described below.

近期论文

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Simple piggyBac transposon-based mammalian cell expression system for inducible protein production. Li, Z, Michael, IP, Zhou, D, Nagy, A. and Rini, JM PNAS (2013), 110, 5004-5009 Read The x-ray crystal structure of human aminopeptidase N reveals a novel dimer and the basis for peptide processing. Wong, AH, Zhou, D, and Rini, JM J Biol Chem (2012), 287, 36804-36814 Read Structural and mechanistic characterization of Core 2 β1,6-N-acetylglucosaminyltransferase: a metal ion independent GT-A glycosyltransferase. Pak, JE, Satkunarajah, M, Seetharaman, J and Rini, JM J Mol Biol (2011), 414, 798-811 Read Structural insights into immune recognition of the Severe Acute Respiratory Syndrome Coronavirus S-protein receptor binding domain. Pak, JE, Sharon, C, Auperin, TC, Satkunarajah, M, Cameron, CM, Kelvin, DJ, Seetharaman, J, Cochrane, A, Plummer, FA, Berry, JD and Rini, JM. J Mol Biol (2009), 388, 815-23 Read N-glycans are direct determinants of CFTR folding and stability in secretory and endocytic membrane traffic. Glozman, R, Okiyoneda, T, Mulvihill, CM, Rini, JM, Barriere, H and Lukacs, GL J Cell Biol (2009), 184, 847-62 Read X-ray Crystal Structure of Rabbit N-Acetylglucosaminyltransferase I: Enzyme Mechanism and a New Protein Superfamily. Ünligil, UM, Zhou, S, Yuwaraj, S, Sarkar, M, Schachter, S. and Rini, JM EMBO J (2000), 19, 5269-5280 Read