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Two new polymorphic structures of alpha-synuclein solved by cryo-electron microscopy
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/ana.10795openalex-snapshot
The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia
inferredcites →https://doi.org/10.1002/ana.23894openalex-snapshot
G51D α‐synuclein mutation causes a novel Parkinsonian–pyramidal syndrome
inferredcites →https://doi.org/10.1002/anie.201408598openalex-snapshot
Atomic‐Resolution Three‐Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation
inferredcites →https://doi.org/10.1002/bip.10179openalex-snapshot
Structural transformation and aggregation of human α‐synuclein in trifluoroethanol: Non‐amyloid component sequence is essential and β‐sheet formation is prerequisite to aggregation
inferredcites →https://doi.org/10.1002/mds.25421openalex-snapshot
Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease
inferredcites →https://doi.org/10.1002/pro.3330openalex-snapshot
MolProbity: More and better reference data for improved all‐atom structure validation
inferredcites →https://doi.org/10.1007/s12104-011-9324-3openalex-snapshot
Solid-state NMR sequential assignments of α-synuclein
inferredcites →https://doi.org/10.1007/s12104-013-9526-yopenalex-snapshot
Yet another polymorph of α-synuclein: solid-state sequential assignments
inferredcites →https://doi.org/10.1007/s12104-015-9628-9openalex-snapshot
Further exploration of the conformational space of α-synuclein fibrils: solid-state NMR assignment of a high-pH polymorph
inferredcites →https://doi.org/10.1016/0014-5793(94)00395-5openalex-snapshot
Identification of two distinct synucleins from human brain
inferredcites →https://doi.org/10.1016/0896-6273(95)90040-3openalex-snapshot
Characterization of a novel protein regulated during the critical period for song learning in the zebra finch
inferredcites →https://doi.org/10.1016/j.jmb.2011.06.026openalex-snapshot
Structured Regions of α-Synuclein Fibrils Include the Early-Onset Parkinson's Disease Mutation Sites
inferredcites →https://doi.org/10.1016/j.jmb.2012.04.009openalex-snapshot
Structural Comparison of Mouse and Human α-Synuclein Amyloid Fibrils by Solid-State NMR
inferredcites →https://doi.org/10.1016/j.jsb.2005.07.007openalex-snapshot
Automated electron microscope tomography using robust prediction of specimen movements
inferredcites →https://doi.org/10.1016/j.jsb.2012.09.006openalex-snapshot
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
inferredcites →https://doi.org/10.1016/j.jsb.2017.02.003openalex-snapshot
Helical reconstruction in RELION
inferredcites →https://doi.org/10.1016/j.jsb.2017.03.007openalex-snapshot
Focus: The interface between data collection and data processing in cryo-EM
inferredcites →https://doi.org/10.1016/j.neurobiolaging.2011.06.022openalex-snapshot
Prion-like acceleration of a synucleinopathy in a transgenic mouse model
inferredcites →https://doi.org/10.1016/j.neurobiolaging.2014.03.024openalex-snapshot
A novel α-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson's disease-type pathology
inferredcites →https://doi.org/10.1016/j.pep.2005.02.014openalex-snapshot
A new method for purification of recombinant human α-synuclein in Escherichia coli
inferredcites →https://doi.org/10.1016/j.sbi.2014.12.001openalex-snapshot
The structure of fibrils from ‘misfolded’ proteins
inferredcites →https://doi.org/10.1016/j.sbi.2019.06.003openalex-snapshot
Imaging of post-mortem human brain tissue using electron and X-ray microscopy
inferredcites →https://doi.org/10.1016/s0006-8993(98)00514-9openalex-snapshot
Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro: Relevance for Lewy body disease
inferredcites →https://doi.org/10.1016/s0014-5793(98)01146-6openalex-snapshot
Synthetic filaments assembled from C‐terminally truncated α‐synuclein
inferredcites →https://doi.org/10.1016/s0014-5793(98)01418-5openalex-snapshot
Aggregates from mutant and wild‐type α‐synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β‐sheet and amyloid‐like filaments
inferredcites →https://doi.org/10.1016/s0079-6123(10)83007-9openalex-snapshot
Role of post-translational modifications in modulating the structure, function and toxicity of α-synuclein
inferredcites →https://doi.org/10.1016/s0140-6736(04)17103-1openalex-snapshot
α-synuclein locus duplication as a cause of familial Parkinson's disease
inferredcites →https://doi.org/10.1016/s0140-6736(04)17104-3openalex-snapshot
Causal relation between α-synuclein locus duplication as a cause of familial Parkinson's disease
inferredcites →https://doi.org/10.1016/s0304-3940(00)01440-3openalex-snapshot
Characterisation of isolated α-synuclein filaments from substantia nigra of Parkinson's disease brain
inferredcites →https://doi.org/10.1016/s0304-3940(98)00504-7openalex-snapshot
Filamentous α-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies
inferredcites →https://doi.org/10.1016/s1353-8020(13)70010-5openalex-snapshot
Update on novel familial forms of Parkinson's disease and multiple system atrophy
inferredcites →https://doi.org/10.1021/ja0650394openalex-snapshot
Proton Assisted Insensitive Nuclei Cross Polarization
inferredcites →https://doi.org/10.1021/ja209019sopenalex-snapshot
