Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

Wälti, Marielle Aulikki; Ravotti, Francesco; Arai, Hiromi; Glabe, Charles G.; Wall, Joseph S.; Böckmann, Anja; Güntert, Peter; Meier, Beat H.; Riek, Roland

doi:10.1073/pnas.1600749113

Title: Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

Journal Article · Thu Jul 28 00:00:00 EDT 2016 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.1600749113· OSTI ID:1351799

Wälti, Marielle Aulikki ^[1]; Ravotti, Francesco ^[1]; Arai, Hiromi ^[2]; Glabe, Charles G. ^[3]; Wall, Joseph S. ^[4]; Böckmann, Anja ^[5]; Güntert, Peter ^[6]; Meier, Beat H. ^[1]; Riek, Roland ^[1]

Eidgenossische Technische Hochschule Zurich, Zurich (Switzerland)
Univ. of California, Irvine, CA (United States)
Univ. of California, Irvine, CA (United States); King Abdulaziz Univ., Jeddah (Saudi Arabia)
King Abdulaziz Univ., Jeddah (Saudi Arabia)
Univ. de Lyon, Lyon (France)
Eidgenossische Technische Hochschule Zurich, Zurich (Switzerland); Goethe Univ. Frankfurt am Main, Frankfurt am Main (Germany); Tokyo Metropolitan Univ., Tokyo (Japan)

Amyloid-β (Aβ) is present in humans as a 39- to 42-amino acid residue metabolic product of the amyloid precursor protein. Although the two predominant forms, Aβ(1–40) and Aβ(1–42), differ in only two residues, they display different biophysical, biological, and clinical behavior. Aβ(1–42) is the more neurotoxic species, aggregates much faster, and dominates in senile plaque of Alzheimer’s disease (AD) patients. Although small Aβ oligomers are believed to be the neurotoxic species, Aβ amyloid fibrils are, because of their presence in plaques, a pathological hallmark of AD and appear to play an important role in disease progression through cell-to-cell transmissibility. Here, we solved the 3D structure of a disease-relevant Aβ(1–42) fibril polymorph, combining data from solid-state NMR spectroscopy and mass-per-length measurements from EM. The 3D structure is composed of two molecules per fibril layer, with residues 15–42 forming a double-horseshoe–like cross–β-sheet entity with maximally buried hydrophobic side chains. Lastly, residues 1–14 are partially ordered and in a β-strand conformation, but do not display unambiguous distance restraints to the remainder of the core structure.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: SC00112704

OSTI ID:: 1351799

Report Number(s):: BNL-113696-2017-JA

Journal Information:: Proceedings of the National Academy of Sciences of the United States of America, Vol. 113, Issue 34; ISSN 0027-8424

Publisher:: National Academy of Sciences, Washington, DC (United States)Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 604 works

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References (66)

