Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions - Wikidata - awgldk - TriplyDB

Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions

Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions

http://www.wikidata.org/entity/Q30496792

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Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo Curcumin and its derivatives: their application in neuropharmacology and neuroscience in the 21st century Systematic mutagenesis of α-synuclein reveals distinct sequence requirements for physiological and pathological activities Versatile Structures of α-Synuclein Dynamic structural flexibility of α-synuclein Alpha-synuclein Toxicity in the Early Secretory Pathway: How It Drives Neurodegeneration in Parkinsons Disease Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Genetically engineered mouse models of Parkinson's disease Inflammation and α-synuclein's prion-like behavior in Parkinson's disease--is there a link?The Synaptic Function of α-Synuclein Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications The phosphorylation of α-synuclein: development and implication for the mechanism and therapy of the Parkinson's disease Dopamine and paraquat enhance α-synuclein-induced alterations in membrane conductance Time course and progression of wild type α-synuclein accumulation in a transgenic mouse model.Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomers Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies Transgenic mice expressing S129 phosphorylation mutations in α-synuclein.Post translational changes to α-synuclein control iron and dopamine trafficking; a concept for neuron vulnerability in Parkinson's disease.Metabolic Investigations of the Molecular Mechanisms Associated with Parkinson's Disease α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer Evaluating the relationship between amyloid-β and α-synuclein phosphorylated at Ser129 in dementia with Lewy bodies and Parkinson's disease.Alpha-synuclein function and dysfunction on cellular membranes.The many faces of α-synuclein: from structure and toxicity to therapeutic target.Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo Systematic comparison of the effects of alpha-synuclein mutations on its oligomerization and aggregation.Characterization of kinases involved in the phosphorylation of aggregated α-synuclein.Photobiomodulation Suppresses Alpha-Synuclein-Induced Toxicity in an AAV-Based Rat Genetic Model of Parkinson's Disease.The Interplay between Alpha-Synuclein Clearance and Spreading Semisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation.α-Synuclein and nonhuman primate models of Parkinson's disease O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein.Induction of de novo α-synuclein fibrillization in a neuronal model for Parkinson's disease Effects of Serine 129 Phosphorylation on α-Synuclein Aggregation, Membrane Association, and Internalization.Changes in properties of serine 129 phosphorylated α-synuclein with progression of Lewy-type histopathology in human brains.Structural basis of synaptic vesicle assembly promoted by α-synuclein.Alpha-synuclein post-translational modifications as potential biomarkers for Parkinson disease and other synucleinopathies.

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P2860

Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions

http://www.wikidata.org/entity/Q30496792

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2010 nî lūn-bûn

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2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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JNEUROSCI.5922-09.2010

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Journal of Neuroscience

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Phosphorylation at S87 is enha ...... ynuclein-membrane interactions

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Abid Oueslati

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Adrian Schmid

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Carla C Rospigliosi

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Claudio O Fernandez

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David Eliezer

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Diego Chiappe

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Fariba Chegini

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Gideon Shakked

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Gonzalo R Lamberto

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Hai-Young Kim

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P2860

Lrrk2 phosphorylates alpha synuclein at serine 129: Parkinson disease implications

Proteomics analysis identifies phosphorylation-dependent alpha-synuclein protein interactions

Secondary structure and dynamics of micelle bound beta- and gamma-synuclein

Residual structure, backbone dynamics, and interactions within the synuclein family

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

1H, 13C and 15N chemical shift referencing in biomolecular NMR

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

NMR View: A computer program for the visualization and analysis of NMR data

Synucleins are a novel class of substrates for G protein-coupled receptor kinases

Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein

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3184-3198

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10.1523/JNEUROSCI.5922-09.2010

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9

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Eliezer Masliah

Bernard L. Schneider

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2010-03-01T00:00:00Z

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20203178

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phosphorylation

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2947449

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