Molecular Insights into the Misfolding and Dimerization Dynamics of the Full-Length α-Synuclein from Atomistic Discrete Molecular Dynamics Simulations

Insights into the Interactions that Trigger the Primary Nucleation of Polymorphic α-Synuclein Dimers

(2022) Sapir Lan-Mark et al.   ACS Chemical Neuroscience

Consequences of variability in α-synuclein fibril structure on strain biology

(2022) Sara A. M. Holec et al.   ACTA NEUROPATHOLOGICA

α‐Synuclein phase separation and amyloid aggregation are modulated by C‐terminal truncations

(2022) Shuai Huang et al.   FEBS LETTERS

Hydrophobic/Hydrophilic Ratio of Amphiphilic Helix Mimetics Determines the Effects on Islet Amyloid Polypeptide Aggregation

(2022) Huayuan Tang et al.   Journal of Chemical Information and Modeling

Molecular crowding accelerates aggregation of α-synuclein by altering its folding pathway

(2021) Soumojit Biswas et al.   EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

(2021) Phuong H. Nguyen et al.   CHEMICAL REVIEWS

Structural insights into α-synuclein monomer–fibril interactions

(2021) Pratibha Kumari et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The structural heterogeneity of α-synuclein is governed by several distinct subpopulations with interconversion times slower than milliseconds

(2021) Jiaxing Chen et al.   STRUCTURE

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

(2021) Roberta Cascella et al.   Nature Communications

Insights into the molecular mechanism of amyloid filament formation: Segmental folding of α-synuclein on lipid membranes

(2021) Leif Antonschmidt et al.   Science Advances

Spontaneous formation of β-sheet nano-barrels during the early aggregation of Alzheimer’s amyloid beta

(2021) Yunxiang Sun et al.   Nano Today

Structure of prion β‐oligomers as determined by short‐distance crosslinking constraint‐guided discrete molecular dynamics simulations

(2021) Jason J. Serpa et al.   PROTEOMICS

Similarity of the non-amyloid-β component and C-terminal tail of monomeric and tetrameric alpha-synuclein with 14-3-3 sigma

(2021) Sarah R. Evans et al.   Computational and Structural Biotechnology Journal

Hydroxylated single-walled carbon nanotube inhibits β2m21–31 fibrillization and disrupts pre-formed proto-fibrils

(2021) Yu Zhang et al.   INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

Discriminating α-synuclein strains in Parkinson’s disease and multiple system atrophy

(2020) Mohammad Shahnawaz et al.   NATURE

The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure

(2020) David R. Boyer et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

New insights on the structure of alpha-synuclein fibrils using cryo-electron microscopy

(2020) Ricardo Guerrero-Ferreira et al.   CURRENT OPINION IN NEUROBIOLOGY

Soluble endogenous oligomeric α-synuclein species in neurodegenerative diseases: Expression, spreading, and cross-talk

(2020) Rakez Kayed et al.   Journal of Parkinsons Disease

Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity

(2020) Amberley D. Stephens et al.   Nature Communications

Conformational ensemble of native α-synuclein in solution as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations

(2019) Nicholas I. Brodie et al.   PLoS Computational Biology

α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis

(2019) Surabhi Mehra et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Molecular simulations reveal terminal group mediated stabilization of helical conformers in both amyloid-β42 and α-synuclein

(2019) Shayon Bhattacharya et al.   ACS Chemical Neuroscience

The role of lipids in α-synuclein misfolding and neurotoxicity

(2019) Cathryn L Ugalde et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Molecular insights into the surface-catalyzed secondary nucleation of amyloid-β40 (Aβ40) by the peptide fragment Aβ16–22

(2019) Samuel J. Bunce et al.   Science Advances

A Protofilament-Protofilament Interface in the Structure of Mouse α-Synuclein Fibrils

(2018) Guohua Lv et al.   BIOPHYSICAL JOURNAL

Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities

(2018) Dipita Bhattacharyya et al.   CHEMICAL COMMUNICATIONS

Comparison of the 3D Structures of Mouse and Human α-Synuclein Fibrils by Solid-State NMR and STEM

