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Stabilization of α-Synuclein Fibril Clusters Prevents Fragmentation and Reduces Seeding Activity and Toxicity

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Binding Modes of Thioflavin T on the Surface of Amyloid Fibrils Studied by NMR

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Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

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Molecular Mechanism of the Misfolding and Oligomerization of the Prion Protein: Current Understanding and Its Implications

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Structure of the toxic core of α-synuclein from invisible crystals

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A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers

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Sequestration of a β-Hairpin for Control of α-Synuclein Aggregation

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Characterizing the Dynamics of α-Synuclein Oligomers Using Hydrogen/Deuterium Exchange Monitored by Mass Spectrometry

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Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

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Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting

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Dissection of Conformational Conversion Events during Prion Amyloid Fibril Formation Using Hydrogen Exchange and Mass Spectrometry

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The Dynamic Structure of α-Synuclein Multimers

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Polymorph-Specific Kinetics and Thermodynamics of β-Amyloid Fibril Growth

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Atomic structure and hierarchical assembly of a cross-  amyloid fibril

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Structural and functional characterization of two alpha-synuclein strains

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Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta

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Dye-Binding Assays for Evaluation of the Effects of Small Molecule Inhibitors on Amyloid (Aβ) Self-Assembly

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Fibrillar α-Synuclein and Huntingtin Exon 1 Assemblies Are Toxic to the Cells

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Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

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α-Synuclein in Central Nervous System and from Erythrocytes, Mammalian Cells, andEscherichia coliExists Predominantly as Disordered Monomer

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Development of the Structural Core and of Conformational Heterogeneity during the Conversion of Oligomers of the Mouse Prion Protein to Worm-like Amyloid Fibrils

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

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Thioflavin T Promotes Aβ(1–40) Amyloid Fibrils Formation

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The many faces of α-synuclein: from structure and toxicity to therapeutic target

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Purified and synthetic Alzheimer's amyloid beta (A ) prions

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Binding Modes of Thioflavin T Molecules to Prion Peptide Assemblies Identified by Using Scanning Tunneling Microscopy

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Structural Role of Compensatory Amino Acid Replacements in the α-Synuclein Protein

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Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils

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In vivo demonstration that  -synuclein oligomers are toxic

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Amyloidogenic Protein-Membrane Interactions: Mechanistic Insight from Model Systems

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Salt-Induced Modulation of the Pathway of Amyloid Fibril Formation by the Mouse Prion Protein

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The Conformation and the Aggregation Kinetics of α-Synuclein Depend on the Proline Residues in Its C-Terminal Region

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Fluoroalcohol-Induced Modulation of the Pathway of Amyloid Protofibril Formation by Barstar

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Crystal structure of thioflavin-T and its binding to amyloid fibrils: insights at the molecular level

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Detection of Transient Interchain Interactions in the Intrinsically Disordered Protein α-Synuclein by NMR Paramagnetic Relaxation Enhancement

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Fibril fragmentation in amyloid assembly and cytotoxicity

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EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity

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Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation

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Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution

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Conserved core of amyloid fibrils of wild type and A30P mutant α-synuclein

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Structurally Distinct Amyloid Protofibrils Form on Separate Pathways of Aggregation of a Small Protein

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Binding Modes of Thioflavin-T to the Single-Layer β-Sheet of the Peptide Self-Assembly Mimics

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Tryptophan Fluorescence Reveals Structural Features of α-Synuclein Oligomers

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Solid-State NMR Reveals Structural Differences between Fibrils of Wild-Type and Disease-Related A53T Mutant α-Synuclein

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Molecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-Assemblies

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On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2

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EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

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Molecular structural basis for polymorphism in Alzheimer's  -amyloid fibrils

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Structure of membrane-bound  -synuclein from site-directed spin labeling and computational refinement

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The fold of  -synuclein fibrils

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Conformational Equilibria in Monomeric α-Synuclein at the Single-Molecule Level

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FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils

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