Adamcik, J and Mezzenga, R (2018) Amyloid polymorphism in the protein folding and aggregation energy landscape. Angewandte Chemie International Edition 57, 8370–8382.
Aggeli, A, Nyrkova, IA, Bell, M, Harding, R, Carrick, L, Mcleish, TCB, Semenov, AN and Boden, N (2001) Hierarchical self-assembly of chiral rod-like molecules as a model for peptide beta-sheet tapes, ribbons, fibrils, and fibers. Proceedings of the National Academy of Sciences of the United States of America 98, 11857–11862.
Auer, S, Ricchiuto, P and Kashchiev, D (2012) Two-step nucleation of amyloid fibrils: omnipresent or not? Journal of Molecular Biology 422, 723–730.
Bauer, H, Aebi, U, Haner, M, Hermann, R, Muller, M, Arvinte, T and Merkle, H (1995) Architecture and polymorphism of fibrillar supramolecular assemblies produced by in-vitro aggregation of human calcitonin. Journal of Structural Biology 115, 1–15.
Berman, HM, Westbrook, J, Feng, Z, Gilliland, G, Bhat, TN, Weissig, H, Shindyalov, IN and Bourne, PE (2000) The protein data bank. Nucleic Acids Research 28, 235–242.
Bodles, AM, Guthrie, DJS, Greer, B and Irvine, GB (2001) Identification of the region of non-Aβ component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity. Journal of Neurochemistry 78, 384–395.
Brookes, A and Stclair, D (1994) Synuclein proteins and Alzheimer's-disease. Trends in Neurosciences 17, 404–405.
Buell, AK, Galvagnion, C, Gaspar, R, Sparr, E, Vendruscolo, M, Knowles, TPJ, Linse, S and Dobson, CM (2014) Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation. Proceedings of the National Academy of Sciences of the United States of America 111, 7671–7676.
Bustamante, C, Tinoco, I and Maestre, M (1983) Circular differential scattering can be an important part of the circular-dichroism of macromolecules. Proceedings of the National Academy of Sciences of the United States of America-Biological Sciences 80, 3568–3572.
Cherny, I and Gazit, E (2008) Amyloids: not only pathological agents but also ordered nanomaterials. Angewandte Chemie-International Edition 47, 4062–4069.
Chiti, F and Dobson, CM (2017) Protein misfolding, amyloid formation, and human disease: a summary of progress over the last decade. Annual Review of Biochemistry 86, 27–68.
Chothia, C (1973) Conformation of twisted β-pleated sheets in proteins. Journal of Molecular Biology 75, 295–302.
Cohen, SIA, Linse, S, Luheshi, LM, Hellstrand, E, White, DA, Rajah, L, Otzen, DE, Vendruscolo, M, Dobson, CM and Knowles, TPJ (2013) Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism. Proceedings of the National Academy of Sciences of the United States of America 110, 9758–9763.
Diaz-Avalos, R, Long, C, Fontano, E, Balbirnie, M, Grothe, R, Eisenberg, D and Caspar, DLD (2003) Cross-beta order and diversity in nanocrystals of an amyloid-forming peptide. Journal of Molecular Biology 330, 1165–1175.
Eanes, E and Glenner, G (1968) X-ray diffraction studies on amyloid filaments. Journal of Histochemistry & Cytochemistry 16, 673.
Eisenberg, DS and Sawaya, MR (2017) Structural studies of amyloid proteins at the molecular level. Annual Review of Biochemistry 86, 69–95.
Fowler, DM, Koulov, AV, Balch, WE and Kelly, JW (2007) Functional amyloid – from bacteria to humans. Trends in Biochemical Sciences 32, 217–224.
Fraser, P, Nguyen, J, Surewicz, W and Kirschner, D (1991) pH-dependent structural transitions of Alzheimer amyloid peptides. Biophysical Journal 60, 1190–1201.
Goldsbury, CS, Cooper, GJS, Goldie, KN, Muller, SA, Saafi, EL, Gruijters, WTM and Misur, MP (1997) Polymorphic fibrillar assembly of human amylin. Journal of Structural Biology 119, 17–27.
