Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease

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Amyloid pores from pathogenic mutations

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Nucleated conformational conversion and the replication of conformational information by a prion determinant.

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Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in Cortical Neurons

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Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical Amyloid

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Water-soluble Aβ(N-40, N-42) oligomers in normal and Alzheimer disease brains

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Assembly of Aβ Amyloid Protofibrils: An in Vitro Model for a Possible Early Event in Alzheimer's Disease

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CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control

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Diabetes and Alzheimer’s disease crosstalk

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Interpreting the Aggregation Kinetics of Amyloid Peptides

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Nuclear factor erythroid 2-related factor 2 protects against beta amyloid

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Pharmacological promotion of inclusion formation: A therapeutic approach for Huntington’s and Parkinson’s diseases

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Targeting Amyloid-β Peptide (Aβ) Oligomers by Passive Immunization with a Conformation-selective Monoclonal Antibody Improves Learning and Memory in Aβ Precursor Protein (APP) Transgenic Mice

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Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies

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High‐resolution NMR studies of the zinc‐binding site of the Alzheimer's amyloid β‐peptide

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Amyloid Fibrils of Mammalian Prion Protein Are Highly Toxic to Cultured Cells and Primary Neurons

Novitskaya, V., Bocharova, O. V., Bronstein, I. B., & Baskakov, I. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511174200 · Cited by 251

Prefibrillar Amyloid Aggregates Could Be Generic Toxins in Higher Organisms

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Hsp70 and Its Molecular Role in Nervous System Diseases

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The cellular prion protein mediates neurotoxic signalling of β‐sheet‐rich conformers independent of prion replication

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Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure

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SOD1 (Copper/Zinc Superoxide Dismutase) Deficiency Drives Amyloid β Protein Oligomerization and Memory Loss in Mouse Model of Alzheimer Disease

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PKC signaling deficits: a mechanistic hypothesis for the origins of Alzheimer's disease

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Molecular mechanisms of α-synuclein neurodegeneration

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Rutin improves spatial memory in Alzheimer's disease transgenic mice by reducing Aβ oligomer level and attenuating oxidative stress and neuroinflammation

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Misfolded proteins activate Factor XII in humans, leading to kallikrein formation without initiating coagulation

Maas, C., Govers‐Riemslag, J. W. P., Bouma, B., Schiks, B., Hazenberg, B. P. C., Lokhorst, H. M., Hammarström, P., Cate, H. T., de Groot, P. G., Bouma, B. N., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35424 · Cited by 244

Hydrogen Peroxide Is Generated during the Very Early Stages of Aggregation of the Amyloid Peptides Implicated in Alzheimer Disease and Familial British Dementia

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Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer?s A? peptides

Huang, X., Atwood, C., Moir, R. D., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (2004) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-004-0602-8 · Cited by 241

Curli biogenesis: Order out of disorder

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Short amino acid stretches can mediate amyloid formation in globular proteins: The Src homology 3 (SH3) case

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Toxic species in amyloid disorders: Oligomers or mature fibrils

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In Vitro and In Vivo Neurotoxicity of Prion Protein Oligomers

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Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds

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A Seed for Alzheimer Amyloid in the Brain

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Peptide and Protein Mimetics Inhibiting Amyloid β-Peptide Aggregation

Takahashi, T., & Mihara, H. (2008) · Accounts of Chemical Research · doi:10.1021/ar8000475 · Cited by 244

Protein misfolding and aggregation in Alzheimer’s disease and type 2 diabetes mellitus

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Increased in Vivo Amyloid-β42 Production, Exchange, and Loss in Presenilin Mutation Carriers

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Recent Insights in Islet Amyloid Polypeptide‐Induced Membrane Disruption and Its Role in β‐Cell Death in Type 2 Diabetes Mellitus

Khemtémourian, L., Killian, J. A., Höppener, J. W. M., & Engel, M. F. M. (2008) · Journal of Diabetes Research · doi:10.1155/2008/421287 · Cited by 238

The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

Cascella, R., Chen, S. W., Bigi, A., Camino, J. D., Xu, C. K., Dobson, C. M., Chiti, F., Cremades, N., & Cecchi, C. (2021) · Nature Communications · doi:10.1038/s41467-021-21937-3 · Cited by 239

Heat Shock Protein 70 Inhibits α-Synuclein Fibril Formation via Preferential Binding to Prefibrillar Species

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Brain and behavior changes in 12-month-old Tg2576 and nontransgenic mice exposed to anesthetics

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The Development of Amyloid β Protein Deposits in the Aged Brain

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Intrinsic disorder in proteins associated with neurodegenerative diseases

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IgG-Assisted Age-Dependent Clearance of Alzheimer's Amyloid β Peptide by the Blood–Brain Barrier Neonatal Fc Receptor

