The fold preference and thermodynamic stability of α-synuclein fibrils is encoded in the non-amyloid-β component region

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes

(2017) Wei Qiang et al.   NATURE

The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction

(2017) Begoña Sot et al.   Scientific Reports

Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy

(2017) Steven J. Roeters et al.   Scientific Reports

Strain-specific Fibril Propagation by an Aβ Dodecamer

(2017) Dexter N. Dean et al.   Scientific Reports

Signature of an aggregation-prone conformation of tau

(2017) Neil A. Eschmann et al.   Scientific Reports

How Does Hyperphopsphorylation Promote Tau Aggregation and Modulate Filament Structure and Stability?

(2016) Liang Xu et al.   ACS Chemical Neuroscience

Molecular tweezers for lysine and arginine – powerful inhibitors of pathologic protein aggregation

(2016) Thomas Schrader et al.   CHEMICAL COMMUNICATIONS

Coupling of the non-amyloid-component (NAC) domain and the KTK(E/Q)GV repeats stabilize the α-synuclein fibrils

(2016) Liang Xu et al.   EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY

Evidence of Coupling between the Motions of Water and Peptides

(2016) Silvina Cerveny et al.   Journal of Physical Chemistry Letters

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

(2016) Michael T. Colvin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Structural disorder of monomeric α-synuclein persists in mammalian cells

(2016) Francois-Xavier Theillet et al.   NATURE

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

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Bifunctional Anti-Non-Amyloid Component α-Synuclein Nanobodies Are Protective In Situ

(2016) David C. Butler et al.   PLoS One

Computational investigation of cold denaturation in the Trp-cage miniprotein

(2016) Sang Beom Kim et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Dynamics and mechanism of ultrafast water–protein interactions

(2016) Yangzhong Qin et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

(2016) Marielle Aulikki Wälti et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Towards a structural biology of the hydrophobic effect in protein folding

(2016) Carlo Camilloni et al.   Scientific Reports

Structural and fluctuational difference between two ends of Aβ amyloid fibril: MD simulations predict only one end has open conformations

(2016) Hisashi Okumura et al.   Scientific Reports

Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson’s disease brain

(2015) Rosalind F. Roberts et al.   BRAIN

Systematic characterization of protein folding pathways using diffusion maps: Application to Trp-cage miniprotein

(2015) Sang Beom Kim et al.   JOURNAL OF CHEMICAL PHYSICS

A Proposed Atomic Structure of the Self-Assembly of the Non-Amyloid-β Component of Human α-Synuclein As Derived by Computational Tools

(2015) Yoav Atsmon-Raz et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Tau Assembly: The Dominant Role of PHF6 (VQIVYK) in Microtubule Binding Region Repeat R3

(2015) Pritam Ganguly et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Targeting α-synuclein for treatment of Parkinson's disease: mechanistic and therapeutic considerations

(2015) Benjamin Dehay et al.   LANCET NEUROLOGY

α-Synuclein strains cause distinct synucleinopathies after local and systemic administration

(2015) W. Peelaerts et al.   NATURE

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

(2015) Jose A. Rodriguez et al.   NATURE

Amyloid Polymorphism: Structural Basis and Neurobiological Relevance

(2015) Robert Tycko   NEURON

KTKEGV repeat motifs are key mediators of normal α-synuclein tetramerization: Their mutation causes excess monomers and neurotoxicity

(2015) Ulf Dettmer et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Hydration water mobility is enhanced around tau amyloid fibers

(2015) Yann Fichou et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Alzheimer's and Parkinson's diseases: The prion concept in relation to assembled A , tau, and  -synuclein

(2015) M. Goedert   SCIENCE

Cold Denaturation of α-Synuclein Amyloid Fibrils

(2014) Tatsuya Ikenoue et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Evidence of Native α-Synuclein Conformers in the Human Brain

(2014) Neal Gould et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies

(2014) David W. Sanders et al.   NEURON

Distinct synthetic A  prion strains producing different amyloid deposits in bigenic mice

(2014) J. Stohr et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Solution conditions determine the relative importance of nucleation and growth processes in  -synuclein aggregation

(2014) A. K. Buell et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Physical and structural basis for polymorphism in amyloid fibrils

(2014) Robert Tycko   PROTEIN SCIENCE

A fully atomistic computer simulation study of cold denaturation of a β-hairpin

(2014) Changwon Yang et al.   Nature Communications

Prion Strains and Amyloid Polymorphism Influence Phenotypic Variation

(2014) Kevin C. Stein et al.   PLoS Pathogens

Prion-like spreading of pathological α-synuclein in brain

(2013) Masami Masuda-Suzukake et al.   BRAIN

Distinct α-Synuclein Strains Differentially Promote Tau Inclusions in Neurons

(2013) Jing L. Guo et al.   CELL

The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes

(2013) Nikolai Lorenzen et al.   FEBS LETTERS

Parkinson's Disease and Alpha Synuclein: Is Parkinson's Disease a Prion-Like Disorder?

(2013) C. Warren Olanow et al.   MOVEMENT DISORDERS

Structural and functional characterization of two alpha-synuclein strains

(2013) Luc Bousset et al.   Nature Communications

The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brush

(2012) Susanne Wegmann et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

α-Synuclein misfolding and Parkinson's disease

(2011) Leonid Breydo et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE

The role of the C-terminus of human α-synuclein: Intra-disulfide bonds between the C-terminus and other regions stabilize non-fibrillar monomeric isomers

(2011) Dong-Pyo Hong et al.   FEBS LETTERS

Structured Regions of α-Synuclein Fibrils Include the Early-Onset Parkinson's Disease Mutation Sites

(2011) Gemma Comellas et al.   JOURNAL OF MOLECULAR BIOLOGY

α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

(2011) Tim Bartels et al.   NATURE

A soluble  -synuclein construct forms a dynamic tetramer

(2011) W. Wang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

In vivo demonstration that  -synuclein oligomers are toxic

(2011) B. Winner et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Protein Simulations with an Optimized Water Model: Cooperative Helix Formation and Temperature-Induced Unfolded State Collapse

(2010) Robert B. Best et al.   JOURNAL OF PHYSICAL CHEMISTRY B

A Combinatorial NMR and EPR Approach for Evaluating the Structural Ensemble of Partially Folded Proteins

(2010) Jampani Nageswara Rao et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Differences in prion strain conformations result from non-native interactions in a nucleus

(2010) Yumiko Ohhashi et al.   Nature Chemical Biology

The effect of amino acid substitution in the imperfect repeat sequences of α-synuclein on fibrillation

(2009) Ryuichi Harada et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE

A unified model of protein dynamics

(2009) H. Frauenfelder et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water

(2008) Hai-Young Kim et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Cold- and Pressure-Induced Dissociation of Protein Aggregates and Amyloid Fibrils

(2008) Rajesh Mishra et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

P-LINCS:  A Parallel Linear Constraint Solver for Molecular Simulation

(2007) Berk Hess   Journal of Chemical Theory and Computation