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Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons

Neurobiology of disease, 2018-03, Vol.111, p.26-35

2018

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Stereotaxic Targeting of Alpha-Synuclein Pathology in Mouse Brain Using Preformed Fibrils

Methods in molecular biology (Clifton, N.J.), 2019, Vol.1948, p.45

2019

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pTSara-NatB, an improved N-terminal acetylation system for recombinant protein expression in E. coli

PloS one, 2018-07, Vol.13 (7), p.e0198715-e0198715

2018

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Dynamic physiological α-synuclein S129 phosphorylation is driven by neuronal activity

NPJ Parkinson's Disease, 2023-01, Vol.9 (1), p.4-15, Article 4

2023

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Aggregation-resistant alpha-synuclein tetramers are reduced in the blood of Parkinson’s patients

EMBO molecular medicine, 2024-07, Vol.16 (7), p.1657-1674

2024

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Effects of Excess Brain-Derived Human α-Synuclein on Synaptic Vesicle Trafficking

Frontiers in neuroscience, 2021-02, Vol.15, p.639414

2021

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ExPLAining early synucleinopathies: Figure 1

Brain (London, England : 1878), 2015-06, Vol.138 (6), p.1449-1451

2015

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GM1 oligosaccharide efficacy against α-synuclein aggregation and toxicity in vitro

Biochimica et biophysica acta. Molecular and cell biology of lipids, 2023-09, Vol.1868 (9), p.159350-159350, Article 159350

2023

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Rapid iPSC inclusionopathy models shed light on formation, consequence, and molecular subtype of α-synuclein inclusions

Neuron (Cambridge, Mass.), 2024-09, Vol.112 (17), p.2886-2909.e16

2024

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Bartels & Selkoe reply

Nature (London), 2013-06, Vol.498 (7453), p.E6-E7

2013

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

Proceedings of the National Academy of Sciences - PNAS, 2015-08, Vol.112 (31), p.9596-9596

2015

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N-Alpha-Acetylation of [alpha]-Synuclein Increases Its Helical Folding Propensity, GM1 Binding Specificity and Resistance to Aggregation

PloS one, 2014-07, Vol.9 (7)

2014

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[alpha]-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

Nature (London), 2011-09, Vol.477 (7362), p.107

2011

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

Nature (London), 2011-09, Vol.477 (7362), p.107

2011

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[beta]2-Adrenoreceptor is a regulator of the [alpha]-synuclein gene driving risk of Parkinson's disease

Science (American Association for the Advancement of Science), 2017-09, Vol.357 (6354), p.891

2017

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Correction: Corrigendum: Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation

Nature communications, 2015-07, Vol.6 (1), Article 8008

2015

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Analysis of α-synuclein species enriched from cerebral cortex of humans with sporadic dementia with Lewy bodies

Brain communications, 2020-01, Vol.2 (1), p.fcaa010

2020

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Properties of native brain a-synuclein/Bartels & Selkoe reply

Nature (London), 2013-06, Vol.498 (7453), p.E4

2013

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Soluble A[beta] Oligomers Are Rapidly Sequestered from Brain ISF In Vivo and Bind GM1 Ganglioside on Cellular Membranes

Neuron (Cambridge, Mass.), 2014-04, Vol.82 (2), p.308

2014

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Defining the Native State of [alpha]-Synuclein

Neuro-degenerative diseases, 2014-01, Vol.13 (2-3), p.114-117

2014

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The N-Terminus of the Intrinsically Disordered Protein [alpha]-Synuclein Triggers Membrane Binding and Helix Folding

Biophysical journal, 2010-10, Vol.99 (7), p.2116-2124

2010

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α-Synuclein N-Terminus Elicits Vesicle Binding and Folding Nucleation

Biophysical journal, 2010-01, Vol.98 (3), p.258a-258a

2010

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Solid-State 2H NMR Spectroscopy Reveals Micromechanics of Raft-Like Ternary Lipid Membranes Containing Sphingomyelin and Cholesterol

Biophysical journal, 2009-02, Vol.96 (3), p.149a-149a

2009

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Plasmon Waveguide Resonance Shows Preferential Binding of Oligomeric alpha-Synuclein to Raft-Like Lipid Mixtures

Biophysical journal, 2009-02, Vol.96 (3), p.206a-206a

2009

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Inhibition of mitochondrial fusion by [alpha]-synuclein is rescued by PINK1, Parkin and DJ-1

The EMBO journal, 2010-10, Vol.29 (20), p.3571

2010

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Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons

Stereotaxic Targeting of Alpha-Synuclein Pathology in Mouse Brain Using Preformed Fibrils

pTSara-NatB, an improved N-terminal acetylation system for recombinant protein expression in E. coli

Dynamic physiological α-synuclein S129 phosphorylation is driven by neuronal activity

Aggregation-resistant alpha-synuclein tetramers are reduced in the blood of Parkinson’s patients

Effects of Excess Brain-Derived Human α-Synuclein on Synaptic Vesicle Trafficking

ExPLAining early synucleinopathies: Figure 1

GM1 oligosaccharide efficacy against α-synuclein aggregation and toxicity in vitro

Rapid iPSC inclusionopathy models shed light on formation, consequence, and molecular subtype of α-synuclein inclusions

Bartels & Selkoe reply

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

N-Alpha-Acetylation of [alpha]-Synuclein Increases Its Helical Folding Propensity, GM1 Binding Specificity and Resistance to Aggregation

[alpha]-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

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

[beta]2-Adrenoreceptor is a regulator of the [alpha]-synuclein gene driving risk of Parkinson's disease

Correction: Corrigendum: Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation

Analysis of α-synuclein species enriched from cerebral cortex of humans with sporadic dementia with Lewy bodies

Properties of native brain a-synuclein/Bartels & Selkoe reply

Soluble A[beta] Oligomers Are Rapidly Sequestered from Brain ISF In Vivo and Bind GM1 Ganglioside on Cellular Membranes

Defining the Native State of [alpha]-Synuclein

The N-Terminus of the Intrinsically Disordered Protein [alpha]-Synuclein Triggers Membrane Binding and Helix Folding

α-Synuclein N-Terminus Elicits Vesicle Binding and Folding Nucleation

Solid-State 2H NMR Spectroscopy Reveals Micromechanics of Raft-Like Ternary Lipid Membranes Containing Sphingomyelin and Cholesterol

Plasmon Waveguide Resonance Shows Preferential Binding of Oligomeric alpha-Synuclein to Raft-Like Lipid Mixtures

Inhibition of mitochondrial fusion by [alpha]-synuclein is rescued by PINK1, Parkin and DJ-1

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