Tyrosine and serine phosphorylation of alpha-synuclein have opposing effects on neurotoxicity and soluble oligomer formation. - Wikidata - wikimedia - TriplyDB

Tyrosine and serine phosphorylation of alpha-synuclein have opposing effects on neurotoxicity and soluble oligomer formation.

Tyrosine and serine phosphorylation of alpha-synuclein have opposing effects on neurotoxicity and soluble oligomer formation.

http://www.wikidata.org/entity/Q37403103

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Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism Dynamic structural flexibility of α-synuclein Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)The Synaptic Function of α-Synuclein 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 Drosophila as an In Vivo Model for Human Neurodegenerative Disease Antidepressants reduce neuroinflammatory responses and astroglial alpha-synuclein accumulation in a transgenic mouse model of multiple system atrophy Phosphorylated α-synuclein in Parkinson's disease.Post translational changes to α-synuclein control iron and dopamine trafficking; a concept for neuron vulnerability in Parkinson's disease.ASIP Outstanding Investigator Award Lecture. New approaches to the pathology and genetics of neurodegeneration Dynamic changes of the phosphoproteome in postmortem mouse brains.Drosophila melanogaster in the study of human neurodegeneration.Neurodegenerative models in Drosophila: polyglutamine disorders, Parkinson disease, and amyotrophic lateral sclerosis.The role of alpha-synuclein oligomerization and aggregation in cellular and animal models of Parkinson's disease.α-Synuclein Transgenic Drosophila As a Model of Parkinson's Disease and Related Synucleinopathies.Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in α-synuclein transgenic mice.Evaluating the relationship between amyloid-β and α-synuclein phosphorylated at Ser129 in dementia with Lewy bodies and Parkinson's disease.Dopamine-mediated oxidation of methionine 127 in α-synuclein causes cytotoxicity and oligomerization of α-synuclein.Accumulation of α-synuclein in dementia with Lewy bodies is associated with decline in the α-synuclein-degrading enzymes kallikrein-6 and calpain-1.Drosophila models of Parkinson's disease: discovering relevant pathways and novel therapeutic strategies.Systematic comparison of the effects of alpha-synuclein mutations on its oligomerization and aggregation.Biochemical increase in phosphorylated alpha-synuclein precedes histopathology of Lewy-type synucleinopathies Drosophila models of proteinopathies: the little fly that could.Semisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation.Disruption of protein quality control in Parkinson's disease.Distinct clinical and neuropathological features of G51D SNCA mutation cases compared with SNCA duplication and H50Q mutation Phosphorylation of α-Synuclein at Y125 and S129 alters its metal binding properties: implications for understanding the role of α-Synuclein in the pathogenesis of Parkinson's Disease and related disorders Possible alterations in β-Synuclein, the non-amyloidogenic homologue of α-Synuclein, during progression of sporadic α-synucleinopathies Intracellular repair of oxidation-damaged α-synuclein fails to target C-terminal modification sites Effects of Serine 129 Phosphorylation on α-Synuclein Aggregation, Membrane Association, and Internalization.Serine 129 phosphorylation of membrane-associated α-synuclein modulates dopamine transporter function in a G protein-coupled receptor kinase-dependent manner.α-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson's disease and multiple system atrophy?Changes in properties of serine 129 phosphorylated α-synuclein with progression of Lewy-type histopathology in human brains.Cortical phosphorylated α-Synuclein levels correlate with brain wave spectra in Parkinson's disease Rab11 modulates α-synuclein-mediated defects in synaptic transmission and behaviour Deubiquitinase Usp8 regulates α-synuclein clearance and modifies its toxicity in Lewy body disease.Alpha-synuclein post-translational modifications as potential biomarkers for Parkinson disease and other synucleinopathies.Phosphorylation induces distinct alpha-synuclein strain formation.In vitro phosphorylation does not influence the aggregation kinetics of WT α-synuclein in contrast to its phosphorylation mutants.

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Tyrosine and serine phosphorylation of alpha-synuclein have opposing effects on neurotoxicity and soluble oligomer formation.

http://www.wikidata.org/entity/Q37403103

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 12 October 2009

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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

Tyrosine and serine phosphoryl ...... nd soluble oligomer formation.

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Tyrosine and serine phosphoryl ...... nd soluble oligomer formation.

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type

label

Tyrosine and serine phosphoryl ...... nd soluble oligomer formation.

@en

Tyrosine and serine phosphoryl ...... nd soluble oligomer formation.

@nl

prefLabel

Tyrosine and serine phosphoryl ...... nd soluble oligomer formation.

@en

Tyrosine and serine phosphoryl ...... nd soluble oligomer formation.

@nl

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Journal of Clinical Investigation

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Tyrosine and serine phosphoryl ...... nd soluble oligomer formation.

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Alessandro Negro

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Li Chen

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Magali Periquet

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Mel B Feany

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Pamela J McLean

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Xu Wang

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P2860

Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies

Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy

Parkin counteracts symptoms in a Drosophila model of Parkinson's disease.

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

alpha-Synuclein locus triplication causes Parkinson's disease

Alpha-synuclein in Lewy bodies

Targeted gene expression as a means of altering cell fates and generating dominant phenotypes

Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila

Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein

Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons

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3257-3265

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scholarly article

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10.1172/JCI39088

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11

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119

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2009-10-12T00:00:00Z

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19855133

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phosphorylation

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2769182

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