Mitochondrial translocation of alpha-synuclein is promoted by intracellular acidification. - Wikidata - awgldk - TriplyDB

Mitochondrial translocation of alpha-synuclein is promoted by intracellular acidification.

Mitochondrial translocation of alpha-synuclein is promoted by intracellular acidification.

http://www.wikidata.org/entity/Q36791338

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alpha-Synuclein and neuronal cell death Mass-spectrometry based oxidative lipidomics and lipid imaging: applications in traumatic brain injury SPG20 protein spartin associates with cardiolipin via its plant-related senescence domain and regulates mitochondrial Ca2+ homeostasis Proteomics analysis identifies phosphorylation-dependent alpha-synuclein protein interactions Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling Parkinson's Disease: The Mitochondria-Iron Link Parkinson's disease proteins: Novel mitochondrial targets for cardioprotection Novel subcellular localization for α-synuclein: possible functional consequences Mitochondrial dysfunction and oxidative stress in Parkinson's disease Endonuclease G mediates α-synuclein cytotoxicity during Parkinson's disease Biophysics of α-synuclein membrane interactions.Adsorption of α-synuclein to supported lipid bilayers: positioning and role of electrostatics Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models Loss of α-Synuclein Does Not Affect Mitochondrial Bioenergetics in Rodent Neurons.Mitochondrial dysfunction in the limelight of Parkinson's disease pathogenesis.Oxidative stress causes reversible changes in mitochondrial permeability and structure.D-beta-hydroxybutyrate extends lifespan in C. elegans.Mitochondrial dysfunction in Parkinson's disease: pathogenesis and neuroprotection.Alpha-synuclein function and dysfunction on cellular membranes.Acceleration of α-synuclein aggregation by exosomes.Direct membrane association drives mitochondrial fission by the Parkinson disease-associated protein alpha-synuclein.NADH fluorescence lifetime is an endogenous reporter of α-synuclein aggregation in live cells Interaction of α-synuclein with vesicles that mimic mitochondrial membranes.Mitochondrial dysfunction in genetic animal models of Parkinson's disease Interaction of α-synuclein and a cell penetrating fusion peptide with higher eukaryotic cell membranes assessed by ¹⁹F NMR α-Synuclein Shows High Affinity Interaction with Voltage-dependent Anion Channel, Suggesting Mechanisms of Mitochondrial Regulation and Toxicity in Parkinson Disease.Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function.α-Synuclein and mitochondria: partners in crime?Mitochondrial mutations: newly discovered players in neuronal degeneration.Nitrated {alpha}-synuclein-induced alterations in microglial immunity are regulated by CD4+ T cell subsets Mitochondrial biology and oxidative stress in Parkinson disease pathogenesis.Proteomic studies of nitrated alpha-synuclein microglia regulation by CD4+CD25+ T cells.α-Synuclein is localized to mitochondria-associated ER membranes.Role of Mitochondria-Associated Endoplasmic Reticulum Membrane in Inflammation-Mediated Metabolic Diseases Mitochondrial trafficking of APP and alpha synuclein: Relevance to mitochondrial dysfunction in Alzheimer's and Parkinson's diseases.Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences.αSynuclein and Mitochondrial Dysfunction: A Pathogenic Partnership in Parkinson's Disease?Parkinson's disease: from genetics to treatments.α-Synuclein and mitochondrial dysfunction in Parkinson's disease.Loss of functional alpha-synuclein: a toxic event in Parkinson's disease?

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Mitochondrial translocation of alpha-synuclein is promoted by intracellular acidification.

http://www.wikidata.org/entity/Q36791338

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Diane Dieuliis

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Drake C Mitchell

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Nelson B Cole

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P2860

DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2

Hereditary early-onset Parkinson's disease caused by mutations in PINK1

Mitochondrial lipid abnormality and electron transport chain impairment in mice lacking alpha-synuclein

Antiapoptotic property of human alpha-synuclein in neuronal cell lines is associated with the inhibition of caspase-3 but not caspase-9 activity

Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease

Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases

Mice lacking alpha-synuclein are resistant to mitochondrial toxins

Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress.

Mitochondrial dysfunction and oxidative damage in parkin-deficient mice

Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin

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