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Microglia modulate neurodegeneration in Alzheimer's and Parkinson's diseases

Science (American Association for the Advancement of Science), 2020-10, Vol.370 (6512), p.66-69

2020

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

Proceedings of the National Academy of Sciences - PNAS, 2015-08, Vol.112 (31), p.9596-9601

2015

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N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation

PloS one, 2014-07, Vol.9 (7), p.e103727-e103727

2014

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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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A traffic jam leads to Lewy bodies

Nature neuroscience, 2019-07, Vol.22 (7), p.1043

Bartels, Tim

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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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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Conformation-Specific Detection of α-Synuclein: The Search for a Biomarker in Parkinson Disease

JAMA neurology, 2017-02, Vol.74 (2), p.146

Bartels, Tim

2017

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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.4-4, Article 4

2023

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New insights into cellular α-synuclein homeostasis in health and disease

Current opinion in neurobiology, 2016-02, Vol.36, p.15-22

2016

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

Nature (London), 2011-09, Vol.477 (7362), p.107-110

2011

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ExPLAining early synucleinopathies

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

2015

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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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In Vivo Cross-linking Reveals Principally Oligomeric Forms of α-Synuclein and β-Synuclein in Neurons and Non-neural Cells

The Journal of biological chemistry, 2013-03, Vol.288 (9), p.6371-6385

2013

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Soluble, Prefibrillar α-Synuclein Oligomers Promote Complex I-dependent, Ca2+-induced Mitochondrial Dysfunction

The Journal of biological chemistry, 2014-08, Vol.289 (31), p.21490-21507

2014

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β2-Adrenoreceptor is a regulator of the α-synuclein gene driving risk of Parkinson’s disease

Science (American Association for the Advancement of Science), 2017-09, Vol.357 (6354), p.891-898

2017

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Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1

The EMBO journal, 2010-10, Vol.29 (20), p.3571-3589

2010

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Soluble Aβ 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.308-319

2014

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

Nature communications, 2015-06, Vol.6 (1), p.7314, Article 7314

2015

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

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

2010

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Refolding of helical soluble α‐synuclein through transient interaction with lipid interfaces

FEBS letters, 2018-05, Vol.592 (9), p.1464-1472

2018

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Purification of α‑Synuclein from Human Brain Reveals an Instability of Endogenous Multimers as the Protein Approaches Purity

Biochemistry (Easton), 2015-01, Vol.54 (2), p.279-292

2015

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E46K-like α-synuclein mutants increase lipid interactions and disrupt membrane selectivity

The Journal of biological chemistry, 2019-06, Vol.294 (25), p.9799-9812

2019

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Loss of native α-synuclein multimerization by strategically mutating its amphipathic helix causes abnormal vesicle interactions in neuronal cells

Human molecular genetics, 2017-09, Vol.26 (18), p.3466-3481

2017

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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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Microglia modulate neurodegeneration in Alzheimer's and Parkinson's diseases

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

N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation

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

A traffic jam leads to Lewy bodies

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

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

Conformation-Specific Detection of α-Synuclein: The Search for a Biomarker in Parkinson Disease

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

New insights into cellular α-synuclein homeostasis in health and disease

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

ExPLAining early synucleinopathies

ExPLAining early synucleinopathies: Figure 1

In Vivo Cross-linking Reveals Principally Oligomeric Forms of α-Synuclein and β-Synuclein in Neurons and Non-neural Cells

Soluble, Prefibrillar α-Synuclein Oligomers Promote Complex I-dependent, Ca2+-induced Mitochondrial Dysfunction

β2-Adrenoreceptor is a regulator of the α-synuclein gene driving risk of Parkinson’s disease

Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1

Soluble Aβ Oligomers Are Rapidly Sequestered from Brain ISF In Vivo and Bind GM1 Ganglioside on Cellular Membranes

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

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

Refolding of helical soluble α‐synuclein through transient interaction with lipid interfaces

Purification of α‑Synuclein from Human Brain Reveals an Instability of Endogenous Multimers as the Protein Approaches Purity

E46K-like α-synuclein mutants increase lipid interactions and disrupt membrane selectivity

Loss of native α-synuclein multimerization by strategically mutating its amphipathic helix causes abnormal vesicle interactions in neuronal cells

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

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