Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease. - Wikidata - awgldk - TriplyDB

Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease.

Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease.

http://www.wikidata.org/entity/Q46593989

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Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism alpha-Synuclein and neuronal cell death LRRK2 interactions with α-synuclein in Parkinson's disease brains and in cell models Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model Proteomics analysis identifies phosphorylation-dependent alpha-synuclein protein interactions 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 Highly pathogenic H5N1 influenza virus can enter the central nervous system and induce neuroinflammation and neurodegeneration Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases p25alpha relocalizes in oligodendroglia from myelin to cytoplasmic inclusions in multiple system atrophy Systematic mutagenesis of α-synuclein reveals distinct sequence requirements for physiological and pathological activities Redox Imbalance and Viral Infections in Neurodegenerative Diseases Dynamic structural flexibility of α-synuclein Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Exploring the accessible conformations of N-terminal acetylated α-synuclein The benefits of humanized yeast models to study Parkinson's disease Alpha-synuclein biology in Lewy body diseases Biochemical premotor biomarkers for Parkinson's disease Inflammation and α-synuclein's prion-like behavior in Parkinson's disease--is there a link?Transmission of α-synucleinopathy from olfactory structures deep into the temporal lobe.The Progressive BSSG Rat Model of Parkinson's: Recapitulating Multiple Key Features of the Human Disease Phosphorylation modulates clearance of alpha-synuclein inclusions in a yeast model of Parkinson's disease Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.GSK-3β dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and α-synuclein NMR Structure of Calmodulin Complexed to an N-Terminally Acetylated α-Synuclein Peptide Selective and brain-permeable polo-like kinase-2 (Plk-2) inhibitors that reduce α-synuclein phosphorylation in rat brain C-Terminal Tyrosine Residue Modifications Modulate the Protective Phosphorylation of Serine 129 of α-Synuclein in a Yeast Model of Parkinson's Disease.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 Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding Small changes huge impact: the role of protein posttranslational modifications in cellular homeostasis and disease Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease Genetic deletion of the GATA1-regulated protein α-synuclein reduces oxidative stress and nitric oxide synthase levels in mature erythrocytes Mitochondrial therapy for Parkinson's disease: neuroprotective pharmaconutrition may be disease-modifying Toxic Dopamine Metabolite DOPAL Forms an Unexpected Dicatechol Pyrrole Adduct with Lysines of α-Synuclein Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein.Proteomic characterization of an isolated fraction of synthetic proteasome inhibitor (PSI)-induced inclusions in PC12 cells might offer clues to aggresomes as a cellular defensive response against proteasome inhibition by PSI.Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions Time course and progression of wild type α-synuclein accumulation in a transgenic mouse model.

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Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease.

http://www.wikidata.org/entity/Q46593989

description

2006 nî lūn-bûn

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Phosphorylation of Ser-129 is ...... nd sporadic Lewy body disease.

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Phosphorylation of Ser-129 is ...... nd sporadic Lewy body disease.

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type

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Phosphorylation of Ser-129 is ...... nd sporadic Lewy body disease.

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Phosphorylation of Ser-129 is ...... nd sporadic Lewy body disease.

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Phosphorylation of Ser-129 is ...... nd sporadic Lewy body disease.

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Phosphorylation of Ser-129 is ...... nd sporadic Lewy body disease.

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Dale Schenk

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Donald E Walker

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Jason M Goldstein

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Jiping Huang

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Kelly Banducci

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Kristin Kling

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Linnea Diep

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Michael G Schlossmacher

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Michael Lee

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10.1074/JBC.M600933200

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