Guerrero-Ferreira, R, Taylor, NMI, Mona, D, Ringler, P, Lauer, ME, Riek, R, Britschgi, M and Stahlberg, H (2018) Cryo-EM structure of alpha-synuclein fibrils. Elife 7, e36402.
Hagan, MF, Elrad, OM and Jack, RL (2011) Mechanisms of kinetic trapping in self-assembly and phase transformation. The Journal of Chemical Physics 135, 104115.
Hoyer, W, Antony, T, Cherny, D, Heim, G, Jovin, TM and Subramaniam, V (2002) Dependence of α-synuclein aggregation morphology on solution conditions. Journal of Molecular Biology 322, 383–393.
Ilie, IM, Nayar, D, Den Otter, WK, Van Der Vegt, NFA and Briels, WJ (2018) Intrinsic conformational preferences and interactions in α-synuclein fibrils: insights from molecular dynamics simulations. Journal of Chemical Theory and Computation 14, 3298–3310.
Jimenez, JL, Nettleton, EJ, Bouchard, M, Robinson, CV, Dobson, CM and Saibil, HR (2002) The protofilament structure of insulin amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America 99, 9196–9201.
Lee, J, Culyba, EK, Powers, ET and Kelly, JW (2011) Amyloid-β forms fibrils by nucleated conformational conversion of oligomers. Nature Chemical Biology 7, 602–609.
Li, B, Ge, P, Murray, KA, Sheth, P, Zhang, M, Nair, G, Sawaya, MR, Shin, WS, Boyer, DR, Ye, S, Eisenberg, DS, Zhou, ZH and Jiang, L (2018) Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel. Nature Communications 9, 3609.
Lindner, P and Zemb, T (eds) (2002). Neutrons, X-Rays and Light: Scattering Methods Applied to Soft Condensed Matter. Amsterdam: Elsevier.
Macrae, CF, Bruno, IJ, Chisholm, JA, Edgington, PR, Mccabe, P, Pidcock, E, Rodriguez-Monge, L, Taylor, R, Van De Streek, J and Wood, PA (2008) Mercury CSD 2.0 – new features for the visualization and investigation of crystal structures. Journal of Applied Crystallography 41, 466–470.
Nilsson, MR (2004) Techniques to study amyloid fibril formation in vitro. Methods 34, 151–160.
Pace, CN, Grimsley, GR and Scholtz, JM (2009) Protein ionizable groups: pK values and their contribution to protein stability and solubility. Journal of Biological Chemistry 284, 13285–13289.
Pedersen, JS, Dikov, D, Flink, JL, Hjuler, HA, Christiansen, G and Otzen, DE (2006) The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. Journal of Molecular Biology 355, 501–523.
Periole, X, Huber, T, Bonito-Oliva, A, Aberg, KC, Van Der Wel, PCA, Sakmar, TP and Marrink, SJ (2018) Energetics underlying twist polymorphisms in amyloid fibrils. Journal of Physical Chemistry B 122, 1081–1091.
Reynolds, NP, Adamcik, J, Berryman, JT, Handschin, S, Zanjani, AAH, Li, W, Liu, K, Zhang, A and Mezzenga, R (2017) Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides. Nature Communications 8, 1338.
Rodriguez, JA, Ivanova, MI, Sawaya, MR, Cascio, D, Reyes, FE, Shi, D, Sangwan, S, Guenther, EL, Johnson, LM, Zhang, M, Jiang, L, Arbing, MA, Nannenga, BL, Hattne, J, Whitelegge, J, Brewster, AS, Messerschmidt, M, Boutet, B, Sauter, NK, Gonen, T and Eisenberg, DS (2015) Structure of the toxic core of α-synuclein from invisible crystals. Nature 525, 486–490.
Saiki, M, Honda, S, Kawasaki, K, Zhou, DS, Kaito, A, Konakahara, T and Morii, H (2005) Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains. Journal of Molecular Biology 348, 983–998.