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Secretion of curli fibre subunits is mediated by the outer membrane‐localized CsgG protein

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Prion detection by an amyloid seeding assay

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A Role for Synaptic Zinc in Activity-Dependent Aβ Oligomer Formation and Accumulation at Excitatory Synapses

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The Inhalation Anesthetic Isoflurane Induces a Vicious Cycle of Apoptosis and Amyloid β-Protein Accumulation

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Intrabody Gene Therapy Ameliorates Motor, Cognitive, and Neuropathological Symptoms in Multiple Mouse Models of Huntington's Disease

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PKC ε Activation Prevents Synaptic Loss, Aβ Elevation, and Cognitive Deficits in Alzheimer's Disease Transgenic Mice

Hongpaisan, J., Sun, M., & Alkon, D. L. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.5209-10.2011 · Cited by 231

d-serine levels in Alzheimer’s disease: implications for novel biomarker development

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Cystatin C-Cathepsin B Axis Regulates Amyloid Beta Levels and Associated Neuronal Deficits in an Animal Model of Alzheimer's Disease

Sun, B., Zhou, Y., Halabisky, B., Lo, I., Cho, S.-H., Mueller-Steiner, S., Devidze, N., Wang, X., Grubb, A., & Gan, L. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.001 · Cited by 231

An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS

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High-resolution Atomic Force Microscopy of Soluble Aβ42 Oligomers

Mastrangelo, I. A., Ahmed, M., Sato, T., Liu, W., Wang, C., Hough, P. V. C., & Smith, S. O. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.01.042 · Cited by 236

Single Particle Characterization of Iron-induced Pore-forming α-Synuclein Oligomers

Kostka, M., Högen, T., Danzer, K. M., Levin, J., Habeck, M., Wirth, A., Wagner, R., Glabe, C. G., Finger, S., Heinzelmann, U., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709634200 · Cited by 233

Bacterial Inclusion Bodies Contain Amyloid-Like Structure

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Near-infrared fluorescence molecular imaging of amyloid beta species and monitoring therapy in animal models of Alzheimer’s disease

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Identification of a highly neurotoxic α-synuclein species inducing mitochondrial damage and mitophagy in Parkinson’s disease

Grassi, D., Howard, S., Zhou, M., Diaz-Perez, N., Urban, N. T., Guerrero-Given, D., Kamasawa, N., Volpicelli-Daley, L. A., LoGrasso, P., & Lasmézas, C. I. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1713849115 · Cited by 228

Evidence for Proteotoxicity in β Cells in Type 2 Diabetes

Gurlo, T., Ryazantsev, S., Huang, C.-J., Yeh, M. W., Reber, H. A., Hines, O. J., O’Brien, T. D., Glabe, C. G., & Butler, P. C. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090532 · Cited by 234

Direct Observation of Aβ Amyloid Fibril Growth and Inhibition

Ban, T., Hoshino, M., Takahashi, S., Hamada, D., Hasegawa, K., Naiki, H., & Goto, Y. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.09.078 · Cited by 227

Soluble Amyloid Oligomers Increase Bilayer Conductance by Altering Dielectric Structure

Sokolov, Y., Kozak, J. A., Kayed, R., Chanturiya, A., Glabe, C. G., & Hall, J. E. (2006) · The Journal of General Physiology · doi:10.1085/jgp.200609533 · Cited by 232

Detection of elevated levels of soluble -synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies

Paleologou, K. E., Kragh, C. L., Mann, D. M. A., Salem, S. A., Al‐Shami, R., Allsop, D., Hassan, A. H. M., Jensen, P. H., & El‐Agnaf, O. M. A. (2008) · Brain · doi:10.1093/brain/awn349 · Cited by 231

Congo red and thioflavin‐T analogs detect Aβ oligomers

Maezawa, I., Hong, H., Liu, R., Wu, C., Cheng, R. H., Kung, M., Kung, H. F., Lam, K. S., Oddo, S., LaFerla, F. M., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04972.x · Cited by 230

Aggresome Formation and Neurodegenerative Diseases: Therapeutic Implications

Chin, L., Olzmann, J. A., & Li, L. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708783330692 · Cited by 233

An accessory protein required for anchoring and assembly of amyloid fibres in B. subtilis biofilms

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Detection of neuron-derived pathological α-synuclein in blood

Kluge, A., Bunk, J., Schaeffer, E., Drobny, A., Xiang, W., Knacke, H., Bub, S., Lückstädt, W., Arnold, P., Lucius, R., et al. (2022) · Brain · doi:10.1093/brain/awac115 · Cited by 230

Amyloid β peptide oligomers directly activate NMDA receptors

Texidó, L., Martín-Satué, M., Alberdi, E. M., Solsona, C., & Matute, C. (2011) · Cell Calcium · doi:10.1016/j.ceca.2011.02.001 · Cited by 233