(2018) Songhwan Hwang et al.   JOURNAL OF STRUCTURAL BIOLOGY

Cryo-EM structure of alpha-synuclein fibrils

(2018) Ricardo Guerrero-Ferreira et al.   eLife

Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy

(2018) Yaowang Li et al.   CELL RESEARCH

Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel

(2018) Binsen Li et al.   Nature Communications

Mitigating Human IAPP Amyloidogenesis In Vivo with Chiral Silica Nanoribbons

(2018) Ava Faridi et al.   Small

Nucleation of β-rich oligomers and β-barrels in the early aggregation of human islet amyloid polypeptide

(2018) Yunxiang Sun et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE

Discrete Molecular Dynamics Approach to the Study of Disordered and Aggregating Proteins

(2017) Agustí Emperador et al.   Journal of Chemical Theory and Computation

Room-temperature in-cell EPR spectroscopy: alpha-Synuclein disease variants remain intrinsically disordered in the cell

(2017) Julia Cattani et al.   PHYSICAL CHEMISTRY CHEMICAL PHYSICS

Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification

(2017) Ricardo Gaspar et al.   QUARTERLY REVIEWS OF BIOPHYSICS

The Synucleinopathies: Twenty Years On

(2017) Michel Goedert et al.   Journal of Parkinsons Disease

Applications of Discrete Molecular Dynamics in biology and medicine

(2016) Elizabeth A Proctor et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

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

Alpha-synuclein structure, functions, and interactions

(2016) FatemehNouri Emamzadeh   Journal of Research in Medical Sciences

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

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

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

Familial Parkinson Disease-associated Mutations Alter the Site-specific Microenvironment and Dynamics of α-Synuclein

(2015) Shruti Sahay et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Insights on the interaction of alpha-synuclein and metals in the pathophysiology of Parkinson's disease

(2015) Eleonora Carboni et al.   Metallomics

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

(2015) Jose A. Rodriguez et al.   NATURE

Co-existence of Two Different α-Synuclein Oligomers with Different Core Structures Determined by Hydrogen/Deuterium Exchange Mass Spectrometry

(2014) Wojciech Paslawski et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

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

(2014) Ewa A. Mirecka et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

A novel α-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson's disease-type pathology

(2014) Petra Pasanen et al.   NEUROBIOLOGY OF AGING

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

Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour

(2014) Giuliana Fusco et al.   Nature Communications

α-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson’s disease and multiple system atrophy?

(2013) Aoife P. Kiely et al.   ACTA NEUROPATHOLOGICA

Identification of Fibril-Like Tertiary Contacts in Soluble Monomeric α-Synuclein

(2013) Santiago Esteban-Martín et al.   BIOPHYSICAL JOURNAL

Grcarma: A fully automated task-oriented interface for the analysis of molecular dynamics trajectories

(2013) Panagiotis I. Koukos et al.   JOURNAL OF COMPUTATIONAL CHEMISTRY

Aggregation and neurotoxicity of recombinant α-synuclein aggregates initiated by dimerization

(2013) Alireza Roostaee et al.   Molecular Neurodegeneration

Alpha-synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease

(2013) Silke Appel-Cresswell et al.   MOVEMENT DISORDERS

α-Synuclein and Neuronal Cell Death

(2012) Toru Yasuda et al.   MOLECULAR NEUROBIOLOGY

Solid-state NMR sequential assignments of α-synuclein

(2011) Julia Gath et al.   Biomolecular NMR Assignments

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

Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation

(2011) Minglei Zhao et al.   PROTEIN SCIENCE

Charge neutralization and collapse of the C-terminal tail of alpha-synuclein at low pH

(2009) Sebastian McClendon et al.   PROTEIN SCIENCE

MedusaScore: An Accurate Force Field-Based Scoring Function for Virtual Drug Screening

(2008) Shuangye Yin et al.   Journal of Chemical Information and Modeling

The fold of  -synuclein fibrils

(2008) M. Vilar et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Ab Initio Folding of Proteins with All-Atom Discrete Molecular Dynamics

(2008) Feng Ding et al.   STRUCTURE