Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae - Wikidata - awgldk - TriplyDB

Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae

Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae

http://www.wikidata.org/entity/Q30481396

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Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement Alpha-synuclein Toxicity in the Early Secretory Pathway: How It Drives Neurodegeneration in Parkinsons Disease Neuronal response in Alzheimer's and Parkinson's disease: the effect of toxic proteins on intracellular pathways Phosphorylation modulates clearance of alpha-synuclein inclusions in a yeast model of Parkinson's disease The Synaptic Function of α-Synuclein Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity α-Syn suppression reverses synaptic and memory defects in a mouse model of dementia with Lewy bodies.{alpha}-synuclein and its A30P mutant affect actin cytoskeletal structure and dynamics.Formation of α-synuclein Lewy neurite-like aggregates in axons impedes the transport of distinct endosomes.Compounds from an unbiased chemical screen reverse both ER-to-Golgi trafficking defects and mitochondrial dysfunction in Parkinson's disease models The first N-terminal amino acids of alpha-synuclein are essential for alpha-helical structure formation in vitro and membrane binding in yeast.A pathologic cascade leading to synaptic dysfunction in alpha-synuclein-induced neurodegeneration.Alpha-synuclein function and dysfunction on cellular membranes.Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis.Direct membrane association drives mitochondrial fission by the Parkinson disease-associated protein alpha-synuclein.α-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding.Aggregation of α-synuclein in S. cerevisiae is associated with defects in endosomal trafficking and phospholipid biosynthesis.Suppression of α-synuclein toxicity and vesicle trafficking defects by phosphorylation at S129 in yeast depends on genetic context.Toxic effects of human and rodent variants of alpha-synuclein in vivo.Structural basis of synaptic vesicle assembly promoted by α-synuclein.Molecular mechanisms of alpha-synuclein neurodegeneration.Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells Yeast unfolds the road map toward alpha-synuclein-induced cell death.Neurodegenerative diseases: Lessons from genome-wide screens in small model organisms.RNA-binding proteins with prion-like domains in ALS and FTLD-U.Aggresome formation and segregation of inclusions influence toxicity of α-synuclein and synphilin-1 in yeast.Contribution of yeast models to neurodegeneration research.Harnessing the power of yeast to unravel the molecular basis of neurodegeneration.Alpha-synuclein and intracellular trafficking: impact on the spreading of Parkinson's disease pathology.Loss of functional alpha-synuclein: a toxic event in Parkinson's disease?The function of α-synuclein.Parallel mechanisms for direct and indirect membrane protein trafficking by synucleins.Posttranslational Modifications and Clearing of α-Synuclein Aggregates in Yeast Unraveling protein misfolding diseases using model systems Exploring the power of yeast to model aging and age-related neurodegenerative disorders.From the baker to the bedside: yeast models of Parkinson's disease.α-Synuclein increases U251 cells vulnerability to hydrogen peroxide by disrupting calcium homeostasis.Prion-like disorders: blurring the divide between transmissibility and infectivity.Familial Parkinson's Disease Mutant E46K α-Synuclein Localizes to Membranous Structures, Forms Aggregates, and Induces Toxicity in Yeast Models.α-Synuclein promotes dilation of the exocytotic fusion pore.

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P2860

Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae

http://www.wikidata.org/entity/Q30481396

description

2008 nî lūn-bûn

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2008 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունվարին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

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2008年論文

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2008年论文

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name

Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae

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Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae

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type

label

Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae

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Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae

@en

prefLabel

Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae

@ast

Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae

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MBC.E07-08-0827

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Molecular Biology of the Cell

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Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiae

@en

P2093

Anna Stieber

http://www.w3.org/2001/XMLSchema#string

Eliza Lee

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James H Soper

http://www.w3.org/2001/XMLSchema#string

Robert B Wilson

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Subhojit Roy

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Virginia M-Y Lee

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P2860

Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity

alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast

Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models

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

The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis.

YGR198w (YPP1) targets A30P alpha-synuclein to the vacuole for degradation.

Brefeldin A-inhibited guanine nucleotide-exchange activity of Sec7 domain from yeast Sec7 with yeast and mammalian ADP ribosylation factors.

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1093-1103

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10.1091/MBC.E07-08-0827

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3

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19

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Christopher G Burd

John Q. Trojanowski

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2008-01-02T00:00:00Z

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5677827

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18172022

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Saccharomyces cerevisiae

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2262993

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