RESEARCH HIGHLIGHTS Research Publications

The Alberta Prion Research Institute has provided over $42 million in research funding to date that has led to collaborations, discoveries and dozens of research publications.

The names in bold are researchers who have received funding from the Alberta Prion Research Institute.




Arnot, C., Laate, E., Unterschultz, J. & Adamowicz, W. 2009. Chronic Wasting Disease (CWD) Potential Economic Impact on Cervid Farming in Alberta. Journal of Toxicology and Environmental Health. 72(17-18):1014-7.


Ding, Y., Veeman, M.W. & Adamowicz, V. 2009. BSE and the Dynamics of Beef Consumption: Influences of Habits and Trust. Conference paper. AGECON search.


Ding, Y., Veeman, M. & Adamowicz, V. 2011. Habit, BSE and the Dynamics of Beef Consumption. Canadian Journal of Agricultural Economics. 59(3):337-59.





Aiken, J. 2010. One Health for One World: A Compendium of Case Studies. 105 pages. Report to Public Health Agency of Canada - contributed a section.


Johnson, C.J., McKenzie, D., Pedersen, J.A. & Aiken, J.M. 2011. Meat and bone meal and mineral feed additives may increase the risk of oral prion disease transmission. Journal of Toxicology and Environmental Health. 74(2-4):161-6.


Johnson, C.J., Aiken, J.M., McKenzie, D., Samuel, M.D. & Pedersen, J.A. 2012. Highly Efficient Amplification of Chronic Wasting Disease Agent by Protein Misfolding Cyclic Amplification with Beads (PMCAb). PLoS ONE. 7(4):e35383.


McKenzie, D. & Aiken, J. 2012. Prion Diseases. Guide to Foodborne Pathogens. Eds. R.G. Labbe and S. Garcia. John Wiley and Sons.





Fleisch, V.C., Fraser, B. & Allison, W.T. 2011. Investigating regeneration and functional integration of CNS neurons: Lessons from zebrafish genetics and other fish species. Biochimica et Biophysica Acta: Molecular Basis of Disease. 1812(3):364-80.


Allison, W.T.  2011. Preface: Zebrafish models of Neurology. Biochimica et Biophysica Acta: Molecular Basis of Disease. 1812(3):333-4.


Fleisch, V.C., Leighton, P.L.A., Wang, H., Pillay, L.M., Ritzel R.G., Bhinder, G., Roy, B., Tierney, K.B., Ali, A.J. Waskiewicz, D.W. & Allison, W.T. 2013. Targeted mutation of the gene encoding prion protein in zebrafish reveals a conserved role in neuron excitability. Neurobiology of Disease. 55:11-25. 


Pillay, L.M., Selland, L.G., Fleisch, V.C., Leighton, P.L.A., Cheng, C.S., Famulski, J.K., Ritzel, R.G., March, L.D., Wang, H., Allison, W.T. & Waskiewicz, A.J. 2013. Evaluating the mutagenic activity of targeted endonucleases containing a Sharkey FokI cleavage domain variant in zebrafish. Zebrafish. 10(3):353-64.


Duval, M.G., Gilbert, M.J.H., Watson, D.E., Zerulla, T.C., Tierney, K.B. & Allison, W.T. 2014. Growth Differentiation Factor 6 as a putative risk factor in neuromuscular degeneration. PLoS ONE 9(2): e89183.





Xu, S., McAllister, T.A., Leonard, J.J., Grant, O.G. & Belosevic, M. 2010. Development of a laboratory-scale composter to assess microbial communities involved in decomposition of specified risk material. Compost Science and Utilization.18:255-65.





Gibbs, S.J. & Braun, J.E.A. 2008. Emerging Roles of J Proteins in Neurodegenerative Disorders. Neurobiology of Disease. 32(2):196-9.


Zhao, X., Braun, A.P. & Braun, J.E.A. 2008. Biological Roles of Neural J Proteins. Cellular and Molecular Life Sciences. 65(15):2385-96.


Gibbs, S., Barren, B., Beck, K.E., Profit, J., Zhao, X., Noskova, T., Braun, A.P., Artemyev, N.O. & Braun J.E.A. 2009. Hsp40 Transiently Assembles with the CSPα Chaperone Complex upon induction of the heat shock response. PLoS ONE. 4(2):e4595.


Rosales-Hernandez, A., Beck, K.E., Zhao, X., Braun, A.P. & Braun, J.E.A. 2009. Rdj2 (DnaJA2) chaperones neural G protein signaling pathways. Cell Stress & Chaperones. 14(1):71-82.


Carnini, A., Casha, S., Yong, V.W., Hurlbert, R.J. & Braun, J.E.A. 2010. Reduction of PrPC in Human Cerebrospinal Fluid after Spinal Cord Injury. Prion. 4:80-6.