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor Kang, Jie; Lemaire, Hans-Georg; Unterbeck, Axel Nature, Vol. 325, Issue 6106 https://doi.org/10.1038/325733a0	journal	February 1987
The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy Wishart, D. S.; Sykes, B. D.; Richards, F. M. Biochemistry, Vol. 31, Issue 6 https://doi.org/10.1021/bi00121a010	journal	February 1992
X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation. Kirschner, D. A.; Abraham, C.; Selkoe, D. J. Proceedings of the National Academy of Sciences, Vol. 83, Issue 2 https://doi.org/10.1073/pnas.83.2.503	journal	January 1986
Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils ^† Petkova, Aneta T.; Yau, Wai-Ming; Tycko, Robert Biochemistry, Vol. 45, Issue 2 https://doi.org/10.1021/bi051952q	journal	January 2006
Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain: BIOCHEMICAL AND IMMUNOCYTOCHEMICAL ANALYSIS WITH ANTIBODIES SPECIFIC FOR FORMS ENDING AT Aβ40 OR Aβ42(43) Gravina, Stephen A.; Ho, Libin; Eckman, Christopher B. Journal of Biological Chemistry, Vol. 270, Issue 13 https://doi.org/10.1074/jbc.270.13.7013	journal	March 1995
Statistical Basis for the Use of13CαChemical Shifts in Protein Structure Determination Luginbühl, Peter; Szyperski, Thomas; Wüthrich, Kurt Journal of Magnetic Resonance, Series B, Vol. 109, Issue 2 https://doi.org/10.1006/jmrb.1995.0016	journal	November 1995
Peptide dimer structure in an Aβ(1–42) fibril visualized with cryo-EM Schmidt, Matthias; Rohou, Alexis; Lasker, Keren Proceedings of the National Academy of Sciences, Vol. 112, Issue 38 https://doi.org/10.1073/pnas.1503455112	journal	September 2015
Solid-state NMR sequential assignment of an Amyloid-β(1–42) fibril polymorph Ravotti, Francesco; Wälti, Marielle Aulikki; Güntert, Peter Biomolecular NMR Assignments, Vol. 10, Issue 2 https://doi.org/10.1007/s12104-016-9682-y	journal	May 2016
Alzheimer's Disease: A Central Role for Amyloid Selkoe, Dennis J. Journal of Neuropathology & Experimental Neurology, Vol. 53, Issue 5 https://doi.org/10.1097/00005072-199409000-00003	journal	September 1994
Structure and mass analysis by scanning transmission electron microscopy Müller, S. A.; Engel, A. Micron, Vol. 32, Issue 1 https://doi.org/10.1016/S0968-4328(00)00022-6	journal	January 2001
Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen Sunde, Margaret; Serpell, Louise C.; Bartlam, Mark Journal of Molecular Biology, Vol. 273, Issue 3 https://doi.org/10.1006/jmbi.1997.1348	journal	October 1997
The cell biology of prion-like spread of protein aggregates: mechanisms and implication in neurodegeneration Costanzo, Maddalena; Zurzolo, Chiara Biochemical Journal, Vol. 452, Issue 1 https://doi.org/10.1042/BJ20121898	journal	April 2013
Exogenous Induction of Cerebral -Amyloidogenesis Is Governed by Agent and Host Meyer-Luehmann, M. Science, Vol. 313, Issue 5794 https://doi.org/10.1126/science.1131864	journal	September 2006
Structural polymorphism of Alzheimer Aβ and other amyloid fibrils Fändrich, Marcus; Meinhardt, Jessica; Grigorieff, Nikolaus Prion, Vol. 3, Issue 2 https://doi.org/10.4161/pri.3.2.8859	journal	April 2009
Influence of 1H chemical shift assignments of the interface residues on structure determinations of homodimeric proteins Lin, Yi-Jan; Kirchner, Donata K.; Güntert, Peter Journal of Magnetic Resonance, Vol. 222 https://doi.org/10.1016/j.jmr.2012.07.001	journal	September 2012
13C–1H dipolar-driven 13C–13C recoupling without 13C rf irradiation in nuclear magnetic resonance of rotating solids Takegoshi, K.; Nakamura, Shinji; Terao, Takehiko The Journal of Chemical Physics, Vol. 118, Issue 5 https://doi.org/10.1063/1.1534105	journal	February 2003
Structural Constraints from Proton-Mediated Rare-Spin Correlation Spectroscopy in Rotating Solids ^† Lange, Adam; Luca, Sorin; Baldus, Marc Journal of the American Chemical Society, Vol. 124, Issue 33 https://doi.org/10.1021/ja026691b	journal	August 2002
Analysis of the Secondary Structure of β-Amyloid (Aβ42) Fibrils by Systematic Proline Replacement Morimoto, Akira; Irie, Kazuhiro; Murakami, Kazuma Journal of Biological Chemistry, Vol. 279, Issue 50 https://doi.org/10.1074/jbc.M406262200	journal	September 2004
The CCPN data model for NMR spectroscopy: Development of a software pipeline Vranken, Wim F.; Boucher, Wayne; Stevens, Tim J. Proteins: Structure, Function, and Bioinformatics, Vol. 59, Issue 4 https://doi.org/10.1002/prot.20449	journal	April 2005
Conformation dependent monoclonal antibodies distinguish different replicating strains or conformers of prefibrillar Aβ oligomers Kayed, Rakez; Canto, Isabel; Breydo, Leonid Molecular Neurodegeneration, Vol. 5, Issue 1 https://doi.org/10.1186/1750-1326-5-57	journal	January 2010
Proton Assisted Insensitive Nuclei Cross Polarization Lewandowski, Józef R.; De Paëpe, Gaël; Griffin, Robert G. Journal of the American Chemical Society, Vol. 129, Issue 4 https://doi.org/10.1021/ja0650394	journal	January 2007
