Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis

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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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Generation and Therapeutic Efficacy of Highly Oligomer-Specific β-Amyloid Antibodies

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Green Tea Extracts EGCG and EGC Display Distinct Mechanisms in Disrupting Aβ42 Protofibril

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pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers

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Amyloid-β-Induced Ion Flux in Artificial Lipid Bilayers and Neuronal Cells: Resolving a Controversy

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A critical evaluation of the ubiquitin–proteasome system in Parkinson's disease

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Amyloid-β Protofibrils Differ from Amyloid-β Aggregates Induced in Dilute Hexafluoroisopropanol in Stability and Morphology

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Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent

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Soluble Aβ Promotes Wild-Type Tau Pathology In Vivo

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Two Distinct Amyloid β-Protein (Aβ) Assembly Pathways Leading to Oligomers and Fibrils Identified by Combined Fluorescence Correlation Spectroscopy, Morphology, and Toxicity Analyses

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Cu and Zn interactions with Aβ peptides: consequence of coordination on aggregation and formation of neurotoxic soluble Aβ oligomers

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Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases

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Hsp104: A Weapon to Combat Diverse Neurodegenerative Disorders

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Triterpenoid CDDO‐methylamide improves memory and decreases amyloid plaques in a transgenic mouse model of Alzheimer’s disease

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Unraveling the Early Events of Amyloid-β Protein (Aβ) Aggregation: Techniques for the Determination of Aβ Aggregate Size

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Aβ-globulomers are formed independently of the fibril pathway

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Host PrP Glycosylation: A Major Factor Determining the Outcome of Prion Infection

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Small‐Molecule Inhibitors of Islet Amyloid Polypeptide Fibril Formation

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Proteotoxicity and Cardiac Dysfunction

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Interactions between misfolded protein oligomers and membranes: A central topic in neurodegenerative diseases?

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Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation

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Selective vulnerability to neurodegenerative disease: the curious case of Prion Protein

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Omega-3 fatty acids, lipids, and apoE lipidation in Alzheimer's disease: a rationale for multi-nutrient dementia prevention

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Toxicity of Eosinophil MBP Is Repressed by Intracellular Crystallization and Promoted by Extracellular Aggregation

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Oligomer-specific Aβ toxicity in cell models is mediated by selective uptake

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The Role of Molecular Simulations in the Development of Inhibitors of Amyloid β-Peptide Aggregation for the Treatment of Alzheimer’s Disease

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Semisynthetic, Site-Specific Ubiquitin Modification of α-Synuclein Reveals Differential Effects on Aggregation

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Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils

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Atomic force microscopy to study molecular mechanisms of amyloid fibril formation and toxicity in Alzheimer’s disease

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β-Amyloid Fibrils in Alzheimer Disease Are Not Inert When Bound to Copper Ions but Can Degrade Hydrogen Peroxide and Generate Reactive Oxygen Species

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ADDLs and the signaling web that leads to Alzheimer’s disease

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The Essential Role of Soluble Aβ Oligomers in Alzheimer’s Disease

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No effects without causes: the Iron Dysregulation and Dormant Microbes hypothesis for chronic, inflammatory diseases

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Interactions between amyloid β peptide and lipid membranes

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Proteotoxic stress and the ubiquitin proteasome system

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Modulation of α-Synuclein Aggregation by Dopamine: A Review

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Soluble Aβ oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain

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Synaptic targeting by Aβ oligomers (ADDLS) as a basis for memory loss in early Alzheimer's disease

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Solvation-assisted Pressure Tuning of Insulin Fibrillation: From Novel Aggregation Pathways to Biotechnological Applications

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A Novel Inhibitor of Amyloid β (Aβ) Peptide Aggregation

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Direct Observation of Nucleation and Growth in Amyloid Self-Assembly

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Ligand binding to distinct states diverts aggregation of an amyloid-forming protein

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Tryptophan Fluorescence Reveals Structural Features of α-Synuclein Oligomers

