Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions
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Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of ParkinsonismParkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer modelc-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's diseasePolo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivoCurcumin and its derivatives: their application in neuropharmacology and neuroscience in the 21st centurySystematic mutagenesis of α-synuclein reveals distinct sequence requirements for physiological and pathological activitiesVersatile Structures of α-SynucleinDynamic structural flexibility of α-synucleinAlpha-synuclein Toxicity in the Early Secretory Pathway: How It Drives Neurodegeneration in Parkinsons DiseasePhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Genetically engineered mouse models of Parkinson's diseaseInflammation and α-synuclein's prion-like behavior in Parkinson's disease--is there a link?The Synaptic Function of α-SynucleinSynthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational ModificationsThe phosphorylation of α-synuclein: development and implication for the mechanism and therapy of the Parkinson's diseaseDopamine and paraquat enhance α-synuclein-induced alterations in membrane conductanceTime 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 oligomersMolecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathiesTransgenic 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 Diseaseα-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomerEvaluating 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 vivoSystematic 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 SpreadingSemisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation.α-Synuclein and nonhuman primate models of Parkinson's diseaseO-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's diseaseCharacterization 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 diseaseEffects 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.
P2860
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P2860
Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions
description
2010 nî lūn-bûn
@nan
2010 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մարտին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Phosphorylation at S87 is enha ...... ynuclein-membrane interactions
@ast
Phosphorylation at S87 is enha ...... ynuclein-membrane interactions
@en
type
label
Phosphorylation at S87 is enha ...... ynuclein-membrane interactions
@ast
Phosphorylation at S87 is enha ...... ynuclein-membrane interactions
@en
prefLabel
Phosphorylation at S87 is enha ...... ynuclein-membrane interactions
@ast
Phosphorylation at S87 is enha ...... ynuclein-membrane interactions
@en
P2093
P2860
P50
P1476
Phosphorylation at S87 is enha ...... ynuclein-membrane interactions
@en
P2093
Abid Oueslati
Adrian Schmid
Carla C Rospigliosi
Claudio O Fernandez
David Eliezer
Diego Chiappe
Fariba Chegini
Gideon Shakked
Gonzalo R Lamberto
Hai-Young Kim
P2860
P304
P356
10.1523/JNEUROSCI.5922-09.2010
P407
P577
2010-03-01T00:00:00Z