The differential solvent exposure of N-terminal residues provides ‘fingerprints’ of alpha-synuclein fibrillar polymorphs

Role of α-Synuclein Regions in Nucleation and Elongation of Amyloid Fiber Assembly

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Differential Membrane Binding and Seeding of Distinct α-Synuclein Fibrillar Polymorphs

(2020) Amulya Nidhi Shrivastava et al.   BIOPHYSICAL JOURNAL

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

(2020) Mohammad Shahnawaz et al.   NATURE

Protein Quality Control Pathways at the Crossroad of Synucleinopathies

(2020) Eduardo P. De Mattos et al.   Journal of Parkinsons Disease

The structural differences between patient-derived α-synuclein strains dictate characteristics of Parkinson’s disease, multiple system atrophy and dementia with Lewy bodies

(2020) Anke Van der Perren et al.   ACTA NEUROPATHOLOGICA

Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson’s disease familial A53T mutation

(2020) Yunpeng Sun et al.   CELL RESEARCH

Parkinson’s disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure

(2020) Kun Zhao et al.   Nature Communications

Interaction of the chaperones alpha B-crystallin and CHIP with fibrillar alpha-synuclein: Effects on internalization by cells and identification of interacting interfaces

(2020) Maya Bendifallah et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Parkinson’s disease-related phosphorylation at Tyr39 rearranges α-synuclein amyloid fibril structure revealed by cryo-EM

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α‐synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities

(2019) Parvez Alam et al.   JOURNAL OF NEUROCHEMISTRY

Structural heterogeneity of α-synuclein fibrils amplified from patient brain extracts

(2019) Timo Strohäker et al.   Nature Communications

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

(2019) Ricardo Guerrero-Ferreira et al.   eLife

α-Synuclein conformational strains spread, seed and target neuronal cells differentially after injection into the olfactory bulb

(2019) Nolwen L. Rey et al.   Acta Neuropathologica Communications

Pulsed Hydrogen–Deuterium Exchange Illuminates the Aggregation Kinetics of α-Synuclein, the Causative Agent for Parkinson’s Disease

(2018) Eva Illes-Toth et al.   ACS Chemical Neuroscience

How the shapes of seeds can influence pathology

(2018) Ronald Melki   NEUROBIOLOGY OF DISEASE

C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH

(2018) Ingrid M. van der Wateren et al.   Chemical Science

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

C-terminal truncation exacerbates the aggregation and cytotoxicity of α-Synuclein: A vicious cycle in Parkinson's disease

(2018) Liang Ma et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE

Parkinson's disease and multiple system atrophy have distinct α-synuclein seed characteristics

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Physico-Pathologic Mechanisms Involved in Neurodegeneration: Misfolded Protein-Plasma Membrane Interactions

(2017) Amulya Nidhi Shrivastava et al.   NEURON

Nanomechanical properties of distinct fibrillar polymorphs of the protein α-synuclein

(2016) Ali Makky et al.   Scientific Reports

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

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Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph

(2015) Joeri Verasdonck et al.   Biomolecular NMR Assignments

 -synuclein assemblies sequester neuronal  3-Na+/K+-ATPase and impair Na+ gradient

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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

The Synaptic Function of α-Synuclein

(2015) Jacqueline Burré   Journal of Parkinsons Disease

Unlike Twins: An NMR Comparison of Two α-Synuclein Polymorphs Featuring Different Toxicity

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Self-propagation of pathogenic protein aggregates in neurodegenerative diseases

(2013) Mathias Jucker et al.   NATURE

α-Synucleinopathy phenotypes

(2013) Heather McCann et al.   PARKINSONISM & RELATED DISORDERS

Structural and functional characterization of two alpha-synuclein strains

(2013) Luc Bousset et al.   Nature Communications

Solid-state NMR sequential assignments of α-synuclein

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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

Prion-like transmission of protein aggregates in neurodegenerative diseases

(2010) Patrik Brundin et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

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

(2010) Zhongqi Zhang et al.   PROTEIN SCIENCE

 -Synuclein Promotes SNARE-Complex Assembly in Vivo and in Vitro

(2010) J. Burre et al.   SCIENCE