α-Synuclein is localized to mitochondria-associated ER membranes. - Wikidata - awgldk - TriplyDB

α-Synuclein is localized to mitochondria-associated ER membranes.

α-Synuclein is localized to mitochondria-associated ER membranes.

http://www.wikidata.org/entity/Q37399930

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Mitochondrial dysfunction in Parkinson's disease There's Something Wrong with my MAM; the ER-Mitochondria Axis and Neurodegenerative Diseases Mitochondria-associated membranes as hubs for neurodegeneration Parkinson's disease proteins: Novel mitochondrial targets for cardioprotection Novel subcellular localization for α-synuclein: possible functional consequences Potentiation of neurotoxicity in double-mutant mice with Pink1 ablation and A53T-SNCA overexpression.Alpha-synuclein spreading in Parkinson's disease Mitochondrial lipids in neurodegeneration Mitochondrial DNA and primary mitochondrial dysfunction in Parkinson's disease.Loss of α-Synuclein Does Not Affect Mitochondrial Bioenergetics in Rodent Neurons.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.α-Synuclein binds to the ER-mitochondria tethering protein VAPB to disrupt Ca2+ homeostasis and mitochondrial ATP production Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases.Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction.Lysosomes and α-synuclein form a dangerous duet leading to neuronal cell death.Region specific mitochondrial impairment in mice with widespread overexpression of alpha-synuclein.Monoallelic and Biallelic Variants in EMC1 Identified in Individuals with Global Developmental Delay, Hypotonia, Scoliosis, and Cerebellar Atrophy A53T human α-synuclein overexpression in transgenic mice induces pervasive mitochondria macroautophagy defects preceding dopamine neuron degeneration PGC-1α activity in nigral dopamine neurons determines vulnerability to α-synuclein Mitochondrial Dysfunction and α-Synuclein Synaptic Pathology in Parkinson's Disease: Who's on First?Isolation of Endoplasmic Reticulum, Mitochondria, and Mitochondria-Associated Membrane and Detergent Resistant Membrane Fractions from Transfected Cells and from Human Cytomegalovirus-Infected Primary Fibroblasts Aggregated Alpha-Synuclein Transfer Efficiently between Cultured Human Neuron-Like Cells and Localize to Lysosomes Understanding the susceptibility of dopamine neurons to mitochondrial stressors in Parkinson's disease.Bent out of shape: α-Synuclein misfolding and the convergence of pathogenic pathways in Parkinson's disease.Phosphatidylethanolamine Metabolism in Health and Disease.Methyl-Arginine Profile of Brain from Aged PINK1-KO+A53T-SNCA Mice Suggests Altered Mitochondrial Biogenesis.High expression of α-synuclein in damaged mitochondria with PLA2G6 dysfunction.The Enemy within: Innate Surveillance-Mediated Cell Death, the Common Mechanism of Neurodegenerative Disease.Monomeric Alpha-Synuclein Exerts a Physiological Role on Brain ATP Synthase.Mitochondria-associated membrane collapse is a common pathomechanism in SIGMAR1- and SOD1-linked ALS Role of Mitochondria-Associated Endoplasmic Reticulum Membrane in Inflammation-Mediated Metabolic Diseases Targeting α-synuclein for treatment of Parkinson's disease: mechanistic and therapeutic considerations A new pathway for mitochondrial quality control: mitochondrial-derived vesicles.Mitochondria-associated endoplasmic reticulum membranes allow adaptation of mitochondrial metabolism to glucose availability in the liver.The Parkinson Disease Mitochondrial Hypothesis: Where Are We at?Mitochondria and endoplasmic reticulum crosstalk in amyotrophic lateral sclerosis.A new role for α-synuclein in Parkinson's disease: Alteration of ER-mitochondrial communication.Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays.Current disease modifying approaches to treat Parkinson's disease.The Ubiquitination of PINK1 Is Restricted to Its Mature 52-kDa Form.

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α-Synuclein is localized to mitochondria-associated ER membranes.

http://www.wikidata.org/entity/Q37399930

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on January 2014

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

α-Synuclein is localized to mitochondria-associated ER membranes.

@en

α-Synuclein is localized to mitochondria-associated ER membranes.

@nl

type

label

α-Synuclein is localized to mitochondria-associated ER membranes.

@en

α-Synuclein is localized to mitochondria-associated ER membranes.

@nl

prefLabel

α-Synuclein is localized to mitochondria-associated ER membranes.

@en

α-Synuclein is localized to mitochondria-associated ER membranes.

@nl

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P356

JNEUROSCI.2507-13.2014

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Journal of Neuroscience

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α-Synuclein is localized to mitochondria-associated ER membranes.

@en

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Cornelia Rüb

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

Cristina Guardia-Laguarta

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

Dorothea Becker

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

Eric A Schon

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

Estela Area-Gomez

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

Jordi Magrané

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Wolfgang Voos

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

Yuhui Liu

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P2860

MAM: more than just a housekeeper

Genetics of Parkinson's disease

Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes

Mitofusin 2 tethers endoplasmic reticulum to mitochondria

ER tubules mark sites of mitochondrial division

Detergent-resistant microdomains determine the localization of sigma-1 receptors to the endoplasmic reticulum-mitochondria junction.

Mitofusins and the mitochondrial permeability transition: the potential downside of mitochondrial fusion

Mitochondria-associated ER membranes in Alzheimer disease.

Bridging gaps in phospholipid transport.

Molecular machinery of mitochondrial fusion and fission.

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249-259

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scholarly article

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10.1523/JNEUROSCI.2507-13.2014

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1

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34

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Serge Przedborski

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2014-01-01T00:00:00Z

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24381286

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3866487

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