Wilson, G., Nakada, S.M., Bollinger, T.K., Pybus, M.J., Merrill, E.H. & Coltman, D.W. 2009. Polymorphisms at the PRNP Gene Influence Susceptibility to Chronic Wasting Disease in Two Species of Deer (Odocoileus Spp.) in Western Canada. Journal of Toxicology and Environmental Health, Part A: Current Issues. Volume 72, Issue 17-18.


Cullingham, C.I., Merrill, E.H., Pybus, M., Bollinger, T.K., Wilson, G.D. & Coltman, D.W. 2011. Broad and fine-scale genetic analysis of white-tailed deer populations: estimating the relative risk of chronic wasting disease spread. Evolutionary Applications. 4:116-31.


Cullingham, C.I., Nakada, S.M., Merrill, E.H., Bollinger, T.K., Pybus, M.J. & Coltman, D.W. 2011. Multi-scale population genetic analysis of mule deer (Odocoileus hemionus hemionus) in western Canada sheds new light on chronic wasting disease spread. CAD Journal of Zoology. 89(2):134-47.  


Habib, T.J., Merrill, E.H., Pybus, M.J. & Coltman, D.W. 2011. Modelling landscape effects on density-contact rate relationships of deer in eastern Alberta: implications for chronic wasting disease. Ecological Modeling. 222:2722-32.


Rees, E. E., Merrill, E.H., Bollinger, T. K., Hwang, Y. T., Pybus, M. & Coltman, D. 2012. Targeting the detection of chronic wasting disease using the hunter harvest during early phases of an outbreak in Saskatchewan, Canada. Preventive Veterinary Medicine. 104:149-59.





Simon, S.L.R., Lamoureux, L., Plews, M., Stobart, M., LeMaistre, J., Ziegler, U., Czub, S., Graham, C., Groschup, M. & Knox, J.D. 2008. The identification of disease-induced biomarkers in the urine of BSE infected cattle. Proteome Science. 6:23.


Dudas, S., Yang, J., Graham, C., Czub, M., McAllister, T.A., Coulthart, M.B. & Czub, S. 2010. Molecular, biochemical and genetic characterizations of BSE in Canada. PLoS ONE. 5(5):e10638.


Plews, M., Lamoureux, L., Simon, S.L.R., Graham, C., Ruddat, V., Czub, S. & Knox, J.D.  2011. Factors Affecting the Accuracy of Urine-Based Biomarkers of BSE. Proteome Science. 9:6.


Lamoureux, L., Simon, S.L.R., Plews, M., Stobart, M., Groschup, M., Czub, S., Graham, C. & Knox, J.D. 2011. Analysis of Clusterin Glycoforms in the Urine of BSE Infected Fleckvieh-Simmental Cows. Journal of Toxicology and Environmental Health. 74(2-4):138-45.


Lamoureux, L., Simon, S., Plews, M., Ruddat, V., Brunet, S., Graham, C., Czub, S. & Knox, J.D. 2013. Urine proteins identified by two-dimensional differential gel electrophoresis facilitate the differential diagnoses of scrapie. PLoS One. 8(5): e64044.


Vrentas, C., Greenlee, J., Baron, T., Caramelli, M., Czub, S. & Nicholson, E. 2013. Stability properties of PrPSc from cattle with experimental transmissible spongiform encephalopathies: use of a rapid whole homogenate, protease-free assay. BMC Veterinary Research. 9:167. 





Gao, T.J., Bowlby, E., Tong, Y.P., Wu, J.T.Y., Wong, L., R.J., Pang, X.L. & Li, X. 2012. Evaluation of the Matrix Effect of Thermophilic anaerobic Digestion on Inactivation of Infectious Laryngotracheitis Virus Using Real-Time PCR and Viral Cell Culture. Bioresource Technol. 110:692-6.





Aguib, Y., Heiseke, A., Gilch, S., Riemer, C., Baier, M., Schätzl, H.M. & Ertmer, A. 2009. Autophagy induction by trehalose counter-acts cellular prion infection. Autophagy. 5(3):361-9.


Bach, C., Gilch, S., Rost, R., Greenwood, A., Horsh, M., Haji, G.M., Brodesser, S., Facius, A., Schadler, S., Sandhoff, K., Beckers, J., Leib-Mosch, C., Schätzl, H. & Vorbert, I. 2009. Prion-induced activation of cholesterogenic gene expression by Srebp2 in neuronal cells. Journal of Biological Chemistry. 284(45):31260-9.


Gilch, S. & Schätzl, H.M. 2009. Aptamers against prion proteins. Cellular and Molecular Life Sciences. 66(15):2445-55.


Gilch, S., Bach, C., Lutzny, G., Vorberg, I. & Schätzl, H.M. 2009. Inhibition of cholesterol recycling impairs cellular PrPSc propagation. Cellular and Molecular Life Sciences. 66(24):3979–91.


Gilch, S., Krammer, C., Vorberg, I. & Schätzl, H.M. 2009. Therapy in prion diseases: from molecular and cellular biology to therapeutic targets. Infectious Disorders-Drug Targets. 9(1):3-14.