Combined automated NOE assignment and structure calculation with CYANA Güntert, Peter; Buchner, Lena Journal of Biomolecular NMR, Vol. 62, Issue 4 https://doi.org/10.1007/s10858-015-9924-9	journal	March 2015
Increased Reliability of Nuclear Magnetic Resonance Protein Structures by Consensus Structure Bundles Buchner, Lena; Güntert, Peter Structure, Vol. 23, Issue 2 https://doi.org/10.1016/j.str.2014.11.014	journal	February 2015
Unlike Twins: An NMR Comparison of Two alpha-Synuclein Polymorphs Featuring Different Toxicity Gath, Julia; Bousset, Luc; Habenstein, Birgit ETH Zurich https://doi.org/10.3929/ethz-b-000081831	text	January 2014
Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis Kayed, R. Science, Vol. 300, Issue 5618 https://doi.org/10.1126/science.1079469	journal	April 2003
Contribution of Specific Residues of the beta-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability Daskalov, Asen Y.; Gantner, Matthias; Wälti, Marielle A. ETH Zurich https://doi.org/10.3929/ethz-b-000087245	text	January 2014
Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity Modi, Tushar; Risso, Valeria A.; Martinez-Rodriguez, Sergio Nature Communications, Vol. 12, Issue 1 https://doi.org/10.1038/s41467-021-22089-0	journal	March 2021
The structure of fibrils from ‘misfolded’ proteins Meier, Beat H.; Böckmann, Anja Current Opinion in Structural Biology, Vol. 30 https://doi.org/10.1016/j.sbi.2014.12.001	journal	February 2015
Characterization of different water pools in solid-state NMR protein samples Böckmann, Anja; Gardiennet, Carole; Verel, René Journal of Biomolecular NMR, Vol. 45, Issue 3 https://doi.org/10.1007/s10858-009-9374-3	journal	September 2009
The precursor of Alzheimer??s disease amyloid A4 protein resembles a cell-surface receptor Kang, J.; Lemaire, H-G; Unterbeck, A. Alzheimer Disease & Associated Disorders, Vol. 1, Issue 3 https://doi.org/10.1097/00002093-198701030-00032	journal	January 1987
The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease Jarrett, Joseph T.; Berger, Elizabeth P.; Lansbury, Peter T. Biochemistry, Vol. 32, Issue 18 https://doi.org/10.1021/bi00069a001	journal	May 1993
Structural and functional characterization of two alpha-synuclein strains Bousset, Luc; Pieri, Laura; Ruiz-Arlandis, Gemma Nature Communications, Vol. 4, Issue 1 https://doi.org/10.1038/ncomms3575	journal	October 2013
Mass analysis of biological macromolecular complexes by STEM Thomas, D. Biology of the Cell, Vol. 80, Issue 2-3 https://doi.org/10.1016/0248-4900(94)90041-8	journal	January 1994
3D TEDOR NMR Experiments for the Simultaneous Measurement of Multiple Carbon−Nitrogen Distances in Uniformly ¹³ C, ¹⁵ N-Labeled Solids Jaroniec, Christopher P.; Filip, Claudiu; Griffin, Robert G. Journal of the American Chemical Society, Vol. 124, Issue 36 https://doi.org/10.1021/ja026385y	journal	September 2002
Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers Kayed, Rakez; Head, Elizabeth; Sarsoza, Floyd Molecular Neurodegeneration, Vol. 2, Issue 1 https://doi.org/10.1186/1750-1326-2-18	journal	January 2007
Acquisition of chemiluminescent signals from immunoblots with a digital single-lens reflex camera Khoury, Mitri K.; Parker, Ian; Aswad, Dana W. Analytical Biochemistry, Vol. 397, Issue 1 https://doi.org/10.1016/j.ab.2009.09.041	journal	February 2010
Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation Schütz, Anne K.; Vagt, Toni; Huber, Matthias Angewandte Chemie International Edition, Vol. 54, Issue 1 https://doi.org/10.1002/anie.201408598	journal	November 2014
Contribution of Specific Residues of the β-Solenoid Fold to HET-s Prion Function, Amyloid Structure and Stability Daskalov, Asen; Gantner, Matthias; Wälti, Marielle Aulikki PLoS Pathogens, Vol. 10, Issue 6 https://doi.org/10.1371/journal.ppat.1004158	journal	June 2014
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils Ahmed, Mahiuddin; Davis, Judianne; Aucoin, Darryl Nature Structural & Molecular Biology, Vol. 17, Issue 5 https://doi.org/10.1038/nsmb.1799	journal	April 2010
A structural model for Alzheimer's -amyloid fibrils based on experimental constraints from solid state NMR Petkova, A. T.; Ishii, Y.; Balbach, J. J. Proceedings of the National Academy of Sciences, Vol. 99, Issue 26 https://doi.org/10.1073/pnas.262663499	journal	December 2002
The amyloid hypothesis of Alzheimer's disease at 25 years Selkoe, Dennis J.; Hardy, John EMBO Molecular Medicine, Vol. 8, Issue 6 https://doi.org/10.15252/emmm.201606210	journal	March 2016
Infectious Alzheimer's disease? Riek, Roland Nature, Vol. 444, Issue 7118 https://doi.org/10.1038/444429a	journal	November 2006
High Resolution Structural Characterization of Aβ ₄₂ Amyloid Fibrils by Magic Angle Spinning NMR Colvin, Michael T.; Silvers, Robert; Frohm, Birgitta Journal of the American Chemical Society, Vol. 137, Issue 23 https://doi.org/10.1021/jacs.5b03997	journal	June 2015
The C-Terminus of the β Protein is Critical in Amyloidogenesisa Jarrett, Joseph T.; Berger, Elizabeth P.; Lansbury, Peter T. Annals of the New York Academy of Sciences, Vol. 695, Issue 1 https://doi.org/10.1111/j.1749-6632.1993.tb23043.x	journal	September 1993