Structural Intermediates during α-Synuclein Fibrillogenesis on Phospholipid Vesicles
inferredcites →https://doi.org/10.1021/ja412105topenalex-snapshot
The Presence of an Air–Water Interface Affects Formation and Elongation of α-Synuclein Fibrils
inferredcites →https://doi.org/10.1038/3311openalex-snapshot
Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease
inferredcites →https://doi.org/10.1038/nature14547openalex-snapshot
α-Synuclein strains cause distinct synucleinopathies after local and systemic administration
inferredcites →https://doi.org/10.1038/nature15368openalex-snapshot
Structure of the toxic core of α-synuclein from invisible crystals
inferredcites →https://doi.org/10.1038/nature23002openalex-snapshot
Cryo-EM structures of tau filaments from Alzheimer’s disease
inferredcites →https://doi.org/10.1038/ncomms3575openalex-snapshot
Structural and functional characterization of two alpha-synuclein strains
inferredcites →https://doi.org/10.1038/ng0298-106openalex-snapshot
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
inferredcites →https://doi.org/10.1038/nmeth.4193openalex-snapshot
MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
inferredcites →https://doi.org/10.1038/nsmb.3194openalex-snapshot
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
inferredcites →https://doi.org/10.1038/s41422-018-0075-xopenalex-snapshot
Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy
inferredcites →https://doi.org/10.1038/s41467-018-03164-5openalex-snapshot
Physical basis of amyloid fibril polymorphism
inferredcites →https://doi.org/10.1038/s41467-018-05971-2openalex-snapshot
Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
inferredcites →https://doi.org/10.1038/s41586-018-0454-yopenalex-snapshot
Structures of filaments from Pick’s disease reveal a novel tau protein fold
inferredcites →https://doi.org/10.1038/s41586-019-1026-5openalex-snapshot
Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules
inferredcites →https://doi.org/10.1038/s41593-019-0423-2openalex-snapshot
Lewy pathology in Parkinson’s disease consists of crowded organelles and lipid membranes
inferredcites →https://doi.org/10.1063/1.3036928openalex-snapshot
Proton assisted recoupling and protein structure determination
inferredcites →https://doi.org/10.1073/pnas.0406976102openalex-snapshot
Aggregation promoting C-terminal truncation of α-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations
inferredcites →https://doi.org/10.1073/pnas.0506109102openalex-snapshot
Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
inferredcites →https://doi.org/10.1073/pnas.0712179105openalex-snapshot
The fold of α-synuclein fibrils
inferredcites →https://doi.org/10.1073/pnas.0908005106openalex-snapshot
Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells
inferredcites →https://doi.org/10.1073/pnas.1600749113openalex-snapshot
Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril
inferredcites →https://doi.org/10.1073/pnas.1604645113openalex-snapshot
Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein aggregation
inferredcites →https://doi.org/10.1073/pnas.1609291113openalex-snapshot
Reducing C-terminal truncation mitigates synucleinopathy and neurodegeneration in a transgenic model of multiple system atrophy
inferredcites →https://doi.org/10.1073/pnas.1610099113openalex-snapshot
Caspase-1 causes truncation and aggregation of the Parkinson’s disease-associated protein α-synuclein
inferredcites →https://doi.org/10.1073/pnas.90.23.11282openalex-snapshot
Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.
inferredcites →https://doi.org/10.1073/pnas.95.11.6469openalex-snapshot
α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodies
inferredcites →https://doi.org/10.1074/jbc.m004851200openalex-snapshot
Interaction of Human α-Synuclein and Parkinson's Disease Variants with Phospholipids
inferredcites →https://doi.org/10.1074/jbc.m008919200openalex-snapshot
A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly
inferredcites →https://doi.org/10.1074/jbc.m114.610774openalex-snapshot
Parkinson Disease Mutant E46K Enhances α-Synuclein Phosphorylation in Mammalian Cell Lines, in Yeast, and in Vivo
inferredcites →https://doi.org/10.1074/jbc.m501508200openalex-snapshot
A Precipitating Role for Truncated α-Synuclein and the Proteasome in α-Synuclein Aggregation
inferredcites →https://doi.org/10.1074/jbc.ra117.001068openalex-snapshot
The invasin D protein from Yersinia pseudotuberculosis selectively binds the Fab region of host antibodies and affects colonization of the intestine
inferredcites →https://doi.org/10.1093/hmg/ddx227openalex-snapshot
Loss of native α-synuclein multimerization by strategically mutating its amphipathic helix causes abnormal vesicle interactions in neuronal cells
inferredcites →https://doi.org/10.1097/wnr.0b013e3282f03db4openalex-snapshot
Localization of α-synuclein to mitochondria within midbrain of mice
inferredcites →https://doi.org/10.1101/470476openalex-snapshot
Subcellular orchestration of alpha-synuclein variants in Parkinson’s disease brains revealed by 3D multicolor STED microscopy
inferredcites →https://doi.org/10.1101/500058openalex-snapshot
The making of a Lewy body: the role of alpha-synuclein post-fibrillization modifications in regulating the formation and the maturation of pathological inclusions.