Judith, M., Brameier, M., Schmädicke, A.C., Gilch, S., Schätzl, H.M. & Motzkus, D. 2012. A genome-wide survey for prion-regulated miRNAs associated with cholesterol homeostasis. BMC Genomics. 13:486.


Lisa, S., Domingo, B., Martinez, J., Gilch, S., Llopis, J.F., Schätzl, H.M. & Gasset, M. 2012. Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms. J Biol Chem. 287:36693-701.


John, T.R., Schätzl, H.M. & Gilch, S. 2013. Early detection of chronic wasting disease in urine of pre-symptomatic deer by real-time quaking-induced conversion assay. Prion. 7(3):253–8.  





Jonge, J.D., Trijp, H.V., Goddard, E. & Frewer, L. 2008. Consumer Confidence in the Safety of Food in Canada and the Netherlands: The Validation of a Generic Framework. Food Quality and Preference. 19(5):439-51.


Maynard, L.J., Goddard, E. & Conley, J. 2008. Impact of BSE on Beef Purchases in Alberta and Ontario Quick-Serve Restaurants. Canadian Journal of Agricultural Economics. 56(3):337-51.


Boyd, A.D. & Jardine, C.G. 2011. Did public risk perspectives of mad cow disease reflect media representations and actual outcomes? Journal of Risk Research. 14(5):615-30. (Acknowledgement of Alberta Prion Research Institute support)


Drescher, L., Herzfeld, T., Jonge, D.J. & Goddard, E. 2012. Consumer's states trust in the food industry and processed meat purchases. Agriculture and Human Values. 29(4):507-17.





Khaniya, B., Almeida, L., Basu, U., Taniguchi, M., Williams, J.L., Barreda, D.R., Moore, S.S. & Guan, L.L. 2009. Microarray Analysis of Differentially Expressed Genes from Peyer's Patches of Cattle Orally Challenged with Bovine Spongiform Encephalopathy. Journal of Toxicology and Environment. 72(17-18):1008-13.  


Almeida, L.M., Basu, U., Khaniya, B., Taniguchi, M., Williams, J.L., Moore, S.S. & Guan, L.L. 2011. Gene expression in the medulla following oral infection of cattle with bovine spongiform encephalopathy. Journal of Toxicology and Environmental Health. 74(2-4):110-26.


Basu, U., Almeida, L.M., Olson, N.E., Meng, Y., Williams, J.L., Moore, S.S. & Guan, L.L. 2011. Transcriptome analysis of the medulla tissue from cattle in response to bovine spongiform encephalopathy using digital gene expression-Tag Profiling. Journal of Toxicology and Environmental Health. 74(2-4):127-37.      





Li, L., Kaslowski, K., Waegner, B., Rashid, T., Yeung, T., Holmes, C.F.B. & Ballermann, B.J. 2007. Phosphorylation of TIMAP by glycogen synthase 3 activates its associated protein phosphatase 1 activity. Journal of Biological Chemistry. 282:25960-9.


Carr, G., Raszek, M., Van Soest, R., Matainho, T., Shopik, M., Holmes, C.F.B. & Andersen, R.J. 2007. Protein phosphatase inhibitors isolated from Spongia Irregularis Collected in Papua New Guinea. Journal of Natural Products. 70(11):1812-5.





Swayampakula, M., Baral, P., Aguzzi, A., Kav, N. & James, M. 2013. The crystal structure of an octapeptide repeat of the prion protein in complex with a fab fragment of the POM2 antibody. Protein Science. 22(7):893-903.


Sonati, T., Reimann, R., Falsig, J., Baral, P., O’Connor, T., Hornemann, S., Yaganoglu, S., Li, B., Herrmann, U., Wieland, B., Swayampakula, M., Rahman, M. H., Das, D., Kav, N., Riek, R., Liberski, P., James, M. & Aguzzi, A. 2013. The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein. Nature. 501(7465):102-6.


Baral, P., Swayampakula, M., Rout, R.K., Kav, N., Spyracopoulos, L., Aguzzi, A. & James, M. 2014. Structural basis of prion inhibition by phenothiazine compounds. Structure. 22(2):291-303.





Alier, K., Li, Z., MacTavish, D., Westaway, D. & Jhamandas, J.H. 2010. Ionic mechanisms of action of prion protein fragment PrP(106-126) in rat basal forebrain neurons. Journal of Neuroscience Research. 88(10):2217-27.


Alier, K., Ma, L., Yang, J., Westaway, D. & Jhamandas, J.H. 2011. AB inhibition of ionic conductance in mouse basal forebrain neurons is dependent upon the cellular prion protein PrPC. Journal of Neuroscience. 31(45):16292-7.





Martin, G.R., Bashashati, M., Keenan, C.M., MacNaughton, W.K., Jirik, F.R. & Sharkey, K.A. 2010. The Functional Role of Cellular Prion Protein in the Enteric Nervous System. Gastroenterology. 138(5):S-97.