Proton assisted recoupling and protein structure determination De Paëpe, Gaël; Lewandowski, Józef R.; Loquet, Antoine The Journal of Chemical Physics, Vol. 129, Issue 24 https://doi.org/10.1063/1.3036928	journal	December 2008
Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43) Iwatsubo, Takeshi; Odaka, Asano; Suzuki, Nobuhiro Neuron, Vol. 13, Issue 1 https://doi.org/10.1016/0896-6273(94)90458-8	journal	July 1994
A New Structural Model of Aβ ₄₀ Fibrils Bertini, Ivano; Gonnelli, Leonardo; Luchinat, Claudio Journal of the American Chemical Society, Vol. 133, Issue 40 https://doi.org/10.1021/ja2035859	journal	October 2011
Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease Xiao, Yiling; Ma, Buyong; McElheny, Dan Nature Structural & Molecular Biology, Vol. 22, Issue 6 https://doi.org/10.1038/nsmb.2991	journal	May 2015
Atomic-Resolution Three-Dimensional Structure of HET-s(218−289) Amyloid Fibrils by Solid-State NMR Spectroscopy Van Melckebeke, Hélène; Wasmer, Christian; Lange, Adam Journal of the American Chemical Society, Vol. 132, Issue 39 https://doi.org/10.1021/ja104213j	journal	October 2010
The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data Wishart, DavidS.; Sykes, BrianD. Journal of Biomolecular NMR, Vol. 4, Issue 2 https://doi.org/10.1007/BF00175245	journal	March 1994
Torsion angle dynamics for NMR structure calculation with the new program Dyana Güntert, P.; Mumenthaler, C.; Wüthrich, K. Journal of Molecular Biology, Vol. 273, Issue 1 https://doi.org/10.1006/jmbi.1997.1284	journal	October 1997
13C–1H dipolar-assisted rotational resonance in magic-angle spinning NMR Takegoshi, K.; Nakamura, Shinji; Terao, Takehiko Chemical Physics Letters, Vol. 344, Issue 5-6 https://doi.org/10.1016/S0009-2614(01)00791-6	journal	August 2001
3D structure of Alzheimer's amyloid- (1-42) fibrils Luhrs, T.; Ritter, C.; Adrian, M. Proceedings of the National Academy of Sciences, Vol. 102, Issue 48 https://doi.org/10.1073/pnas.0506723102	journal	November 2005
beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease. Roher, A. E.; Lowenson, J. D.; Clarke, S. Proceedings of the National Academy of Sciences, Vol. 90, Issue 22 https://doi.org/10.1073/pnas.90.22.10836	journal	November 1993
Amyloid plaque core protein in Alzheimer disease and Down syndrome. Masters, C. L.; Simms, G.; Weinman, N. A. Proceedings of the National Academy of Sciences, Vol. 82, Issue 12 https://doi.org/10.1073/pnas.82.12.4245	journal	June 1985
Oligomerization and Toxicity of β-Amyloid-42 Implicated in Alzheimer's Disease El-Agnaf, Omar M. A.; Mahil, Devinder S.; Patel, Bhroma P. Biochemical and Biophysical Research Communications, Vol. 273, Issue 3 https://doi.org/10.1006/bbrc.2000.3051	journal	July 2000
Supramolecular Structural Constraints on Alzheimer's β-Amyloid Fibrils from Electron Microscopy and Solid-State Nuclear Magnetic Resonance ^† Antzutkin, Oleg N.; Leapman, Richard D.; Balbach, John J. Biochemistry, Vol. 41, Issue 51 https://doi.org/10.1021/bi0204185	journal	December 2002
Annular Protofibrils Are a Structurally and Functionally Distinct Type of Amyloid Oligomer Kayed, Rakez; Pensalfini, Anna; Margol, Larry Journal of Biological Chemistry, Vol. 284, Issue 7 https://doi.org/10.1074/jbc.M808591200	journal	December 2008
Molecular basis for amyloid- polymorphism Colletier, J. -P.; Laganowsky, A.; Landau, M. Proceedings of the National Academy of Sciences, Vol. 108, Issue 41 https://doi.org/10.1073/pnas.1112600108	journal	September 2011
Solution NMR Studies of Recombinant Aβ(1-42): From the Presence of a Micellar Entity to Residual β-Sheet Structure in the Soluble Species Wälti, Marielle Aulikki; Orts, Julien; Vögeli, Beat ChemBioChem, Vol. 16, Issue 4 https://doi.org/10.1002/cbic.201402595	journal	February 2015
TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts Shen, Yang; Delaglio, Frank; Cornilescu, Gabriel Journal of Biomolecular NMR, Vol. 44, Issue 4 https://doi.org/10.1007/s10858-009-9333-z	journal	June 2009
Unlike Twins: An NMR Comparison of Two α-Synuclein Polymorphs Featuring Different Toxicity Gath, Julia; Bousset, Luc; Habenstein, Birgit PLoS ONE, Vol. 9, Issue 3 https://doi.org/10.1371/journal.pone.0090659	journal	March 2014
Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein Glenner, George G.; Wong, Caine W. Biochemical and Biophysical Research Communications, Vol. 122, Issue 3 https://doi.org/10.1016/0006-291X(84)91209-9	journal	August 1984
Amyloid Fibrils of the HET-s(218-289) Prion Form a Solenoid with a Triangular Hydrophobic Core Wasmer, C.; Lange, A.; Van Melckebeke, H. Science, Vol. 319, Issue 5869 https://doi.org/10.1126/science.1151839	journal	March 2008
Structure of the cross-β spine of amyloid-like fibrils Nelson, Rebecca; Sawaya, Michael R.; Balbirnie, Melinda Nature, Vol. 435, Issue 7043 https://doi.org/10.1038/nature03680	journal	June 2005
Structural and functional characterization of two alpha-synuclein strains Luc, Bousset,; Laura, Pieri,; Gemma, Ruiz-Arlandis, ETH Zurich https://doi.org/10.3929/ethz-b-000074657	text	January 2013

