Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis

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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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TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle

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Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients

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Serum response factor and myocardin mediate arterial hypercontractility and cerebral blood flow dysregulation in Alzheimer's phenotype

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Heart Failure and Protein Quality Control

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Tau Paired Helical Filaments from Alzheimer's Disease Brain and Assembled in Vitro Are Based on β-Structure in the Core Domain

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Lipoprotein-Based Nanoparticles Rescue the Memory Loss of Mice with Alzheimer’s Disease by Accelerating the Clearance of Amyloid-Beta

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Amyloid pathology is associated with progressive monoaminergic neurodegeneration in a transgenic mouse model of Alzheimer’s disease

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Phosphorylated α‐synuclein can be detected in blood plasma and is potentially a useful biomarker for Parkinson's disease

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Donepezil-based multi-functional cholinesterase inhibitors for treatment of Alzheimer's disease

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Age-dependent accumulation of oligomeric SNCA/α-synuclein from impaired degradation in mutant LRRK2 knockin mouse model of Parkinson disease: role for therapeutic activation of chaperone-mediated autophagy (CMA)

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An ALS-Linked Mutant SOD1 Produces a Locomotor Defect Associated with Aggregation and Synaptic Dysfunction When Expressed in Neurons of Caenorhabditis elegans

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Lysozyme Amyloid Oligomers and Fibrils Induce Cellular Death via Different Apoptotic/Necrotic Pathways

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EGb 761 enhances adult hippocampal neurogenesis and phosphorylation of CREB in transgenic mouse model of Alzheimer's disease

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Molecular and cellular aspects of protein misfolding and disease

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Apoptosis in pancreatic β-islet cells in Type 2 diabetes

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The green tea polyphenol (−)‐epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios

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Molecular Mechanisms and Genetics of Oxidative Stress in Alzheimer’s Disease

Cioffi, F., Adam, R. H. I., & Broersen, K. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190863 · Cited by 204

Natural product-based amyloid inhibitors

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Aggregation of Protein Therapeutics Enhances Their Immunogenicity: Causes and Mitigation Strategies

Lundahl, M. L. E., Fogli, S., Colavita, P. E., & Scanlan, E. M. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00067e · Cited by 212

Disease-specific tau filaments assemble via polymorphic intermediates

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Hierarchical Assembly of β2-Microglobulin Amyloid In Vitro Revealed by Atomic Force Microscopy

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How Epigallocatechin Gallate Can Inhibit α-Synuclein Oligomer Toxicity in Vitro

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Microglial activation facilitates Aβ plaque removal following intracranial anti-Aβ antibody administration

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Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers

Luibl, V. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25843 · Cited by 203

Mechanisms of islet amyloidosis toxicity in type 2 diabetes

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Inhibition of tau aggregation in a novel Caenorhabditis elegans model of tauopathy mitigates proteotoxicity

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Neuroprotective natural antibodies to assemblies of amyloidogenic peptides decrease with normal aging and advancing Alzheimer's disease

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Distinct Effects of Zn2+, Cu2+, Fe3+, and Al3+ on Amyloid-β Stability, Oligomerization, and Aggregation

Chen, W.-T., Liao, Y., Yu, H.-M., Cheng, I. H.-J., & Chen, Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.177246 · Cited by 199

How is protein aggregation in amyloidogenic diseases modulated by biological membranes?

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Harnessing Chaperones to Generate Small-Molecule Inhibitors of Amyloid ß Aggregation

Gestwicki, J. E., Crabtree, G. R., & Graef, I. A. (2004) · Science · doi:10.1126/science.1101262 · Cited by 200

p25/Cyclin-Dependent Kinase 5 Induces Production and Intraneuronal Accumulation of Amyloid βIn Vivo

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Detection of Misfolded Aβ Oligomers for Sensitive Biochemical Diagnosis of Alzheimer’s Disease

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Soluble Amyloid β-Oligomers Affect Dielectric Membrane Properties by Bilayer Insertion and Domain Formation: Implications for Cell Toxicity

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Exercise-Induced Cognitive Plasticity, Implications for Mild Cognitive Impairment and Alzheimer’s Disease

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Inhibition of Aggregation of Amyloid Peptides by Beta-Sheet Breaker Peptides and Their Binding Affinity

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Destruction or Potentiation of Different Prions Catalyzed by Similar Hsp104 Remodeling Activities

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Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes

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Genome-Wide Screen for Modifiers of Ataxin-3 Neurodegeneration in Drosophila

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Structural properties of pore-forming oligomers of alpha-synuclein.

