Sumoylation inhibits alpha-synuclein aggregation and toxicity. - Wikidata - awgldk - TriplyDB

Sumoylation inhibits alpha-synuclein aggregation and toxicity.

Sumoylation inhibits alpha-synuclein aggregation and toxicity.

http://www.wikidata.org/entity/Q35102441

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Propagation of prions causing synucleinopathies in cultured cells Sumoylation in Synaptic Function and Dysfunction Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Disruption of SUMO-specific protease 2 induces mitochondria mediated neurodegeneration The Synaptic Function of α-Synuclein SUMOylation regulates the homologous to E6-AP carboxyl terminus (HECT) ubiquitin ligase Rsp5p.The contribution of alpha synuclein to neuronal survival and function - Implications for Parkinson's disease Alpha-synuclein structure, functions, and interactions Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications SUMO-mediated regulation of DNA damage repair and responses Comprehensive Protein Interactome Analysis of a Key RNA Helicase: Detection of Novel Stress Granule Proteins SUMOylation Is an Inhibitory Constraint that Regulates the Prion-like Aggregation and Activity of CPEB3 Dynamic Sumoylation of a Conserved Transcription Corepressor Prevents Persistent Inclusion Formation during Hyperosmotic Stress Is Transthyretin a Regulator of Ubc9 SUMOylation?Developmental regulation and spatiotemporal redistribution of the sumoylation machinery in the rat central nervous system.Dynamic Arc SUMOylation and Selective Interaction with F-Actin-Binding Protein Drebrin A in LTP Consolidation In Vivo.Lysosomes and α-synuclein form a dangerous duet leading to neuronal cell death.Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction.Complex network-driven view of genomic mechanisms underlying Parkinson's disease: analyses in dorsal motor vagal nucleus, locus coeruleus, and substantia nigra SUMO proteomics to decipher the SUMO-modified proteome regulated by various diseases.Systematic comparison of the effects of alpha-synuclein mutations on its oligomerization and aggregation.Sumoylation influences DNA break repair partly by increasing the solubility of a conserved end resection protein.The Interplay between Alpha-Synuclein Clearance and Spreading The Epstein-Barr virus miR-BHRF1-1 targets RNF4 during productive infection to promote the accumulation of SUMO conjugates and the release of infectious virus In vivo localization and identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice.Divergent signaling via SUMO modification: potential for CFTR modulation.Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins Age-related changes of protein SUMOylation balance in the AβPP Tg2576 mouse model of Alzheimer's disease.α-Synuclein and neuronal cell death.Sumoylation in neurodegenerative diseases.Protein sumoylation in brain development, neuronal morphology and spinogenesis.SUMO and Parkinson's disease.SUMO rules: regulatory concepts and their implication in neurologic functions.SUMO: a (oxidative) stressed protein.Cellular maintenance of nuclear protein homeostasis Posttranslational Modifications and Clearing of α-Synuclein Aggregates in Yeast Mechanisms of alpha-synuclein action on neurotransmission: cell-autonomous and non-cell autonomous role Sorting out release, uptake and processing of alpha-synuclein during prion-like spread of pathology.

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Sumoylation inhibits alpha-synuclein aggregation and toxicity.

http://www.wikidata.org/entity/Q35102441

description

2011 nî lūn-bûn

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2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2011 թվականի հուլիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Sumoylation inhibits alpha-synuclein aggregation and toxicity.

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Sumoylation inhibits alpha-synuclein aggregation and toxicity.

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type

label

Sumoylation inhibits alpha-synuclein aggregation and toxicity.

@ast

Sumoylation inhibits alpha-synuclein aggregation and toxicity.

@en

prefLabel

Sumoylation inhibits alpha-synuclein aggregation and toxicity.

@ast

Sumoylation inhibits alpha-synuclein aggregation and toxicity.

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Journal of Cell Biology

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Sumoylation inhibits alpha-synuclein aggregation and toxicity

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Erik Meulmeester

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

He-Hsuan Hsiao

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

Henning Urlaub

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

Jochen H Weishaupt

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

Markus Zweckstetter

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

Mathias Bähr

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Petranka Krumova

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P2860

SUMO modification of Huntingtin and Huntington's disease pathology

Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover

Transcription factor Sp3 is silenced through SUMO modification by PIAS1

Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases

Double-knockout mice for alpha- and beta-synucleins: effect on synaptic functions

Structure determination of the small ubiquitin-related modifier SUMO-1

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

alpha-Synuclein locus triplication causes Parkinson's disease

Performing in vitro sumoylation reactions using recombinant enzymes.

Mechanisms, regulation and consequences of protein SUMOylation

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49-60

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scholarly article

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10.1083/JCB.201010117

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P433

1

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194

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Frauke Melchior

Guillaume Bossis

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2011-07-01T00:00:00Z

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51483477

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21746851

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3135405

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