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A structural model of the hierarchical assembly of an amyloid nanosheet by an infrared probe technique Jia, Baohuan; Sun, Ying; Yang, Lujuan Physical Chemistry Chemical Physics, Vol. 20, Issue 43 https://doi.org/10.1039/c8cp03003k	journal	January 2018
Low Energy Optical Excitations as an Indicator of Structural Changes Initiated at the Termini of Amyloid Proteins Jong, KwangHyok; Azar, Yavar T.; Grisanti, Luca https://doi.org/10.26434/chemrxiv.7215065	posted_content	October 2018
Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state Chen, Gefei; Abelein, Axel; Nilsson, Harriet E. Nature Communications, Vol. 8, Issue 1 https://doi.org/10.1038/s41467-017-02056-4	journal	December 2017
HIV and Alzheimer’s disease: complex interactions of HIV-Tat with amyloid β peptide and Tau protein Hategan, Alina; Masliah, Eliezer; Nath, Avindra Journal of NeuroVirology, Vol. 25, Issue 5 https://doi.org/10.1007/s13365-019-00736-z	journal	April 2019
Structural dissection of amyloid aggregates of TDP‐43 and its C‐terminal fragments TDP‐35 and TDP‐16 Shenoy, Jayakrishna; El Mammeri, Nadia; Dutour, Antoine The FEBS Journal, Vol. 287, Issue 12 https://doi.org/10.1111/febs.15159	journal	December 2019
Formation of Neutral Peptide Aggregates as Studied by Mass‐Selective IR Action Spectroscopy Bakels, Sjors; Porskamp, Sebastiaan B. A.; Rijs, Anouk M. Angewandte Chemie, Vol. 131, Issue 31 https://doi.org/10.1002/ange.201902644	journal	June 2019
The Role of Structural Polymorphism in Driving the Mechanical Performance of the Alzheimer's Beta Amyloid Fibrils Grasso, Gianvito; Rebella, Martina; Morbiducci, Umberto Frontiers in Bioengineering and Biotechnology, Vol. 7 https://doi.org/10.3389/fbioe.2019.00083	journal	April 2019
Significantly different contact patterns between Aβ40 and Aβ42 monomers involving the N‐terminal region Liu, Ziye; Jiang, Fan; Wu, Yun‐Dong Chemical Biology & Drug Design, Vol. 94, Issue 3 https://doi.org/10.1111/cbdd.13431	journal	August 2019
Biophysical Aspects of Alzheimer’s Disease: Implications for Pharmaceutical Sciences: Theme: Drug Discovery, Development and Delivery in Alzheimer’s Disease Guest Editor: Davide Brambilla Arosio, Paolo Pharmaceutical Research, Vol. 34, Issue 12 https://doi.org/10.1007/s11095-017-2266-4	journal	September 2017
Mechanisms and rates of nucleation of amyloid fibrils Lee, Cheng-Tai; Terentjev, Eugene M. The Journal of Chemical Physics, Vol. 147, Issue 10 https://doi.org/10.1063/1.4995255	journal	September 2017
No effects without causes: the Iron Dysregulation and Dormant Microbes hypothesis for chronic, inflammatory diseases: Iron Dysregulation and Dormant Microbes Kell, Douglas B.; Pretorius, Etheresia Biological Reviews, Vol. 93, Issue 3 https://doi.org/10.1111/brv.12407	journal	March 2018
Assessment of a Large Enzyme–Drug Complex by Proton‐Detected Solid‐State NMR Spectroscopy without Deuteration Vasa, Suresh K.; Singh, Himanshu; Grohe, Kristof Angewandte Chemie International Edition, Vol. 58, Issue 17 https://doi.org/10.1002/anie.201811714	journal	February 2019
Structure-based inhibitors of amyloid beta core suggest a common interface with tau Griner, Sarah L.; Seidler, Paul; Bowler, Jeannette eLife, Vol. 8 https://doi.org/10.7554/elife.46924	journal	October 2019
A near atomic-scale view at the composition of amyloid-beta fibrils by atom probe tomography Rusitzka, Kristiane A. K.; Stephenson, Leigh T.; Szczepaniak, Agnieszka Scientific Reports, Vol. 8, Issue 1 https://doi.org/10.1038/s41598-018-36110-y	journal	December 2018
Charakterisierung eines großen Enzym‐Wirkstoff‐Komplexes mittels protonendetektierter Festkörper‐NMR ohne Deuterierung Vasa, Suresh K.; Singh, Himanshu; Grohe, Kristof Angewandte Chemie, Vol. 131, Issue 17 https://doi.org/10.1002/ange.201811714	journal	February 2019
Nano-assembly of amyloid β peptide: role of the hairpin fold Maity, Sibaprasad; Hashemi, Mohtadin; Lyubchenko, Yuri L. Scientific Reports, Vol. 7, Issue 1 https://doi.org/10.1038/s41598-017-02454-0	journal	May 2017
Electrostatic Complementarity Drives Amyloid/Nucleic Acid Co‐Assembly Rha, Allisandra K.; Das, Dibyendu; Taran, Olga Angewandte Chemie, Vol. 132, Issue 1 https://doi.org/10.1002/ange.201907661	journal	November 2019
Formation of Neutral Peptide Aggregates as Studied by Mass‐Selective IR Action Spectroscopy Bakels, Sjors; Porskamp, Sebastiaan B. A.; Rijs, Anouk M. Angewandte Chemie International Edition, Vol. 58, Issue 31 https://doi.org/10.1002/anie.201902644	journal	June 2019
Resveratrol Protects Optic Nerve Head Astrocytes from Oxidative Stress-Induced Cell Death by Preventing Caspase-3 Activation, Tau Dephosphorylation at Ser422 and Formation of Misfolded Protein Aggregates Means, John C.; Lopez, Adam A.; Koulen, Peter Cellular and Molecular Neurobiology, Vol. 40, Issue 6 https://doi.org/10.1007/s10571-019-00781-6	journal	January 2020
Autocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluid. Frankel, Rebecca; Törnquist, Mattias; Meisl, Georg Apollo - University of Cambridge Repository https://doi.org/10.17863/cam.46678	text	January 2019
Elucidating the Aβ42 Anti-Aggregation Mechanism of Action of Tramiprosate in Alzheimer’s Disease: Integrating Molecular Analytical Methods, Pharmacokinetic and Clinical Data Kocis, Petr; Tolar, Martin; Yu, Jeremy CNS Drugs, Vol. 31, Issue 6 https://doi.org/10.1007/s40263-017-0434-z	journal	April 2017
Effects of Single Amino Acid Substitutions on Aggregation and Cytotoxicity Properties of Amyloid β Peptide Estrada-Rodríguez, Ana Esther; Valdez-Pérez, Donato; Ruiz-García, Jaime International Journal of Peptide Research and Therapeutics, Vol. 25, Issue 2 https://doi.org/10.1007/s10989-018-9693-x	journal	March 2018
Inhibition of the Self-Assembly of Aβ and of Tau by Polyphenols: Mechanistic Studies Zheng, Qiuchen; Kebede, Micheal T.; Kemeh, Merc M. Molecules, Vol. 24, Issue 12 https://doi.org/10.3390/molecules24122316	journal	June 2019