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Insulin signaling, glucose metabolism and mitochondria: Major players in Alzheimer's disease and diabetes interrelation

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Targeting the neurotoxic species in Alzheimer's disease: inhibitors of Aβ oligomerization

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Ibuprofen reduces Aβ, hyperphosphorylated tau and memory deficits in Alzheimer mice

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In Vitro Polymerization of a Functional Escherichia coli Amyloid Protein

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CSF Biomarkers for Alzheimer's Disease Diagnosis

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Alzheimer’s Disease, Oligomers, and Inflammation

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Molecular Dynamics Simulation of Amyloid β Dimer Formation

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Tau-Centric targets and drugs in clinical development for the treatment of alzheimer's disease

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Towards non-invasive diagnostic imaging of early-stage Alzheimer's disease

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Human Islet Amyloid Polypeptide Oligomers Disrupt Cell Coupling, Induce Apoptosis, and Impair Insulin Secretion in Isolated Human Islets

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β-Amyloid Is Different in Normal Aging and in Alzheimer Disease

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Orally Administrated Cinnamon Extract Reduces β-Amyloid Oligomerization and Corrects Cognitive Impairment in Alzheimer's Disease Animal Models

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A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides

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The Therapeutic Potential of Rosemary (Rosmarinus officinalis) Diterpenes for Alzheimer’s Disease

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Phosphorylation Does Not Prompt, Nor Prevent, the Formation of -synuclein Toxic Species in a Rat Model of Parkinson's Disease

da Silveira, S. A., Schneider, B. L., Cifuentes-Díaz, C., Sage, D., Abbas‐Terki, T., Iwatsubo, T., Unser, M. A., & Aebischer, P. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn417 · Cited by 196

Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer’s disease immunotherapeutics

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Aromatic Small Molecules Remodel Toxic Soluble Oligomers of Amyloid β through Three Independent Pathways

Ladiwala, A. R. A., Dordick, J. S., & Tessier, P. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.173856 · Cited by 194

Hsp104 antagonizes α-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease

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Methylene Blue Inhibits Amyloid Aβ Oligomerization by Promoting Fibrillization

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Small Heat‐shock Proteins and Clusterin: Intra‐ and Extracellular Molecular Chaperones with a Common Mechanism of Action and Function?

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Age-dependent Accumulation of Soluble Amyloid β (Aβ) Oligomers Reverses the Neuroprotective Effect of Soluble Amyloid Precursor Protein-α (sAPPα) by Modulating Phosphatidylinositol 3-Kinase (PI3K)/Akt-GSK-3β Pathway in Alzheimer Mouse Model

Jiménez, S., Torres, M., Vizuete, M., Sanchez-Varo, R. M., Sánchez‐Mejías, E., Trujillo‐Estrada, L., Carmona‐Cuenca, I., Caballero, C., Ruano, D., Gutiérrez, A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209718 · Cited by 190

Alpha-synuclein-induced mitochondrial dysfunction is mediated via a sirtuin 3-dependent pathway

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Amyloid Accumulation and Pathogensis of Alzheimer’s Disease: Significance of Monomeric, Oligomeric and Fibrillar Aβ

Glabe, C. C. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_8 · Cited by 193

Tau Oligomers Impair Artificial Membrane Integrity and Cellular Viability

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Mutant huntingtin, abnormal mitochondrial dynamics, defective axonal transport of mitochondria, and selective synaptic degeneration in Huntington's disease

Reddy, P. H., & Shirendeb, U. P. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.10.016 · Cited by 188

Amyloid Peptide Channels

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Helix Stabilization Precedes Aqueous and Bilayer-Catalyzed Fiber Formation in Islet Amyloid Polypeptide

Williamson, J. A., Loria, J. P., & Miranker, A. D. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.07.077 · Cited by 186

A longitudinal study on α-synuclein in blood plasma as a biomarker for Parkinson's disease

Foulds, P. G., Diggle, P. J., Mitchell, J. D., Parker, A., Hasegawa, M., Masuda‐Suzukake, M., Mann, D. M. A., & Allsop, D. (2013) · Scientific Reports · doi:10.1038/srep02540 · Cited by 191

Common molecular mechanism of amyloid pore formation by Alzheimer’s β-amyloid peptide and α-synuclein

Scala, C. D., Yahi, N., Boutemeur, S., Flores, A., Rodriguez, L., Chahinian, H., & Fantini, J. (2016) · Scientific Reports · doi:10.1038/srep28781 · Cited by 186