Martin, G.R., Keenan, C.M., Sharkey, K.A. & Jirik, F.R. 2010. Over-expression of the Endogenous Prion Protein (PrPC) Attenuates Experimentally-Induced Colitis. Gastroenterology. 138(5):S-263.


Pushie, J.M., Pickering, I.J., Martin, G.R., Tsutsui, S., Jirik, F.R. & George, G.N. 2011. Prion protein expression level alters regional copper, iron and zinc content in the mouse brain. Metallomics. 3:206-14.





Drabik, P., Gusarov, S. & Kovalenko, A. 2007. Microtubule Stability Studies by Three-dimensional Molecular Theory of Solvation. Biophysical Journal. 92(2):394-403.


Yamazaki, T., Blinov, N., Wishart, D. & Kovalenko, A. 2008. Hydration effects on the HET-s prion and amyloid-beta fibrillous aggregates, studied with three-dimensional molecular theory of solvation. Biophysical Journal. 95(10):4540-8.


Yamazaki, T., Blinov, N., Wishart, D.S. & Kovalenko, A. 2009. Essential Role of Hydration in Aggregation of Misfolded Prion Proteins: Quantification by Molecular Theory of Solvation. Journal of Toxicology and Environmental Health. 72(17-18):1060-8.


Blinov, N., Dorosh, L., Wishart, D.S. & Kovalenko, A. 2010. Association thermodynamics and conformational stability of beta-sheet amyloid beta (17-42) oligomers: effects of E22Q (Dutch) mutation and charge neutralization. Biophysical. 98(2):282-96.


Kovalenko, A. & Blinov, N. 2011. Multiscale methods for nanochemistry and biophysics in solution. Journal of Molecular Liquids. 164:101-2.


Kovalenko, A., Kobryn, A., Gusarov, S., Lyubimova, O., Liu, X., Blinov, N. & Yoshida, M. 2012. Molecular theory of solvation for supramolecules and soft matter structures: application to ligand binding, ion channels, and oligomeric polyelectrolyte gelator. Soft Matter. 8(5):1508-20.      





Reuter, T., Xu, W., Baker, B.C., Alexander, T.W., Larney, F., Stanford, K. & McAllister, T.A. 2008. A simple method for temporal collection of microbial and tissue samples from static composting systems. Biosystems Engineering. 50:6.17-6.20.


Xu, W.P., Reuter, T., Inglis, G.D., Larney, F.J., Alexander, T.W., Guan, J., Stanford, K., Xu, Y.P. & McAllister, T.A. 2008. Development of a composting system for emergency disposal of cattle carcasses and manure during an infectious disease outbreak.


Puhl, A. A., Selinger, L. B., McAllister, T. A. & Inglis, G. D. 2009. Actinomadura keratinolytica sp. nov., a novel keratin-degrading actinobacterium isolated from bovine compost. International journal of systematic and evolutionary microbiology. 59(Pt 4):828-34.


Reuter, T., Gilroyed, B.H., Alexander, T.W., Mitchell, G., Balachandran, A., Czub, S. & McAllister, T.A. 2009. Prion protein detection via direct immuno-quantitative real-time PCR. Journal of Microbiological Methods. 78(3):307-11.


Reuter, T., Xu, W., Alexander, T.W., Stanford, K., Xu, Y. & McAllister, T.A. 2009. Purification of polymerase chain reaction (PCR)-amplifiable DNA from compost piles containing bovine mortalities. Bioresource Technology. 100(13):3343-9.


Xu, W., Reuter, T., Inglis, G.D., Larney, F.J., Alexander, T.W., Guan, J., Stanford, K., Xu, Y. & McAllister, T.A. 2009. A biosecure composting system for disposal of cattle carcasses and manure following infectious disease outbreak. Journal of Environmental Quality. 38(2):437-50.


Xu, W., Reuter, T., Xu, Y., Alexander, T.W., Gilroyed, B., Jin, L., Stanford, K., Larney, F.J. & McAllister, T.A. 2009. Use of quantitative and conventional PCR to assess biodegradation of bovine and plant DNA during cattle mortality composting. Environmental Science and Technology. 43(16):6248-55.


Reuter, T., Xu, W., Alexander, T.W., Gilroyed, B.H., Inglis, G.D., Larney, F.J., Stanford, K. & McAllister, T.A. 2010. Biocontained carcass composting for control of infectious disease outbreak in livestock. Journal of Visualized Experiments. (39):e1946.


Xu, W., Xu, Y., Reuter, T., Gilroyed, B., Jin, L., Stanford, K., Larney, F.J. & McAllister, T.A. 2010. An improved design for biocontained composting of cattle mortalities. Compost Science and Utilization. 18(1):32-41.


Xu, W., Reuter, T., Xu, Y., Hsu, Y., Stanford, K. & McAllister, T.A. 2011. Field scale evaluation of bovine-specific DNA as an indicator of tissue degradation during cattle mortality composting. Bioresource Technology. 102(7):4800-6.


