Prion strain discrimination using luminescent conjugated polymers

Novel Proteinaceous Infectious Particles Cause Scrapie

Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,118

Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

Petkova, A. T., Leapman, R. D., Guo, Z., Yau, W.-M., Mattson, M. P., & Tycko, R. (2005) · Science · doi:10.1126/science.1105850 · Cited by 1,687

Eight prion strains have PrPSc molecules with different conformations

Safar, J., Wille, H., Itri, V., Groth, D., Serban, H., Torchia, M., Cohen, F. E., & Prusiner, S. B. (1998) · Nature Medicine · doi:10.1038/2654 · Cited by 1,245

Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host

Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971

Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie.

Fischer, M., Rülicke, T., Raeber, A., Sailer, A., Moser, M., Oesch, B., Brandner, S., Aguzzi, A., & Weissmann, C. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00467.x · Cited by 877

The protofilament structure of insulin amyloid fibrils

Jiménez, J. L., Nettleton, E. J., Bouchard, M., Robinson, C. V., Dobson, C. M., & Saibil, H. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142459399 · Cited by 834

The sequential development of the brain lesions of scrapie in three strains of mice

Fraser, H., & Dickinson, A. G. (1968) · Journal of Comparative Pathology · doi:10.1016/0021-9975(68)90006-6 · Cited by 476

Identification of a second bovine amyloidotic spongiform encephalopathy: Molecular similarities with sporadic Creutzfeldt-Jakob disease

Casalone, C., Zanusso, G., Acutis, P., Ferrari, S., Capucci, L., Tagliavini, F., Monaco, S., & Caramelli, M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305777101 · Cited by 476

Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent

Bessen, R. A., & Marsh, R. F. (1992) · Journal of Virology · doi:10.1128/jvi.66.4.2096-2101.1992 · Cited by 446

The disease characteristics of different strains of scrapie in Sinc congenic mouse lines: implications for the nature of the agent and host control of pathogenesis

Bruce, M. E., McConnell, I., Fraser, H., & Dickinson, A. G. (1991) · Journal of General Virology · doi:10.1099/0022-1317-72-3-595 · Cited by 388

BSE prions propagate as either variant CJD-like or sporadic CJD-like prion strains in transgenic mice expressing human prion protein

Asante, E. A. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf653 · Cited by 357

Scrapie in mice

Fraser, H., & Dickinson, A. G. (1973) · Journal of Comparative Pathology · doi:10.1016/0021-9975(73)90024-8 · Cited by 347

A 'unified theory' of prion propagation

Weissmann, C. (1991) · Nature · doi:10.1038/352679a0 · Cited by 305

Precise targeting of the pathology of the sialoglycoprotein, PrP, and vacuolar degeneration in mouse scrapie

Bruce, M. E., McBride, P. A., & Farquhar, C. F. (1989) · Neuroscience Letters · doi:10.1016/0304-3940(89)90298-x · Cited by 277

A Change in the Conformation of Prions Accompanies the Emergence of a New Prion Strain

Peretz, D., Williamson, R. A., Legname, G., Matsunaga, Y., Vergara, J., Burton, D. R., DeArmond, S. J., Prusiner, S. B., & Scott, M. R. (2002) · Neuron · doi:10.1016/s0896-6273(02)00726-2 · Cited by 224

Coexistence of multiple PrPSc types in individuals with Creutzfeldt-Jakob disease

Polymenidou, M., Stoeck, K., Glatzel, M., Vey, M., Bellon, A., & Aguzzi, A. (2005) · The Lancet Neurology · doi:10.1016/s1474-4422(05)70225-8 · Cited by 213

Scrapie in Mice: Ultrastructural Observations in the Cerebral Cortex

David-ferreira, J. F., David-ferreira, K. L., Gibbs, C. J., & Morris, J. A. (1968) · Experimental Biology and Medicine · doi:10.3181/00379727-127-32680 · Cited by 185

Conjugated Polyelectrolytes: Conformation-Sensitive Optical Probes for Detection of Amyloid Fibril Formation

Nilsson, K. P. R., Herland, A., Hammarström, P., & Inganäs, O. (2005) · Biochemistry · doi:10.1021/bi047402u · Cited by 176

Distinct glycoform ratios of protease resistant prion protein associated with PRNP point mutations

Hill, A. F., Joiner, S., Beck, J. A., Campbell, T., Dickinson, A., Poulter, M., Wadsworth, J. D. F., & Collinge, J. (2006) · Brain · doi:10.1093/brain/awl013 · Cited by 112

Twisting macromolecular chains: Self-assembly of a chiral supermolecule from nonchiral polythiophene polyanions and random-coil synthetic peptides

Nilsson, K. P. R., Rydberg, J., Baltzer, L., & Inganäs, O. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401853101 · Cited by 109

Polymorphism at Residue 129 Modulates the Conformational Conversion of the D178N Variant of Human Prion Protein 90−231

Apetri, A. C., Vanik, D. L., & Surewicz, W. K. (2005) · Biochemistry · doi:10.1021/bi051455+ · Cited by 80

Understanding the diversity of prions

Aguzzi, A. (2004) · Nature Cell Biology · doi:10.1038/ncb0404-290 · Cited by 52

The Amyloid State of Proteins in Human Diseases

Eisenberg, D., & Jucker, M. (2012) · Cell · doi:10.1016/j.cell.2012.02.022 · Cited by 1,744

Discriminating α-synuclein strains in Parkinson’s disease and multiple system atrophy

Shahnawaz, M., Mukherjee, A., Pritzkow, S., Mendez, N., Rabadia, P., Liu, X., Hu, B., Schmeichel, A., Singer, W., Wu, G., et al. (2020) · Nature · doi:10.1038/s41586-020-1984-7 · Cited by 820

Nanomechanics of functional and pathological amyloid materials

Knowles, T. P. J., & Buehler, M. J. (2011) · Nature Nanotechnology · doi:10.1038/nnano.2011.102 · Cited by 784

Water-soluble fluorescent conjugated polymers and their interactions with biomacromolecules for sensitive biosensors

Feng, X., Liu, L., Wang, S., & Zhu, D. (2010) · Chemical Society Reviews · doi:10.1039/b909065g · Cited by 621

The activities of amyloids from a structural perspective

Riek, R., & Eisenberg, D. S. (2016) · Nature · doi:10.1038/nature20416 · Cited by 508