Inhibition of Islet Amyloid Polypeptide Fibril Formation: A Potential Role for Heteroaromatic Interactions

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Reversible Conformational Conversion of α-Synuclein into Toxic Assemblies by Glucosylceramide

Zunke, F., Moise, A. C., Belur, N. R., Gelyana, E., Stojkovska, I., Dzaferbegovic, H., Toker, N., Jeon, S., Fredriksen, K., & Mazzulli, J. R. (2017) · Neuron · doi:10.1016/j.neuron.2017.12.012 · Cited by 230

Games Played by Rogue Proteins in Prion Disorders and Alzheimer's Disease

Aguzzi, A., & Haass, C. (2003) · Science · doi:10.1126/science.1087348 · Cited by 223

Conformational Differences between Two Amyloid β Oligomers of Similar Size and Dissimilar Toxicity

Ladiwala, A. R. A., Litt, J., Kane, R. S., Aucoin, D., Smith, S. O., Ranjan, S., Davis, J., Nostrand, W. E. V., & Tessier, P. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.329763 · Cited by 228

JNK Signalling: A Possible Target to Prevent Neurodegeneration

Borsello, T., & Forloni, G. (2007) · Current Pharmaceutical Design · doi:10.2174/138161207780858384 · Cited by 226

The systemic amyloidoses: clearer understanding of the molecular mechanisms offers hope for more effective therapies

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The Interplay of Catalysis and Toxicity by Amyloid Intermediates on Lipid Bilayers: Insights from Type II Diabetes

Hebda, J. A., & Miranker, A. D. (2009) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133622 · Cited by 223

Pathology of early- vs late-onset TTR Met30 familial amyloid polyneuropathy

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Cell-produced α-synuclein oligomers are targeted to, and impair, the 26S proteasome

Emmanouilidou, E., Stefanis, L., & Vekrellis, K. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.07.008 · Cited by 236

Neurotoxic protein oligomers — what you see is not always what you get

Bitan, G., Fradinger, E. A., Spring, S. M., & Teplow, D. B. (2005) · Amyloid · doi:10.1080/13506120500106958 · Cited by 221

Progressive accumulation of amyloid‐ β oligomers in Alzheimer’s disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins

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The aggregation potential of human amylin determines its cytotoxicity towards islet β‐cells

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Reduction of oxidative stress, amyloid deposition, and memory deficit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer's disease

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Extracellular phosphorylation of the amyloid β‐peptide promotes formation of toxic aggregates during the pathogenesis of Alzheimer's disease

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Protein aggregation and degradation mechanisms in neurodegenerative diseases.

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Inhibiting toxic aggregation of amyloidogenic proteins: A therapeutic strategy for protein misfolding diseases

Cheng, B., Gong, H., Xiao, H., Petersen, R. B., Zheng, L., & Huang, K. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.06.029 · Cited by 223

Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Aβ protofibrils

Habicht, G., Haupt, C., Friedrich, R. P., Hortschansky, P., Sachse, C., Meinhardt, J., Wieligmann, K., Gellermann, G. P., Brodhun, M., Götz, J., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703793104 · Cited by 221

Rifampicin Inhibits α-Synuclein Fibrillation and Disaggregates Fibrils

Li, J., Zhu, M., Rajamani, S., Uversky, V. N., & Fink, A. L. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.08.025 · Cited by 221

Identifying polyglutamine protein species in situ that best predict neurodegeneration

Miller, J. M. L., Arrasate, M., Brooks, E., Libeu, C. P., Legleiter, J. A., Hatters, D. M., Curtis, J., Cheung, K., Krishnan, P., Mitra, S. S., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.694 · Cited by 220

Neuroprotective and neurotoxic properties of glial cells in the pathogenesis of Alzheimer's disease

Farfara, D., Lifshitz, V., & Frenkel, D. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00314.x · Cited by 216

Amyloid peptides and proteins in review

Harrison, R. S., Sharpe, P. C., Singh, Y., & Fairlie, D. P. (2007) · Springer eBooks · doi:10.1007/112_2007_0701 · Cited by 222

Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid

King, M. E., Kan, H.-M., Baas, P. W., Erişir, A., Glabe, C. G., & Bloom, G. S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605187 · Cited by 215

Modelling amyloid fibril formation kinetics: mechanisms of nucleation and growth

Gillam, J., & MacPhee, C. E. (2013) · Journal of Physics Condensed Matter · doi:10.1088/0953-8984/25/37/373101 · Cited by 217

Mysterious oligomerization of the amyloidogenic proteins

Uversky, V. N. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07721.x · Cited by 219

Human Islet Amyloid Polypeptide Monomers Form Ordered β-hairpins: A Possible Direct Amyloidogenic Precursor

