Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation. - Test2 - elhamkhani - TriplyDB

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.

http://www.wikidata.org/entity/Q35085788

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Sumoylation in Synaptic Function and Dysfunction Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity Exploring the accessible conformations of N-terminal acetylated α-synuclein Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications Mutant huntingtin, abnormal mitochondrial dynamics, defective axonal transport of mitochondria, and selective synaptic degeneration in Huntington's disease The Interplay between Alpha-Synuclein Clearance and Spreading Divergent signaling via SUMO modification: potential for CFTR modulation.Inhibition of Protein Ubiquitination by Paraquat and 1-Methyl-4-Phenylpyridinium Impairs Ubiquitin-Dependent Protein Degradation Pathways.Covalent ISG15 conjugation positively regulates the ubiquitin E3 ligase activity of parkin Emerging roles of sumoylation in the regulation of actin, microtubules, intermediate filaments, and septins Site-specific differences in proteasome-dependent degradation of monoubiquitinated α-synuclein.SUMO-2 and PIAS1 modulate insoluble mutant huntingtin protein accumulation.Protein truncation as a common denominator of human neurodegenerative foldopathies.SUMO and Parkinson's disease.SUMO rules: regulatory concepts and their implication in neurologic functions.Sorting out release, uptake and processing of alpha-synuclein during prion-like spread of pathology.SUMO-regulated mitochondrial function in Parkinson's disease.Chemical ubiquitination for decrypting a cellular code.Post-translational protein arginylation in the normal nervous system and in neurodegeneration.Cell Biology and Pathophysiology of α-Synuclein.SUMO-1 is associated with a subset of lysosomes in glial protein aggregate diseases.SUMOylation and ubiquitination reciprocally regulate α-synuclein degradation and pathological aggregation.Sumoylation: Implications for Neurodegenerative Diseases.SUMO targeting of a stress-tolerant Ulp1 SUMO protease.ER Stress Induced by Tunicamycin Triggers α-Synuclein Oligomerization, Dopaminergic Neurons Death and Locomotor Impairment: a New Model of Parkinson's Disease.Fractionation for Resolution of Soluble and Insoluble Huntingtin Species.SUMO-1 promotes degradation of the polyglutamine disease protein ataxin-3 SUMOylation of Alpha-Synuclein Influences on Alpha-Synuclein Aggregation Induced by Methamphetamine

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P2860

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.

http://www.wikidata.org/entity/Q35085788

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

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name

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.

@ast

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.

@en

type

label

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.

@ast

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.

@en

prefLabel

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.

@ast

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.

@en

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J.JNS.2011.04.015

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Journal of the Neurological Sciences

P1476

Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation.

@en

P2093

Eunsung Junn

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

Kwang Chul Chung

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M Maral Mouradian

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Martha M Quezado

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Won Hee Jang

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Yong Man Kim

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P2860

Conformational equilibria in monomeric alpha-synuclein at the single-molecule level

SUMO modification of Huntingtin and Huntington's disease pathology

Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association

Alpha-synuclein in Lewy bodies

Mechanisms, regulation and consequences of protein SUMOylation

The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer.

Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein

Aggresomes formed by alpha-synuclein and synphilin-1 are cytoprotective

SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting

A novel method for high accuracy sumoylation site prediction from protein sequences

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10.1016/J.JNS.2011.04.015

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1-2

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