Protein aggregate spreading in neurodegenerative diseases: Problems and perspectives

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Direct characterization of amyloidogenic oligomers by single-molecule fluorescence

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Amyloid fibrils are the molecular trigger of inflammation in Parkinson's disease

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Amyloid assembly and disassembly

Chuang, E., Hori, A. M., Hesketh, C. D., & Shorter, J. (2018) · Journal of Cell Science · doi:10.1242/jcs.189928 · Cited by 188

Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity

Stefani, M. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07889.x · Cited by 185

The Role of the Cell Surface LRP and Soluble LRP in Blood-Brain Barrier Aβ Clearance in Alzheimers Disease

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Toxic Human Islet Amyloid Polypeptide (h-IAPP) Oligomers Are Intracellular, and Vaccination to Induce Anti-Toxic Oligomer Antibodies Does Not Prevent h-IAPP–Induced β-Cell Apoptosis in h-IAPP Transgenic Mice

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Extracellular Chaperones and Proteostasis

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Curcumin Attenuates Amyloid-β Aggregate Toxicity and Modulates Amyloid-β Aggregation Pathway

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Effects of in vivo conditions on amyloid aggregation

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Amyloid-Peptide Vaccinations Reduce β-Amyloid Plaques but Exacerbate Vascular Deposition and Inflammation in the Retina of Alzheimer’s Transgenic Mice

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SUMO on the road to neurodegeneration

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Modeling the Alzheimer Aβ17-42 Fibril Architecture: Tight Intermolecular Sheet-Sheet Association and Intramolecular Hydrated Cavities

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Pathological Interface Between Oligomeric Alpha-Synuclein and Tau in Synucleinopathies

Sengupta, U., Guerrero‐Munoz, M. J., Castillo‐Carranza, D. L., Lasagna‐Reeves, C. A., Gerson, J. E., Paulucci-Holthauzen, A. A., Krishnamurthy, S., Farhed, M., Jackson, G. R., & Kayed, R. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.12.019 · Cited by 187

Recent progress on understanding the mechanisms of amyloid nucleation

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Neprilysin-sensitive Synapse-associated Amyloid-β Peptide Oligomers Impair Neuronal Plasticity and Cognitive Function

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Insulin-Degrading Enzyme in the Fight against Alzheimer's Disease

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Tau protein and tau aggregation inhibitors

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Toxic oligomers and islet beta cell death: guilty by association or convicted by circumstantial evidence?

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Mechanism of Islet Amyloid Polypeptide Fibrillation at Lipid Interfaces Studied by Infrared Reflection Absorption Spectroscopy

Lopes, D. H. J., Meister, A., Gohlke, A., Hauser, A., Blume, A., & Winter, R. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.110635 · Cited by 180

Interaction of the Molecular Chaperone DNAJB6 with Growing Amyloid-beta 42 (Aβ42) Aggregates Leads to Sub-stoichiometric Inhibition of Amyloid Formation

Månsson, C., Arosio, P., Hussein, R. M., Kampinga, H. H., Hashem, R. M., Boelens, W. C., Dobson, C. M., Knowles, T. P. J., Linse, S. S., & Emanuelsson, C. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.595124 · Cited by 186

Common mechanism unites membrane poration by amyloid and antimicrobial peptides

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A role for helical intermediates in amyloid formation by natively unfolded polypeptides?

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Destabilizing Alzheimer’s Aβ42Protofibrils with Morin: Mechanistic Insights from Molecular Dynamics Simulations

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Lipid bilayer disruption by oligomeric α-synuclein depends on bilayer charge and accessibility of the hydrophobic core

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Size-dependent neurotoxicity of β-amyloid oligomers

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Opposing Effects of Glutamine and Asparagine Govern Prion Formation by Intrinsically Disordered Proteins

Halfmann, R., Alberti, S., Krishnan, R., Lyle, N. J., O'Donnell, C. W., King, O. D., Berger, B., Pappu, R. V., & Lindquist, S. L. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.013 · Cited by 179

Small Heat Shock Proteins Potentiate Amyloid Dissolution by Protein Disaggregases from Yeast and Humans

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Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration

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Systematic Mutagenesis of α-Synuclein Reveals Distinct Sequence Requirements for Physiological and Pathological Activities

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Human IAPP–induced pancreatic β cell toxicity and its regulation by autophagy

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Structural features and cytotoxicity of amyloid oligomers: Implications in Alzheimer's disease and other diseases with amyloid deposits

Stefani, M. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.03.002 · Cited by 175

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

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

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

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Amyloid oligomers

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