Distal amyloid β-protein fragments template amyloid assembly: Distal Amyloid Β-Protein Fragments Template Amyloid Assembly Do, Thanh D.; Sangwan, Smriti; de Almeida, Natália E. C. Protein Science, Vol. 27, Issue 7 https://doi.org/10.1002/pro.3375	journal	February 2018
Direct amide 15N to 13C transfers for solid-state assignment experiments in deuterated proteins Lends, Alons; Ravotti, Francesco; Zandomeneghi, Giorgia Journal of Biomolecular NMR, Vol. 72, Issue 1-2 https://doi.org/10.1007/s10858-018-0207-0	journal	September 2018
Fibril structure of amyloid-β(1–42) by cryo–electron microscopy Gremer, Lothar; Schölzel, Daniel; Schenk, Carla Science, Vol. 358, Issue 6359 https://doi.org/10.1126/science.aao2825	journal	September 2017
Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors Chakraborty, Srirupa; Das, Payel Scientific Reports, Vol. 7, Issue 1 https://doi.org/10.1038/s41598-017-10212-5	journal	August 2017
Accuracy and precision of protein structures determined by magic angle spinning NMR spectroscopy: for some ‘with a little help from a friend’ Russell, Ryan W.; Fritz, Matthew P.; Kraus, Jodi Journal of Biomolecular NMR, Vol. 73, Issue 6-7 https://doi.org/10.1007/s10858-019-00233-9	journal	March 2019
Structure of amyloid-β (20-34) with Alzheimer’s-associated isomerization at Asp23 reveals a distinct protofilament interface Warmack, Rebeccah A.; Boyer, David R.; Zee, Chih-Te Nature Communications, Vol. 10, Issue 1 https://doi.org/10.1038/s41467-019-11183-z	journal	July 2019
Mammalian amyloidogenic proteins promote prion nucleation in yeast Chandramowlishwaran, Pavithra; Sun, Meng; Casey, Kristin L. Journal of Biological Chemistry, Vol. 293, Issue 9 https://doi.org/10.1074/jbc.m117.809004	journal	March 2018
A new era for understanding amyloid structures and disease Iadanza, Matthew G.; Jackson, Matthew P.; Hewitt, Eric W. Nature Reviews Molecular Cell Biology, Vol. 19, Issue 12 https://doi.org/10.1038/s41580-018-0060-8	journal	September 2018
Amyloid assembly and disassembly Chuang, Edward; Hori, Acacia M.; Hesketh, Christina D. Journal of Cell Science, Vol. 131, Issue 8 https://doi.org/10.1242/jcs.189928	journal	April 2018
Aggregation kinetics of the Aβ1–40 peptide monitored by NMR Bellomo, Giovanni; Bologna, Sara; Gonnelli, Leonardo Chemical Communications, Vol. 54, Issue 55 https://doi.org/10.1039/c8cc01710g	journal	January 2018
Site-specific structural order in Alzheimer's Aβ42 fibrils Wang, Hongsu; Lee, Yoon Kyung; Xue, Christine Royal Society Open Science, Vol. 5, Issue 7 https://doi.org/10.1098/rsos.180166	journal	July 2018
Revisiting the earliest signatures of amyloidogenesis: Roadmaps emerging from computational modeling and experiment Bhattacharya, Shayon; Xu, Liang; Thompson, Damien Wiley Interdisciplinary Reviews: Computational Molecular Science, Vol. 8, Issue 4 https://doi.org/10.1002/wcms.1359	journal	February 2018
Imaging Aβ(1–42) fibril elongation reveals strongly polarised growth and growth incompetent states Young, Laurence J.; Kaminski Schierle, Gabriele S.; Kaminski, Clemens F. Phys. Chem. Chem. Phys., Vol. 19, Issue 41 https://doi.org/10.1039/c7cp03412a	journal	January 2017
Vibrational Approach to the Dynamics and Structure of Protein Amyloids Li, Haoqian; Lantz, Richard; Du, Deguo Molecules, Vol. 24, Issue 1 https://doi.org/10.3390/molecules24010186	journal	January 2019
Spontaneous self-assembly of amyloid β (1–40) into dimers Hashemi, Mohtadin; Zhang, Yuliang; Lv, Zhengjian Nanoscale Advances, Vol. 1, Issue 10 https://doi.org/10.1039/c9na00380k	journal	January 2019
Mechanical and thermodynamic properties of Aβ ₄₂ , Aβ ₄₀ , and α-synuclein fibrils: a coarse-grained method to complement experimental studies Poma, Adolfo B.; Guzman, Horacio V.; Li, Mai Suan Beilstein Journal of Nanotechnology, Vol. 10 https://doi.org/10.3762/bjnano.10.51	journal	January 2019
Dihydrochalcone molecules destabilize Alzheimer's amyloid-β protofibrils through binding to the protofibril cavity Jin, Yibo; Sun, Yunxiang; Lei, Jiangtao Physical Chemistry Chemical Physics, Vol. 20, Issue 25 https://doi.org/10.1039/c8cp01631c	journal	January 2018
A method of predicting the in vitro fibril formation propensity of Aβ40 mutants based on their inclusion body levels in E. coli Sanagavarapu, Kalyani; Nüske, Elisabeth; Nasir, Irem Scientific Reports, Vol. 9, Issue 1 https://doi.org/10.1038/s41598-019-39216-z	journal	March 2019
Imaging Aβ(1–42) fibril elongation reveals strongly polarised growth and growth incompetent states Young, Lj; Kaminski, Gabriele; Kaminski, Clemens Apollo - University of Cambridge Repository https://doi.org/10.17863/cam.22363	text	January 2017
Secondary nucleation in amyloid formation Törnquist, Mattias; Michaels, Thomas C. T.; Sanagavarapu, Kalyani Chemical Communications, Vol. 54, Issue 63 https://doi.org/10.1039/c8cc02204f	journal	January 2018
Simulating the effect of formation of amyloid plaques on aggregation of tau protein Kuznetsov, I. A.; Kuznetsov, A. V. Proceedings of the Royal Society A: Mathematical, Physical and Engineering Sciences, Vol. 474, Issue 2220 https://doi.org/10.1098/rspa.2018.0511	journal	December 2018
Total chemical synthesis and biophysical properties of a designed soluble 24 kDa amyloid analogue Boehringer, Régis; Kieffer, Bruno; Torbeev, Vladimir Chemical Science, Vol. 9, Issue 25 https://doi.org/10.1039/c8sc01790e	journal	January 2018
Diverse Misfolded Conformational Strains and Cross-seeding of Misfolded Proteins Implicated in Neurodegenerative Diseases Lim, Kwang Hun Frontiers in Molecular Neuroscience, Vol. 12 https://doi.org/10.3389/fnmol.2019.00158	journal	July 2019
Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents Perov, Sergei; Lidor, Ofir; Salinas, Nir Deutsches Elektronen-Synchrotron, DESY, Hamburg https://doi.org/10.3204/pubdb-2020-00018	text	January 2019