Xu, S., Inglis, D., Reuter, T., Clark, O.G., Belosevic, M., Leonard, J.J. & McAllister, T.A. 2011. Biodegradation of specified risk material and characterization of actinobacterial communities in laboratory-scale composters. Biodegradation. 22(5):1029-43.


Xu, S., Reuter, T., Gilroyed, B.H., Tymensen, L., Hao, Y., Hao, X., Belosevic, M., Leonard, J.J. & McAllister, T.A. 2012. Microbial communities and greenhouse gas emissions associated with the biodegradation of specified risk material in compost. Waste Management. 33(6):1372-80.


Xu, S., Reuter, T., Gilroyed, B.H., Dudas, S., Graham, C., Neumann, N.F., Balachandran, A., Czub, S., Belosevic, M., Leonard, J.J. & McAllister, T.A. 2013. Biodegradation of specified risk material and fate of scrapie prions in compost. Journal of Environmental Science and Health Part A, Toxic/Hazardous Substances & Environmental Engineering. 48(1):26-36.


Xu, S., Rasmussen, J., Ding, N., Neumann, N., El-Din, M.G., Belosevic, M. & McAllister, T. Inactivation of infectious prions in the environment: A mini-review. 2014. Journal of Environmental Engineering and Science. In press.


Rasmussen, J., Gilroyed, B., Reuter, T., Dudas, S., Neumann, N., Balachandran, Aru, Kav, N., Czub, S. & McAllister, T. 2014. Can plants serve as a vector for prions causing chronic wasting disease? Prion.8(1):135-41.





McKenzie, D. & Aiken, J. 2012. Prion Diseases. Guide to Foodborne Pathogens. Eds. R.G. Labbe and S. Garcia. John Wiley and Sons.


Herbst, A., Banser, P., Valasquez, C.D., May, C., Sim, V., Westaway, D., Aiken, J. & McKenzie, D. 2013. Infectious prions accumulate to high levels in non-proliferative C2C12 myotubes. PLoS Pathogens. 9(11):e1003755.





Merrill, E.H., Pybus, M. & Boyce, M.S. 2010. Chronic wasting disease - the big unknown. Alberta Outdoors. 12(Sept):10-2.


Potapov, A., Merrill, E. & Lewis, M.A. 2012. Wildlife disease elimination and density dependence. Proceedings of the Royal Society. B. 279(1741):3139-45.


Potapov, A., Merrill, E., Pybus, M., Coltman, D. & Lewis, M. 2012. Chronic wasting disease: possible transmission mechanisms in deer. Ecological Modelling. 250:244-57.





Murdoch, B.M., Clawson, M.L., Yue, S., Basu, U., McKay, S., Settles, M., Capoferri, R., Laegreid, W.W., Williams, J.L. & Moore, S.S. 2010. PRNP Halotype Associated with Classical BSE Incidence in European Holstein Cattle. PLoS ONE. 5(9):e12786.


Murdoch, B.M., Clawson, M.L., Laegreid, W.W., Stothard, P., Settles, M., McKay, S., Prasad, A., Wang, Z.Q., Moore, S.S. & Williams, J.L. 2010. A 2cM genome-wide scan of European Holstein cattle affected by classical BSE. BMC Genetics. 11:20.





Hedlin, P., Taschuk, R., Potter, A., Griebel, P. & Napper S. 2012. Detection and Control of Prion Diseases in Food Animals. ISRN Veterinary Sciences. 2012: 254739.


Marciniuk, K., Taschuk, R. & Napper, S. 2013. Evidence for Prion-like Mechanisms in Several Neurodegenerative Diseases: Potential Implications for Immunotherapy. Clinical and Developmental Immunology. 2013:473706.


Madampage, C. A., Maattanen, P., Marciniuk, K., Brownlie, R., Andrievskaia, O., Potter, A., Cashman, N., Lee, J. S. & Napper, S. 2013. Binding of bovine T194A PrPC by PrPSc-specific antibodies: Potential implications for immunotherapy of familial prion diseases. Prion 7(4):1-11


Maattanen, P., Taschuk, R., Ross, L., Marciniuk, K., Potter, A., Cashman, N. & Napper, S. 2013. PrPSc-specific antibodies do not induce prion disease or misfolding of PrPC in highly susceptible Tga20 mice. Prion.7(5): 434- 9.  


Madampage, C., Marciniuk, K., Määttänen, P., Cashman, N., Potter, A., Lee, J. & Napper, S. 2013 Nanopore analysis reveals differences in structural stability of ovine PrPC proteins corresponding to scrapie susceptible (VRQ) and resistance(ARR) genotypes. Prion. 7(6):511-9.


Marciniuk, K., Määttänen, P., Taschuk, R., Airey, T.D., Potter, A., Cashman, N., Griebel, P. & Napper, S. 2014. Development of a Multivalent, PrPSc-Specific Prion Vaccine through Rational Optimization of Three Disease-Specific Epitopes. Vaccine. 32(17): 1988–97.





