Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking. - Wikidata - wikimedia - TriplyDB

Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.

Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.

http://www.wikidata.org/entity/Q36673364

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Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain Native α-synuclein induces clustering of synaptic-vesicle mimics via binding to phospholipids and synaptobrevin-2/VAMP2 Versatile Structures of α-Synuclein Alpha-synuclein Toxicity in the Early Secretory Pathway: How It Drives Neurodegeneration in Parkinsons Disease Biophysical characterization of α-synuclein and its controversial structure The Synaptic Function of α-Synuclein Alpha-Synuclein Oligomers-Neurotoxic Molecules in Parkinson's Disease and Other Lewy Body Disorders Alpha-synuclein structure, functions, and interactions Seeking a mechanism for the toxicity of oligomeric α-synuclein The phosphorylation of α-synuclein: development and implication for the mechanism and therapy of the Parkinson's disease Vesicular integrity in Parkinson's disease Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.Convergence of pathology in dementia with Lewy bodies and Alzheimer's disease: a role for the novel interaction of alpha-synuclein and presenilin 1 in disease.Nonaggregated α-synuclein influences SNARE-dependent vesicle docking via membrane binding.Synucleins regulate the kinetics of synaptic vesicle endocytosis.Beta-amyloid oligomers activate apoptotic BAK pore for cytochrome c release.Alpha-synuclein function and dysfunction on cellular membranes.Dynamin1 concentration in the prefrontal cortex is associated with cognitive impairment in Lewy body dementia Environmental neurotoxic challenge of conditional alpha-synuclein transgenic mice predicts a dopaminergic olfactory-striatal interplay in early PD.β-Amyloid and α-synuclein cooperate to block SNARE-dependent vesicle fusion Real-time submillisecond single-molecule FRET dynamics of freely diffusing molecules with liposome tethering.Biophysics of α-synuclein induced membrane remodelling Aggregated Alpha-Synuclein Transfer Efficiently between Cultured Human Neuron-Like Cells and Localize to Lysosomes Towards reconstitution of membrane fusion mediated by SNAREs and other synaptic proteins DT-Diaphorase Prevents Aminochrome-Induced Alpha-Synuclein Oligomer Formation and Neurotoxicity.α-Synuclein can inhibit SNARE-mediated vesicle fusion through direct interactions with lipid bilayers.Age- and brain region-dependent α-synuclein oligomerization is attributed to alterations in intrinsic enzymes regulating α-synuclein phosphorylation in aging monkey brains.Targeting α-synuclein for treatment of Parkinson's disease: mechanistic and therapeutic considerations Synaptic vesicle glycoprotein 2C (SV2C) modulates dopamine release and is disrupted in Parkinson disease.Neurodegenerative Disease Related Proteins Have Negative Effects on SNARE-Mediated Membrane Fusion in Pathological Confirmation.Structure, function and toxicity of alpha-synuclein: the Bermuda triangle in synucleinopathies.Synaptic failure and α-synuclein.Accumulation of oligomer-prone α-synuclein exacerbates synaptic and neuronal degeneration in vivo Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress.The role of Ca2+ signaling in Parkinson's disease.Animal models of α-synucleinopathy for Parkinson disease drug development.Early synaptic dysfunction induced by α-synuclein in a rat model of Parkinson's disease.A critical role for alpha-synuclein in development and function of T lymphocytes.Late stages of hematopoiesis and B cell lymphopoiesis are regulated by α-synuclein, a key player in Parkinson's disease.Amyloid-β Oligomers May Impair SNARE-Mediated Exocytosis by Direct Binding to Syntaxin 1a.

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P2860

Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.

http://www.wikidata.org/entity/Q36673364

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name

Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.

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Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.

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type

label

Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.

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Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.

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Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.

@ast

Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.

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Proceedings of the National Academy of Sciences of the United States of America

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Large α-synuclein oligomers inhibit neuronal SNARE-mediated vesicle docking.

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Bong-Kyu Choi

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Dae-Hyuk Kweon

http://www.w3.org/2001/XMLSchema#string

Jae-Yeol Kim

http://www.w3.org/2001/XMLSchema#string

Mal-Gi Choi

http://www.w3.org/2001/XMLSchema#string

Nam Ki Lee

http://www.w3.org/2001/XMLSchema#string

Yeon-Kyun Shin

http://www.w3.org/2001/XMLSchema#string

Ying Lai

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Yoosoo Yang

http://www.w3.org/2001/XMLSchema#string

P2860

Arachidonic acid-induced carbon-centered radicals and phospholipid peroxidation in cyclo-oxygenase-2-transfected PC12 cells

The synaptic vesicle cycle

Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro

Membrane fusion: grappling with SNARE and SM proteins

Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

Conformational switch of syntaxin-1 controls synaptic vesicle fusion

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

alpha-Synuclein locus triplication causes Parkinson's disease

Alpha-synuclein in Lewy bodies

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