Raman fingerprints of amyloid structures Flynn, Jessica D.; Lee, Jennifer C. Chemical Communications, Vol. 54, Issue 51 https://doi.org/10.1039/c8cc03217c	journal	January 2018
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide Michaels, Thomas C. T.; Šarić, Andela; Curk, Samo bioRxiv https://doi.org/10.1101/2020.01.08.897488	posted_content	January 2020
Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissue Ghosh, Ujjayini; Yau, Wai-Ming; Tycko, Robert Chemical Communications, Vol. 54, Issue 40 https://doi.org/10.1039/c8cc01967c	journal	January 2018
Residue‐Specific Dynamics and Local Environmental Changes in Aβ40 Oligomer and Fibril Formation Liu, Haiyang; Morris, Clifford; Lantz, Richard Angewandte Chemie, Vol. 130, Issue 27 https://doi.org/10.1002/ange.201802490	journal	July 2018
Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1 Paul, Kacy R.; Molliex, Amandine; Cascarina, Sean Molecular and Cellular Biology, Vol. 37, Issue 8 https://doi.org/10.1128/mcb.00652-16	journal	January 2017
Two new polymorphic structures of alpha-synuclein solved by cryo-electron microscopy Guerrero-Ferreira, Ricardo; Taylor, Nicholas M. I.; Arteni, Ana-Andrea https://doi.org/10.1101/654582	posted_content	November 2019
The activities of amyloids from a structural perspective Riek, Roland; Eisenberg, David S. Nature, Vol. 539, Issue 7628 https://doi.org/10.1038/nature20416	journal	November 2016
Modulation of Disordered Proteins with a Focus on Neurodegenerative Diseases and Other Pathologies Martinelli, Anne; Lopes, Fernanda; John, Elisa International Journal of Molecular Sciences, Vol. 20, Issue 6 https://doi.org/10.3390/ijms20061322	journal	March 2019
Cryo-EM structures of tau filaments from Alzheimer’s disease Fitzpatrick, Anthony W. P.; Falcon, Benjamin; He, Shaoda Nature, Vol. 547, Issue 7662 https://doi.org/10.1038/nature23002	journal	July 2017
The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug‐Like Miniprotein Taricska, Nóra; Horváth, Dániel; Menyhárd, Dóra K. Chemistry – A European Journal, Vol. 26, Issue 9 https://doi.org/10.1002/chem.201903826	journal	December 2019
Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue Kollmer, Marius; Close, William; Funk, Leonie Nature Communications, Vol. 10, Issue 1 https://doi.org/10.1038/s41467-019-12683-8	journal	October 2019
Different protonated states at the C-terminal of the amyloid-β peptide modulate the stability of S-shaped protofibril Yin, Xiuhua; Liu, Shengtang; Perez-Aguilar, Jose Manuel The Journal of Chemical Physics, Vol. 150, Issue 18 https://doi.org/10.1063/1.5081948	journal	May 2019
Computational Study of the Aza-Michael Addition of the Flavonoid (+)-Taxifolin in the Inhibition of β-Amyloid Fibril Aggregation Ginex, Tiziana; Trius, Marta; Luque, F. Javier Chemistry - A European Journal, Vol. 24, Issue 22 https://doi.org/10.1002/chem.201706072	journal	March 2018
Distinct oligomerization and fibrillization dynamics of amyloid core sequences of amyloid-beta and islet amyloid polypeptide Sun, Yunxiang; Wang, Bo; Ge, Xinwei Phys. Chem. Chem. Phys., Vol. 19, Issue 41 https://doi.org/10.1039/c7cp05695h	journal	January 2017
Aggregation Mechanism of Alzheimer’s Amyloid β-Peptide Mediated by α-Strand/α-Sheet Structure Balupuri, Anand; Choi, Kwang-Eun; Kang, Nam Sook International Journal of Molecular Sciences, Vol. 21, Issue 3 https://doi.org/10.3390/ijms21031094	journal	February 2020
How the formation of amyloid plaques and neurofibrillary tangles may be related: a mathematical modelling study Kuznetsov, I. A.; Kuznetsov, A. V. Proceedings of the Royal Society A: Mathematical, Physical and Engineering Sciences, Vol. 474, Issue 2210 https://doi.org/10.1098/rspa.2017.0777	journal	February 2018
Detection of side-chain proton resonances of fully protonated biosolids in nano-litre volumes by magic angle spinning solid-state NMR Tolchard, James; Pandey, Manoj Kumar; Berbon, Mélanie Journal of Biomolecular NMR, Vol. 70, Issue 3 https://doi.org/10.1007/s10858-018-0168-3	journal	March 2018
Zinc-binding structure of a catalytic amyloid from solid-state NMR Lee, Myungwoon; Wang, Tuo; Makhlynets, Olga V. Proceedings of the National Academy of Sciences, Vol. 114, Issue 24 https://doi.org/10.1073/pnas.1706179114	journal	May 2017
Quantifying proton NMR coherent linewidth in proteins under fast MAS conditions: a second moment approach Malär, Alexander A.; Smith-Penzel, Susanne; Camenisch, Gian-Marco Physical Chemistry Chemical Physics, Vol. 21, Issue 35 https://doi.org/10.1039/c9cp03414e	journal	January 2019
Dissecting the behaviour of β-amyloid peptide variants during oligomerization and fibrillation: ROLES OF Β-AMYLOID PEPTIDE MOTIFS IN OLIGOMERIZATION AND FIBRILLATION Shi, Jing-Ming; Zhang, Lin; Liu, En-Qi Journal of Peptide Science, Vol. 23, Issue 11 https://doi.org/10.1002/psc.3028	journal	August 2017
Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein Wälti, Marielle A.; Schmidt, Thomas; Murray, Dylan T. Proceedings of the National Academy of Sciences, Vol. 114, Issue 34 https://doi.org/10.1073/pnas.1711645114	journal	August 2017
Low energy optical excitations as an indicator of structural changes initiated at the termini of amyloid proteins Jong, Kwang Hyok; Azar, Yavar T.; Grisanti, Luca Physical Chemistry Chemical Physics, Vol. 21, Issue 43 https://doi.org/10.1039/c9cp04648h	journal	January 2019
Recent Advances by In Silico and In Vitro Studies of Amyloid-β 1-42 Fibril Depicted a S-Shape Conformation Acosta, Daniel Miguel Ángel Villalobos; Vega, Brenda Chimal; Basurto, José Correa International Journal of Molecular Sciences, Vol. 19, Issue 8 https://doi.org/10.3390/ijms19082415	journal	August 2018
The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations Gelenter, Martin D.; Smith, Katelyn J.; Liao, Shu-Yu Nature Structural & Molecular Biology, Vol. 26, Issue 7 https://doi.org/10.1038/s41594-019-0238-6	journal	June 2019