Saric, A, Buell, AK, Meisl, G, Michaels, TCT, Dobson, CM, Linse, S, Knowles, TPJ and Frenkel, D (2016) Physical determinants of the self-replication of protein fibrils. Nature Physics 12, 874–880.
Serio, TR, Cashikar, AG, Kowal, AS, Sawicki, GJ, Moslehi, JJ, Serpell, L, Arnsdorf, MF and Lindquist, SL (2000) Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289, 1317–1321.
Serpell, LC, Berriman, J, Jakes, R, Goedert, M and Crowther, RA (2000) Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation. Proceedings of the National Academy of Sciences of the United States of America 97, 4897–4902.
Solomon, MJ and Spicer, PT (2010) Microstructural regimes of colloidal rod suspensions, gels, and glasses. Soft Matter 6, 1391–1400.
Spillantini, MG, Schmidt, ML, Lee, VMY, Trojanowski, JQ, Jakes, R and Goedert, M (1997) α-Synuclein in Lewy bodies. Nature 388, 839–840.
Spillantini, MG, Crowther, RA, Jakes, R, Hasegawa, M and Goedert, M (1998 a) α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proceedings of the National Academy of Sciences of the United States of America 95, 6469–6473.
Spillantini, MG, Crowther, RA, Jakes, R, Cairns, NJ, Lantos, PL and Goedert, M (1998 b) Filamentous α-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies. Neuroscience Letters 251, 205–208.
Sunde, M, Serpell, LC, Bartlam, M, Fraser, PE, Pepys, MB and Blake, CCF (1997) Common core structure of amyloid fibrils by synchrotron X-ray diffraction. Journal of Molecular Biology 273, 729–739.
Tornquist, M, Michaels, TCT, Sanagavarapu, K, Yang, X, Meisl, G, Cohen, SIA, Knowles, TPJ and Linse, S (2018) Secondary nucleation in amyloid formation. Chemical Communications 54, 8667–8684.
Tuttle, MD, Comellas, G, Nieuwkoop, AJ, Covell, DJ, Berthold, DA, Kloepper, KD, Courtney, JM, Kim, JK, Barclay, AM, Kendall, A, Wan, W, Stubbs, G, Schwieters, CD, Lee, VMY, George, JM and Rienstra, CM (2016) Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. Nature Structural & Molecular Biology 23, 409–415.
Ueda, K, Fukushima, H, Masliah, E, Xia, Y, Iwai, A, Yoshimoto, M, Otero, D, Kondo, J, Ihara, Y and Saitoh, T (1993) Molecular-cloning of cDNA-encoding an unrecognized component of amyloid. Proceedings of the National Academy of Sciences of the United States of America 90, 11282–11286.
Vetri, V, Canale, C, Relini, A, Librizzi, F, Militello, V, Gliozzi, A and Leone, M (2007) Amyloid fibrils formation and amorphous aggregation in concanavalin A. Biophysical Chemistry 125, 184–190.
Wallace, B and Teeters, C (1987) Differential absorption flattening optical effects are significant in the circular-dichroism spectra of large membrane-fragments. Biochemistry 26, 65–70.
Weatherford, D and Salemme, F (1979) Conformations of twisted parallel β-sheets and the origin of chirality in protein structures. Proceedings of the National Academy of Sciences of the United States of America 76, 19–23.
Wei, L, Jiang, P, Xu, W, Li, H, Zhang, H, Yan, L, Chan-Park, MB, Liu, XW, Tang, K, Mu, Y and Pervushin, K (2011) The molecular basis of distinct aggregation pathways of islet amyloid polypeptide. Journal of Biological Chemistry 286, 6291–6300.
Yoshimura, Y, Lin, Y, Yagi, H, Lee, YH, Kitayama, H, Sakurai, K, So, M, Ogi, H, Naiki, H and Goto, Y (2012) Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation. Proceedings of the National Academy of Sciences of the United States of America 109, 14446–14451.