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BIOCOMP'08 Keynote - Prof. Vladimir N. Uversky
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"Unfoldomics" of Human Diseases
Professor Vladimir N. Uversky Senior Research Professor Indiana University School of Medicine, Indianapolis, Indiana, USA Russian Academy of Sciences, Moscow, Russia Date: July 15, 2008 Time: 12:50 PM Location: Ballroom 5 |
Intrinsically disordered proteins lack stable tertiary and/or secondary structure under physiological conditions in vitro. They are highly abundant in nature, being often involved in functions associated with regulation, recognition, signaling and control. Functions of intrinsically disordered proteins may arise from the specific disorder form, from inter-conversion of disordered forms, or from transitions between disordered and ordered conformations. Intrinsically disordered proteins are key players in protein-protein interaction networks and are highly abundant among hubs. Numerous intrinsically disordered proteins are involved in the pathogenesis of such diseases as cancer, cardiovascular disease, amyloidoses, neurodegenerative diseases, diabetes and others. Overall, there is an intriguing interconnection between intrinsic disorder, cell signaling and human diseases, which suggests that many diseases may result not only from protein misfolding, but also from misidentification and missignaling. Therefore, new strategies are required to implement intrinsically disordered proteins as novel targets for drugs modulating protein-protein interactions.
Dr. Uversky received broad training, with an MS in Physics (Leningrad State University, Russia, 1986), a PhD (Moscow Institute of Technical Physics, 1991) and a DSc in Biophysics (Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences, 1998) and with pre- and postdoctoral research in Structural Biology, Biochemistry and Biophysics (1991-1998, Institute of Protein Research, Russian Academy of Sciences). Dr. Uversky uses molecular biophysics methods to study protein folding, misfolding and non-folding. He has found that many biologically active proteins do not have rigid structure and are often involved in human diseases. He is known for his work on structural characterization of partially folded and intrinsically disordered proteins and development of novel tools to study protein folding,misfolding and non-folding. While he continues to use biophysics, more recently Dr. Uversky has focused on the development and use of bioinformatics methods for the study of intrinsically disordered proteins.
