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McDowall, J. S. and Brown, D. R., 2016. Alpha-synuclein:relating metals to structure, function and inhibition. Metallomics, 8 (4), pp. 385-397. Pass, R., Frudd, K., Barnett, J. P., Blindauer, C. A. and Brown, D. R., 2015. Prion infection in cells is abolished by a mutated manganese transporter but shows no relation to zinc. Molecular and Cellular Neuroscience, 68, pp. 186-193. Go?i, F., Mathiason, C. K., Yim, L., Wong, K., Hayes-Klug, J., Nalls, A., Peyser, D., Estevez, V., Denkers, N., Xu, J., Osborn, D. A., Miller, K. V., Warren, R. J., Brown, D. R., Chabalgoity, J. A., Hoover, E. A. and Wisniewski, T., 2015. Mucosal immunization with an attenuated Salmonella vaccine partially protects white-tailed deer from chronic wasting disease. Vaccine, 33 (5), pp. 726-733. Cichon, A.-C. and Brown, D. R., 2014. Nrf-2 regulation of prion protein expression is independent of oxidative stress. Molecular and Cellular Neuroscience, 63, pp. 31-37. Walsh, K. P., Minamide, L. S., Kane, S. J., Shaw, A. E., Brown, D. R., Pulford, B., Zabel, M. D., Lambeth, J. D., Kuhn, T. B. and Bamburg, J. R., 2014. Amyloid-β and proinflammatory cytokines utilize a prion protein-dependent pathway to activate NADPH oxidase and induce cofilin-actin rods in hippocampal neurons. PLoS ONE, 9 (4), e95995. Brown, D. R., 2013. α-Synuclein as a ferrireductase. Biochemical Society Transactions, 41 (6), pp. 1513-1517. Wright, J. A., Mchugh, P. C., Pan, S., Cunningham, A. and Brown, D. R., 2013. Counter-regulation of alpha- and beta-synuclein expression at the transcriptional level. Molecular and Cellular Neuroscience, 57, pp. 33-41. Younan, N.D., Sarell, C.J., Davies, P., Brown, D.R. and Viles, J.H., 2013. The cellular prion protein traps Alzheimer's Aβ in an oligomeric form and disassembles amyloid fibers. FASEB Journal, 27 (5), pp. 1847-1858. McHugh, P. C., Wright, J. A., Williams, R. J. and Brown, D. R., 2012. Prion protein expression alters APP cleavage without interaction with BACE-1. Neurochemistry International, 61 (5), pp. 672-680. Younan, N.D., Nadal, R.C., Davies, P., Brown, D. R. and Viles, J.H., 2012. Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathway. Journal of Biological Chemistry, 287 (34), pp. 28263-28275. Brown, D. R., 2012. Brain Diseases and Metalloproteins. Pan Stanford Publishing. Brown, D. R., 2012. Introduction. In: Brown, D. R., ed. Brain Diseases and Metalloproteins. Singapore: Pan Stanford Publishing, pp. 1-10. Davies, P. and Brown, D. R., 2012. Prion diseases, metals and antioxidants. In: Brown, D. R., ed. Brain Diseases and Metalloproteins. Singapore: Pan Stanford Publishing, pp. 249-293. Meloni, G., Crameri, A., Fritz, G., Davies, P., Brown, D. R., Kroneck, P. M. H. and Va?ák, M., 2012. The catalytic redox activity of prion protein-cuII is controlled by metal exchange with the ZnII-Thiolate clusters of Zn7Metallothionein-3. ChemBiochem, 13 (9), pp. 1261-1265. Hesketh, S., Thompsett, A. R. and Brown, D. R., 2012. Prion protein polymerisation triggered by manganese-generated prion protein seeds. Journal of Neurochemistry, 120 (1), pp. 177-189. Wojtera, M., Sobów, T., K?oszewska, I., Liberski, P. P., Brown, D. R. and Sikorska, B., 2012. Expression of immunohistochemical markers on microglia in Creutzfeldt-Jakob disease and Alzheimer's disease:Morphometric study and review of the literature. Folia Neuropathologica, 50 (1), pp. 74-84. Mot, A. I., Wedd, A. G., Sinclair, L., Brown, D. R., Collins, S. J. and Brazier, M. W., 2011. Metal attenuating therapies in neurodegenerative disease. Expert Review of Neurotherapeutics, 11 (12), pp. 1717-1745. Younan, N. D., Klewpatinond, M., Davies, P., Ruban, A. V., Brown, D. R. and Viles, J. H., 2011. Copper(II)-Induced Secondary Structure Changes and Reduced Folding Stability of the Prion Protein. Journal of Molecular Biology, 410 (3), pp. 369-382. Brown, D. R., 2011. Prions and manganese: A maddening beast. Metallomics, 3 (3), pp. 229-238. Davies, P., Wang, X. Y., Sarell, C. J., Drewett, A., Marken, F., Viles, J. H. and Brown, D. R., 2011. The synucleins are a family of redox-active copper binding proteins. Biochemistry, 50 (1), pp. 37-47.