inferredcites →https://doi.org/10.1101/cshperspect.a009399openalex-snapshot
-Synuclein in Parkinson's Disease
inferredcites →https://doi.org/10.1101/cshperspect.a023572openalex-snapshot
The Three-Dimensional Structures of Amyloids
inferredcites →https://doi.org/10.1107/s0907444904019158openalex-snapshot
Coot : model-building tools for molecular graphics
inferredcites →https://doi.org/10.1111/j.1742-4658.2005.04776.xopenalex-snapshot
PA700, the regulatory complex of the 26S proteasome, interferes with α‐synuclein assembly
inferredcites →https://doi.org/10.1111/j.1750-3639.2012.00597.xopenalex-snapshot
Critical Role of Truncated α‐Synuclein and Aggregates in Parkinson's Disease and Incidental Lewy Body Disease
inferredcites →https://doi.org/10.1111/joim.12732openalex-snapshot
Amyloid fibril polymorphism: a challenge for molecular imaging and therapy
inferredcites →https://doi.org/10.1126/science.1090278openalex-snapshot
α-Synuclein Locus Triplication Causes Parkinson's Disease
inferredcites →https://doi.org/10.1126/science.276.5321.2045openalex-snapshot
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
inferredcites →https://doi.org/10.1126/science.aao2825openalex-snapshot
Fibril structure of amyloid-β(1–42) by cryo–electron microscopy
inferredcites →https://doi.org/10.1212/wnl.0b013e31828727baopenalex-snapshot
A novel α-synuclein missense mutation in Parkinson disease
inferredcites →https://doi.org/10.1371/journal.pone.0015801openalex-snapshot
Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli
inferredcites →https://doi.org/10.1371/journal.pone.0090659openalex-snapshot
Unlike Twins: An NMR Comparison of Two α-Synuclein Polymorphs Featuring Different Toxicity
inferredcites →https://doi.org/10.2353/ajpath.2007.061232openalex-snapshot
Calpain-Cleavage of α-Synuclein
inferredcites →https://doi.org/10.3389/fnins.2018.00161openalex-snapshot
Can Interactions Between α-Synuclein, Dopamine and Calcium Explain Selective Neurodegeneration in Parkinson's Disease?
inferredcites →https://doi.org/10.7554/elife.36402openalex-snapshot
Cryo-EM structure of alpha-synuclein fibrils
inferredcites →https://doi.org/10.7554/elife.42166openalex-snapshot
New tools for automated high-resolution cryo-EM structure determination in RELION-3
inferredcites →https://doi.org/10.7554/elife.43584openalex-snapshot
Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s diseases
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1016/j.bbrc.2020.04.091openalex-snapshot
Interaction of the chaperones alpha B-crystallin and CHIP with fibrillar alpha-synuclein: Effects on internalization by cells and identification of interacting interfaces
inferred← citeshttps://doi.org/10.1016/j.conb.2020.01.014openalex-snapshot
New insights on the structure of alpha-synuclein fibrils using cryo-electron microscopy
inferred← citeshttps://doi.org/10.1038/s41583-020-00416-6openalex-snapshot
Reverse engineering Lewy bodies: how far have we come and how far can we go?
inferred← citeshttps://doi.org/10.1073/pnas.1917914117openalex-snapshot
The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure
inferred← citeshttps://doi.org/10.1101/2020.05.29.124537openalex-snapshot
CryoEM reveals how the small molecule EGCG binds to Alzheimer’s brain-derived tau fibrils and initiates fibril disaggregation
inferred← citeshttps://doi.org/10.1101/2021.01.05.423442openalex-snapshot
SERF deletion modifies amyloid aggregation in a mouse model of Alzheimer’s disease
inferred← citeshttps://doi.org/10.1101/2024.01.25.577078openalex-snapshot
Stepwise recruitment of Hsc70 by DNAJB1 produces ordered arrays primed for bursts of amyloid fibre disassembly
inferred← citeshttps://doi.org/10.1186/s13024-019-0329-1openalex-snapshot
Alpha-synuclein structure and Parkinson’s disease – lessons and emerging principles
inferred← citeshttps://doi.org/10.3233/jpd-191790openalex-snapshot
Protein Quality Control Pathways at the Crossroad of Synucleinopathies
inferred← citeshttps://doi.org/10.70675/35d706bfz0d1bz440ezac4bz7fd4138464f8openalex-snapshot
Déterminants structuraux d’agrégats de Tau distincts : vers de nouveaux outils moléculaires pour discriminer les tauopathies
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