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Transgenic Drosophila models of Alzheimer’s disease and tauopathies

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Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity

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In Vitro and Mechanistic Studies of an Antiamyloidogenic Self-Assembled Cyclic d , l -α-Peptide Architecture

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Protein aggregation as a paradigm of aging

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Amyloid Formation by the Pro-Inflammatory S100A8/A9 Proteins in the Ageing Prostate

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Monoclonal Antibodies Recognize Distinct Conformational Epitopes Formed by Polyglutamine in a Mutant Huntingtin Fragment

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Characterization of Hydrophobic Residue Requirements for α-Synuclein Fibrillization

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Molecules that Target beta‐Amyloid

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Neuronal expression of constitutive heat shock proteins: implications for neurodegenerative diseases

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CCL2 Accelerates Microglia-Mediated Aβ Oligomer Formation and Progression of Neurocognitive Dysfunction

Kiyota, T., Yamamoto, M., Xiong, H., Lambert, M. P., Klein, W. L., Gendelman, H. E., Ransohoff, R. M., & Ikezu, T. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006197 · Cited by 114

The Dynamic Structure of α-Synuclein Multimers

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Analysis of Protein Aggregation in Neurodegenerative Disease

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Discovery and Biological Evaluation of a Novel Highly Potent Selective Butyrylcholinsterase Inhibitor

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TDP-43 and Tau Oligomers in Alzheimer's Disease, Amyotrophic Lateral Sclerosis, and Frontotemporal Dementia

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Essential Role of Proline Isomerization in Stefin B Tetramer Formation

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Reversal of amyloid-induced heart disease in desmin-related cardiomyopathy

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Natural human antibodies to amyloid beta peptide

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Active Solubilization and Refolding of Stable Protein Aggregates By Cooperative Unfolding Action of Individual Hsp70 Chaperones

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Mechanisms of Protein Oligomerization: Inhibitor of Functional Amyloids Templates α-Synuclein Fibrillation

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Are oxidative stress and mitochondrial dysfunction the key players in the neurodegenerative diseases?

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Phosphorylation of the amyloid β-peptide at Ser26 stabilizes oligomeric assembly and increases neurotoxicity

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A Two-Year Study with Fibrillar β-Amyloid (Aβ) Immunization in Aged Canines: Effects on Cognitive Function and Brain Aβ

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Amyloid‐β oligomers impair fear conditioned memory in a calcineurin‐dependent fashion in mice

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Evidence of Aβ‐ and transgene‐dependent defects in ERK‐CREB signaling in Alzheimer’s models

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Molecular Origin of Polyglutamine Aggregation in Neurodegenerative Diseases

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Amyloid-β oligomers stimulate microglia through a tyrosine kinase dependent mechanism

Manocha, G. D., Floden, A. M., & Combs, C. K. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.10.027 · Cited by 110

Amyloidogenesis of Type III-dependent Harpins from Plant Pathogenic Bacteria

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Inter-laboratory comparison of neuropathological assessments of β-amyloid protein: a study of the BrainNet Europe consortium

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The effects of cholesterol on learning and memory

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Preferential accumulation of Aβ(1−42) on gel phase domains of lipid bilayers: An AFM and fluorescence study

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α-Sheet: The Toxic Conformer in Amyloid Diseases?

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Age‐dependent impairment of glucose tolerance in the 3xTg‐AD mouse model of Alzheimer's disease

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Aβ40 Oligomers Identified as a Potential Biomarker for the Diagnosis of Alzheimer's Disease

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Rational design of potent domain antibody inhibitors of amyloid fibril assembly

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Complement component C1q inhibits β‐amyloid‐ and serum amyloid P‐induced neurotoxicity via caspase‐ and calpain‐independent mechanisms

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Mechanistic aspects of Parkinson’s disease: α-synuclein and the biomembrane

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ILQINS Hexapeptide, Identified in Lysozyme Left-Handed Helical Ribbons and Nanotubes, Forms Right-Handed Helical Ribbons and Crystals

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