Ding, N., Neumann, N.F., Price, L.M., Braithwaite, S.L., Balachandran, A., Belosevic, M. & El-Din, M.G. 2012. Inactivation of template-directed misfolding of infectious prion protein by ozone. Appl. Environ Microbiol. 78(3):613-20.


Ding, N., Neumann, N.F., Price, L.M., Braithwaite, S.L., Balachandran, A., Mitchell, G., Belosevic, M. & Gamal El-Din, M. 2013. Kinetics of ozone inactivation of infectious prion protein.  Applied and Environmental Microbiology. 79(8):2721-30.





Gilch, S. & Schätzl, H.M. 2009. Aptamers against prion proteins. Cellular and Molecular Life Sciences. 66(15):2445-55.


Gilch, S., Bach, C., Lutzny, G., Vorberg, I. & Schätzl, H.M. 2009. Inhibition of cholesterol recycling impairs cellular PrPSc propagation. Cellular and Molecular Life Sciences. 66(24):3979–91.


Gilch, S., Krammer, C., Vorberg, I. & Schätzl, H.M. 2009. Therapy in prion diseases: from molecular and cellular biology to therapeutic targets. Infectious Disorders-Drug Targets. 9(1):3-14.


Heiseke, A., Aguib, Y., Baier, M. & Schätzl, H.M. 2009. Lithium induces clearance of prions in prion-infected cells by induction of autophagy. Journal of Neurochemistry. 109(1):25-34.


Heiske, A., Aguib, Y. & Schätzl, H.M. 2010. Autophagy, prion infections and their mutual interactions. Molecular Biology. 12(2):87-97.


Gilch, S., Chitoor, N., Taguchi, Y., Stuart, M., Jewell, J.E. & Schätzl, H.M. 2011. Chronic Wasting Disease. Topics in Current Chemistry. 305:51-77.


Leidel, F., Eiden, M., Geissen, M., Kretzschmar, H.A., Giese, A., Hirschberger, T., Tavan, P., Schätzl, H.M. & Groschup, M.H. 2011. Diphenyl-pyrazole derived compounds increase survival time of mice after prion infection. Antimicrobial Agents and Chemotherapy. 55(10):4774-81.


Nunziante, M., Ackermann, K., Dietrich, K., Wolf, H., Gadtke, L., Gilch, S., Vorberg, I., Groschup, M. & Schätzl, H.M. 2011. Proteasomal dysfunction and ER stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of PrPSc. Journal of Biological Chemistry. 286(39):33942-53.


Schätzl, H. 2012. Cellular mechanisms of propagation and clearance. Prions and Prion Diseases (ed. Wen-Quan Zou and Pierluigi Gambetti). 11:147-8


Franz, M., Eiden, M., Balkema-Buschmann, A., Greenlee, J., Schätzl, H.M., Fast, C., Richt, J., Hildebrandt, J.P. & Groschup, M. 2012. Detection of PrPSc in peripheral tissues of clinically affected cattle after oral challenges with BSE. J. Gen. Virol. 93(Pt 12):2740-8.


Taguchi, Y., Mistica, A.M.A., Kitamoto, T. & Schätzl, H.M. 2013. Critical significance of the region between helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion protein. PLoS Pathogens. 9(6):e1003466.


Taguchi, Y. & Schätzl, H. 2013. Identifying critical sites of PrPC-PrPSc interaction in prion-infected cells by dominant-negative inhibition. Prion. 7(6): 452-6.





Gordon, P.M.K., Schutz, E., Beck, J., Urnovitz, H.B., Graham, C., Clark, R., Dudas, S., Czub, S., Sensen, M., Brenig, B., Groschup, M.H., Church, R.B. & Sensen, C.W. 2008. Disease-specific motifs can be identified in circulating nucleic acids from live elk and cattle infected with transmissible spongiform encephalopathies. Nucleic Acids Research. 37(2):550–6.





Cortez, L.M. & Sim, V.L. 2013. Implications of prion polymorphisms. Prion. 7(4):276-279.


Cortez, L.M., Kumar, J., Renault, L., Young, H.S. & Sim, V.L. 2013. Mouse prion protein polymorphism 108F/189V affects the kinetics of fibril formation and the response to seeding; evidence for a two step nucleation polymerization mechanism. J Biol Chem. 288(7):4772-81.


Campeau, J.L., Wu, G., Bell, J.R., Rasmussen, J. & Sim, V.L. 2013. Early increase and late decrease of Purkinje cell dendritic spine density in prion-infected organotypic mouse cerebellar cultures. PLoS ONE 8(12): e81776.


Walsh, P., Vanderlee, G., Yau, J., Campeau, J., Sim, V.L., Yip, C.M. & Sharpe, S. 2014. The mechanism of membrane disruption by cytotoxic amyloid oligomers formed by PrP(106-126) is dependent on bilayer composition. J Biol Chem. (In press).


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Julien, O., Graether, S.P. & Sykes, B.D. 2009. Monitoring prion protein stability by NMR. Journal of Toxicology and Environmental Health. 72(17-18):1069-74.