Rational Structure‐Based Design of Fluorescent Probes for Amyloid Folds Orts, Julien; Aulikki Wälti, Marielle; Ghosh, Dhiman ChemBioChem, Vol. 20, Issue 9 https://doi.org/10.1002/cbic.201800664	journal	February 2019
Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly Aubrey, Liam D.; Blakeman, Ben J. F.; Lutter, Liisa Communications Chemistry, Vol. 3, Issue 1 https://doi.org/10.1038/s42004-020-00372-3	journal	September 2020
Monomer-dependent secondary nucleation in amyloid formation Linse, Sara Biophysical Reviews, Vol. 9, Issue 4 https://doi.org/10.1007/s12551-017-0289-z	journal	August 2017
Front Cover: The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug‐Like Miniprotein (Chem. Eur. J. 9/2020) Taricska, Nóra; Horváth, Dániel; Menyhárd, Dóra K. Chemistry – A European Journal, Vol. 26, Issue 9 https://doi.org/10.1002/chem.201905180	journal	January 2020
CONFINE-MAS: a magic-angle spinning NMR probe that confines the sample in case of a rotor explosion Wiegand, Thomas; Hunkeler, Andreas; Däpp, Alexander Journal of Biomolecular NMR, Vol. 72, Issue 3-4 https://doi.org/10.1007/s10858-018-0218-x	journal	December 2018
The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism Iadanza, Matthew G.; Silvers, Robert; Boardman, Joshua Nature Communications, Vol. 9, Issue 1 https://doi.org/10.1038/s41467-018-06761-6	journal	October 2018
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms De, Suman; Wirthensohn, David C.; Flagmeier, Patrick Nature Communications, Vol. 10, Issue 1 https://doi.org/10.1038/s41467-019-09477-3	journal	April 2019
Kinetic fingerprints differentiate anti-Aβ therapies Linse, Sara; Scheidt, Tom; Bernfur, Katja https://doi.org/10.1101/815308	posted_content	February 2020
The fold preference and thermodynamic stability of α-synuclein fibrils is encoded in the non-amyloid-β component region Xu, Liang; Bhattacharya, Shayon; Thompson, Damien Physical Chemistry Chemical Physics, Vol. 20, Issue 6 https://doi.org/10.1039/c7cp08321a	journal	January 2018
The Effect of Retro-inverse D-Amino Acid Aβ-peptides on Aβ-Fibril Formation Xi, Wenhui; Hansmann, Ulrich H. E. https://doi.org/10.1101/457325	posted_content	October 2018
Comparing the Folds of Prions and Other Pathogenic Amyloids Flores-Fernández, José; Rathod, Vineet; Wille, Holger Pathogens, Vol. 7, Issue 2 https://doi.org/10.3390/pathogens7020050	journal	May 2018
Elucidating the Molecular Determinants of Aβ Aggregation with Deep Mutational Scanning Gray, Vanessa E.; Sitko, Katherine; Kameni, Floriane Z. Ngako G3 Genes\|Genomes\|Genetics, Vol. 9, Issue 11 https://doi.org/10.1534/g3.119.400535	journal	November 2019
Covalent Protein Painting Reveals Structural Changes in the Proteome in Alzheimer Disease Bamberger, Casimir; Pankow, Sandra; Martínez-Bartolomé, Salvador bioRxiv https://doi.org/10.1101/2020.01.31.929117	posted_content	February 2020
Mechanical and thermodynamic properties of Aβ₄₂ , Aβ₄₀ and α-synuclein fibrils: A coarse-grained method to complement experimental studies Poma, Adolfo; Vargas Guzman, Horacio Andres; Li, Mai Suan https://doi.org/10.1101/527242	posted_content	January 2019
Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro Chen, Gefei; Andrade-Talavera, Yuniesky; Tambaro, Simone Communications Biology, Vol. 3, Issue 1 https://doi.org/10.1038/s42003-020-0757-z	journal	January 2020
Elucidating the molecular determinants of Aβ aggregation with deep mutational scanning Gray, Vanessa E.; Sitko, Katherine; Kameni, Floriane Z. Ngako bioRxiv https://doi.org/10.1101/662213	posted_content	June 2019
Key Peptides and Proteins in Alzheimer’s Disease Penke, Botond; Bogár, Ferenc; Paragi, Gábor Current Protein & Peptide Science, Vol. 20, Issue 6 https://doi.org/10.2174/1389203720666190103123434	journal	May 2019
Direct amide N-15 to C-13 transfers for solid-state assignment experiments in deuterated proteins Lends, Alons; Ravotti, Francesco; Zandomeneghi, Giorgia ETH Zurich https://doi.org/10.3929/ethz-b-000302186	text	January 2018
Modulation of amyloid assembly by glycosaminoglycans: from mechanism to biological significance Quittot, Noé; Sebastiao, Mathew; Bourgault, Steve Biochemistry and Cell Biology, Vol. 95, Issue 3 https://doi.org/10.1139/bcb-2016-0236	journal	June 2017
Alkali ion influence on structure and stability of fibrillar amyloid-β oligomers Huraskin, Danyil; Horn, Anselm H. C. Journal of Molecular Modeling, Vol. 25, Issue 2 https://doi.org/10.1007/s00894-018-3920-4	journal	January 2019
Femtosecond X-ray coherent diffraction of aligned amyloid fibrils on low background graphene Seuring, Carolin; Ayyer, Kartik; Filippaki, Eleftheria Deutsches Elektronen-Synchrotron, DESY, Hamburg https://doi.org/10.3204/pubdb-2018-01731	text	January 2018
The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug‐Like Miniprotein Taricska, Nóra; Horváth, Dániel; Menyhárd, Dóra K. Chemistry – A European Journal, Vol. 26, Issue 9 https://doi.org/10.1002/chem.201905181	journal	January 2020
Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspired Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents Perov, Sergei; Lidor, Ofir; Salinas, Nir https://doi.org/10.1101/493668	posted_content	January 2019
Inflammatory mechanisms in neurodegeneration Nichols, Michael R.; St‐Pierre, Marie‐Kim; Wendeln, Ann‐Christin Journal of Neurochemistry, Vol. 149, Issue 5 https://doi.org/10.1111/jnc.14674	journal	March 2019
Nature-inspired design and evolution of anti-amyloid antibodies Julian, Mark C.; Rabia, Lilia A.; Desai, Alec A. Journal of Biological Chemistry, Vol. 294, Issue 21 https://doi.org/10.1074/jbc.ra118.004731	journal	May 2019
First-passage Fingerprints of Water Diffusion near Glutamine Surfaces Belousov, Roman; Qaisrani, Muhammad Nawaz; Hassanali, Ali arXiv https://doi.org/10.48550/arxiv.2003.12615	preprint	January 2020

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