Microsoft PowerPoint - 2007 Prion poster - 4.ppt
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چکیده
The authors would like to thank PrioNet Canada for the opportunity to present these findings, the authors of the AGADIR method for providing their software, and NSERC Canada for their financial support. Acknowledgements and References Prion protein misfolding is responsible for the Transmissible Spongiform Encephalopathies (TSE) [1]. Experimental investigations suggest that the pathogen of prion diseases is characterized by the unfolding of normal prion (PrPC) followed by misfolding into an infectious scrapie isoform (PrPSc) [2]. We present novel in-silico results that identify potential factors that predispose PrPC to misfold into PrPSc using computational methods. In-silico exploration of possible factors involved in the misfolding process is a crucial first step in understanding and (eventually) treating TSEs, as the number of possible factors is literally astronomical. In-silico techniques identify candidate factors for further wet-lab investigations, providing an enormous gain in efficiency compared to manual wet-lab searches through all the possible factors. Background and Motivation
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[1] Thieffry et’al (1998). BioEssays 20:433-440. [2] Teichmann & Babu (2004). Nat. Gen. 36:492-496. [3] Martínez-Antonio & Collado-Vides (2003). Curr. Opin. Microbiol. 6:482-489. [4] http://regulondb.ccg.unam.mx/index.html [5] http://dbtbs.hgc.jp/ [6] Yu et’ al (2004). Genome Res. 14:1107-1118. [7] http://www.weizmann.ac.il/mcb/UriAlon/groupNetworkMotifSW.html [8] de Hoon, et’al (2004). Bioinfo...
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