Graether, S.P & Sykes, B.D. 2009. Structural characterization of amyloidotic antifreeze protein fibrils and intermediates. Journal of Toxicology and Environmental Health. 72(17-18):1030-3.


Julien, O., Chatterjee, S., Thiessen, A., Graether, S.P. & Sykes, B.D. 2009. Differential stability of the bovine prion protein upon urea unfolding. Protein Science. 18(10):2172-82.


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Westaway, D., Daude, N., Wohlgemuth, S. & Harrison, P. 2011. The PrP-like proteins shadoo and dopel. Topics in Current Chemistry. 305:225-56.


Daude, N. & Westaway, D. 2012. Shadoo/PrP (Sprn0/0/Prnp0/0) double knockout mice: more than zeroes. Prion. 6(5):420-4.         


Mays, C.E., Joy, S., Li, L., Yu, L., Genovesi, S., West, F.G. & Westaway, D. 2012. Prion inhibition with multivalent PrPSc binding compounds. Biomaterials. 33(28):6808-22.       


Daude, N., Wohlegemuth, S., Brown, R., Pitstick, R., Gapeshina, H., Yang, J., Carslon, G.A. & Westaway, D. 2012. Knockout of the prion protein (PrP)-like Sprn gene does not produce embryonic lethality in combination with PrPC-deficiency. Proc. Natl. Acad. Sci. USA. 109(23):9035-40.


Mercer, R., Ma, L., Watts, J., Strome, R., Wohlgemuth, J.Y., Cashman, N., Coulthart, M., Schmitt-Ulms, G., Jhamandas, J. & Westaway, D. 2013. The prion protein modulates A-type K+ currents mediated by Kv4.2 complexes through dipeptidyl aminopeptidase-like protein 6. The Journal of Biological Chemistry. 288(52):37241-55.


Mays, C. Coomaraswamy, J., Watts, J., Yang, J., Ko, K., Strome, B., Mercer, R., Wohlgemuth, S., Schmitt-Ulms, G. & Westaway, D. 2014. Endoproteolytic processing of the mammalian prion glycoprotein family. FEBS Journal. 281(3):862-76.


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Berjanskii, M.V., Neal, S. & Wishart, D.S. 2006. PREDITOR: a web server for predicting protein torsion angle restraints. Nucleic Acids Research. 34(Web Server issue):W63-9.


Montgomerie, S., Sundararaj, S., Gallin, W.J. & Wishart, D.S. 2006. Improving the accuracy of protein secondary structure prediction using structural alignment. BMC Bioinformatics. 7:301.


Neal, S., Berjanskii, M.V., Zhang, H. & Wishart, D.S. 2006. Accurate Prediction of Protein Torsion Angles Using Chemical Shifts and Sequence Homology. Magnetic Resonance in Chemistry. 44(S1): 58-67.


Berjanskii, M.V. & Wishart, D.S. 2007.RCI: A web server for predicting protein flexibility from NMR chemical shifts. Nucleic Acids Research. 35(Web Server issue):W531–7.


Berjanskii, M.V. & Wishart, D.S.  2008. Application of the Random Coil Index to Studying Protein Flexibility. The Journal of Biomolecular NMR. 40(1):31-48.


Mongomerie, S., Cruz, J., Shrivastava, S., Arndt, D., Berjanskii, M. & Wishart, D.S. 2008. Proteus2: A Web Server for Comprehensive Protein Structure Prediction and Structure-Based Annotation. Nucleic Acids Research. 36(2):W202-9.


Shi, Y., Zhou, J., Arndt, D., Wishart, D.S. & Lin, G. 2008. Protein contact order prediction from primary sequences. BMC Bioinformatics. 9(1):255.


Wishart, D.S., Arndt, D., Berjanskij, M., Tang, P., Zhou, J. & Lin, G.  2008. CS23D: a web server for rapid protein structure generation using NMR chemical shifts and sequence data. Nucleic Acid Research. 36:W496-502.


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Xia, J., Bjorndahl, T.C., Tang, P. & Wishart, D.S. 2008. MetaboMiner - semi-automated identification of metabolites from 2D NMR spectra of complex biofluids. BMC Bioinformatics. 9:507.


Zhang, N., Shaw, A.R., Li, N., Chen, R., Mak, A., Hu, X., Young, N., Wishart, D.S. & Li, L. 2008. Liquid chromatography electrospray ionization and matrix-assisted laser desorption ionization tandem mass spectrometry for the analysis of lipid raft proteome of monocytes. Analytica Chimica Acta. 627(1):82-90.


Berjanskii, M., Tang, P., Liang, J., Cruz, J.A., Zhou, J., Zhou, Y., Bassett, E., MacDonell, C., Lu, P., Lin, Guohui, L. & Wishart, D.S. 2009. GeNMR: a web server for rapid NMR-based protein structure determination. Nucleic Acids Research. 37(Web Server issue):W670-7.