Dupuis, N., Wu, C. F., Shea, J., & Bowers, M. T. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903814q · Cited by 215

Inhibitory activity of stilbenes on Alzheimer’s β-amyloid fibrils in vitro

Rivière, C., Richard, T., Quentin, L., Krisa, S., Mérillon, J., & Monti, J. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2006.09.069 · Cited by 219

Physicochemical interactions of amyloid β-peptide with lipid bilayers

Matsuzaki, K. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.009 · Cited by 220

Structural Reorganisation and Potential Toxicity of Oligomeric Species Formed during the Assembly of Amyloid Fibrils

Cheon, M., Chang, I., Mohanty, S., Luheshi, L. M., Dobson, C. M., Vendruscolo, M., & Favrin, G. (2007) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0030173 · Cited by 218

The Bacterial Curli System Possesses a Potent and Selective Inhibitor of Amyloid Formation

Evans, M. L., Chorell, E., Taylor, J. D., Ådén, J., Götheson, A., Li, F., Koch, M., Sefer, L., Matthews, S., Wittung-Stafshede, P. E., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.025 · Cited by 210

Peripheral immune system in aging and Alzheimer’s disease

Cao, W., & Zheng, H. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0284-2 · Cited by 214

Nanofluidic Biosensing for β-Amyloid Detection Using Surface Enhanced Raman Spectroscopy

Chou, I.-H., Benford, M. E., Beier, H. T., Coté, G. L., Wang, M., Jing, N., Kameoka, J., & Good, T. A. (2008) · Nano Letters · doi:10.1021/nl0808132 · Cited by 213

Soluble oligomers of amyloid-β peptide induce neuronal apoptosis by activating a cPLA2-dependent sphingomyelinase-ceramide pathway

Malaplate, C., Florent‐Béchard, S., Youssef, I., Koziel, V., Sponne, I., Kriem, B., Leininger‐Muller, B., Olivier, J. L., Oster, T., & Pillot, T. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.02.010 · Cited by 224

Autophagy defends pancreatic β cells from human islet amyloid polypeptide-induced toxicity

Rivera, J. F., Costes, S., Gurlo, T., Glabe, C. G., & Butler, P. C. (2014) · Journal of Clinical Investigation · doi:10.1172/jci71981 · Cited by 220

Distinct Early Folding and Aggregation Properties of Alzheimer Amyloid-β Peptides Aβ40 and Aβ42

Chen, Y., & Glabe, C. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602363200 · Cited by 221

Mechanism of Membrane Interaction and Disruption by α-Synuclein

Reynolds, N. P., Soragni, A., Rabe, M., Verdes, D., Liverani, E., Handschin, S., Riek, R., & Seeger, S. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2029848 · Cited by 215

Selection of DNA Aptamers That Recognize α-Synuclein Oligomers Using a Competitive Screening Method

Tsukakoshi, K., Abe, K., Sode, K., & Ikebukuro, K. (2012) · Analytical Chemistry · doi:10.1021/ac300330g · Cited by 211

Seeking a Mechanism for the Toxicity of Oligomeric α-Synuclein

Hall‐Roberts, H., & Brown, D. R. (2015) · Biomolecules · doi:10.3390/biom5020282 · Cited by 222

Alzheimer disease and Down syndrome: factors in pathogenesis

Lott, I. T., & Head, E. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.08.005 · Cited by 212

Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies

Schmid, A. W., Fauvet, B., Moniatte, M., & Lashuel, H. A. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r113.032730 · Cited by 209

Chemical Fluorescent Probe for Detection of Aβ Oligomers

Teoh, C. L., Su, D., Sahu, S., Yun, S., Drummond, E., Prelli, F. C., Lim, S., Cho, S., Ham, S., Wısnıewskı, T., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b06190 · Cited by 212

Amyloid Oligomer Structures and Toxicity

Glabe, C. G. (2009) · The Open Biology Journal · doi:10.2174/1874196700902010222 · Cited by 18

1874-1967/09 2009 Bentham Open Open Access

Structures, A. O., & Glabe, C. G. (2016)

Distinct types of amyloid‐β oligomers displaying diverse neurotoxicity mechanisms in Alzheimer's disease

Madhu, P., & Mukhopadhyay, S. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30141 · Cited by 53

ChemInform Abstract: Structure of Amyloid Oligomers and Their Mechanisms of Toxicities: Targeting Amyloid Oligomers Using Novel Therapeutic Approaches

Salahuddin, P., Fatima, M. T., Abdelhameed, A. S., Nusrat, S., & Khan, R. H. (2016) · ChemInform · doi:10.1002/chin.201622261 · Cited by 1

Amyloid oligomers

Zako, T. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07567.x · Cited by 2