Perez-Pineiro, R., Dong, Y.W. & Wishart, D.S. 2009. Solid phase synthesis of acylglycine human metabolites. Bioorganic and Medical Chemistry Letters. 19(23):6706-8.


Blinov, N., Berjanskii, M., Stepanova, M. & Wishart, D.S. 2009. Structural domains and main-chain flexibility in prion proteins. Biochemistry. 48(7):1488-97.


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Xia, J., Psychogios, N., Young, N. & Wishart, D.S. 2009. MetaboAnalyst: a web server for metabolomic data analysis and interpretation. Nucleic Acids Research. 37(Web Server issue): W652–60.


Wang, B., Wang, Y. & Wishart, D.S. 2010. A probabilistic approach for validating protein NMR chemical shift assignments. The Journal of Biomolecular NMR. 47(2):85-99.


Frolkis, A., Knox, C., Lim, E., Jewison, T., Law, V., Hau, D.D., Liu, P., Gautam, B., Ly, S., Guo, A.C., Xia, J., Liang, Y., Shrivastava, S. & Wishart, D.S. 2010. SMPDB: The Small Molecule Pathway Database. Nucleic Acids Research. 38:D480-D487.


Lim, E., Pon, A., Djoumbou, Y., Knox, C., Shrivastava, S., Guo, A.C., Neveu, V. & Wishart, D.S. 2010. T3DB: a comprehensively annotated database of common toxins and their targets. Nucleic Acids Research. 38:D781-6.


Wishart, D.S. 2010. Computational Approaches to Metabolomics. Methods in Molecular Biology. 593:283-313.


Bjorndahl, T.C., Zhou, G.P., Liu, X.H., Perez-Pineiro, R., Semenchenko, V., Saleem, F., Acharya, S., Bujold, A., Sobsey, C.A. & Wishart, D.S. 2011. Detailed Biophysical Characterization of the Acid-induced PrPC to PrPb Conversion Process. Biochemistry. 50(7):1162-73.


Stumpe, M., Blinov, N., Wishart, D.S., Kovalenko, A. & Pande, V. 2011. Calculation of Local Water Densities in Biological Systems – A Comparison of Molecular Dynamics Simulations and the 3D-RISM-KH Molecular Theory of Solvation. The Journal of Physical Chemistry B. 115(2):319-28.


Julien, O., Chatterjee, S., Bjorndahl, T.C., Sweeting, B., Acharya, S., Samenchenko, V., Chakrabartty, A., Pai, E.F., Wishart, D.S., Sykes, B.D. & Cashman, N.R. 2011. Relative and regional stabilities of the hamster, mouse, rabbit, and bovine prion proteins toward urea unfolding assessed by nuclear magnetic resonance and circular dichroism spectroscopies. Biochemistry. 50(35):7536-45.


Mercier, P., Lewis, M.J., Chang, D., Baker, D. & Wishart, D.S. 2011. Towards automatic metabolomic profiling of high-resolution one-dimensional proton NMR spectra. Journal of Biomolecular NMR. 49(3-4):307-23.


Perez-Pineiro, R., Bjorndahl, T.C., Berjanskii, M.V., Haung, A., Lee, R., Gibbs, E., Ladner, C., Dong, Y.W., Abera, A., Cashman, N.R. & Wishart, D.S. 2011. The prion protein binds thiamine. FEBS Journal. 278(21):4002–14.     


Santo, K.P., Berjanskii, M., Stepanova, M. & Wishart, D.S. 2011. Comparative Analysis of essential collective dynamics and NMR-derived flexibility profiled in evolutionarily diverse prion proteins. Prion. 5(3):188-200.


Berjanskii, M., Zhou, J., Liang, Y., Lin, G. & Wishart, D.S. 2012. Resolution-by-proxy: a simple measure for assessing and comparing the overall quality of NMR protein structures. Journal of Biomolecular NMR. 53(3):167-80.


Petrotchenko, E.V., Serpa, J.J., Hardie, D.B., Berjanskii, M., Suriyamongkol, B.P., Wishart, D.S. & Borchers, C.H. 2012. Use of proteinase K non-specific digestion for selective and comprehensive identification of interpeptide crosslinks: application to prion proteins. Molecular & Cellular Proteomics. 11(7):M111.013524.


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Ladner, C.L. & Wishart, D.S. 2012. Resolution enhanced native acidic gel electrophoresis: A method for resolving, sizing quantifying prion protein oligomers. Analytical Biochemistry. 426(1):54-62.


Jetha, N.N., Semenchenko, V., Wishart, D.S., Cashman, N.R. & Marziali, A. 2013. Nanopore analysis of wild-type and mutant prion protein (PrpC): single molecule discrimination and PrPC kinetics. PLoS ONE. 8(2): e54982.


Pagadala, N., Bjorndahl, T., Blinov, N., Kovalenko, A. & Wishart, D. S. 2013. Molecular docking of thiamine reveals similarity in binding properties between the prion protein and other thiamine binding proteins. Journal of Molecular Modeling. 19(12):5225-35.





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