Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
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TARDBP mutation analysis in TDP-43 proteinopathies and deciphering the toxicity of mutant TDP-43TDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets.Differential roles of the ubiquitin proteasome system and autophagy in the clearance of soluble and aggregated TDP-43 speciesCasein kinase II induced polymerization of soluble TDP-43 into filaments is inhibited by heat shock proteins.A fruitful endeavor: modeling ALS in the fruit flyMutations in the ubiquitin-binding domain of OPTN/optineurin interfere with autophagy-mediated degradation of misfolded proteins by a dominant-negative mechanism.PABPN1 suppresses TDP-43 toxicity in ALS disease models.Conformational switch of polyglutamine-expanded huntingtin into benign aggregates leads to neuroprotective effect.Dominantly inherited myotonia congenita resulting from a mutation that increases open probability of the muscle chloride channel CLC-1The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates.Disease animal models of TDP-43 proteinopathy and their pre-clinical applications.Protein aggregation in amyotrophic lateral sclerosis.RNA metabolism in ALS: when normal processes become pathological.Lymphocyte repertoire selection and intracellular self/non-self-discrimination: historical overview.An acetylation switch controls TDP-43 function and aggregation propensity.Old versus New Mechanisms in the Pathogenesis of ALS.Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions.TDP-43 expression influences amyloidβ plaque deposition and tau aggregation.Activation of AMP-activated protein kinase α1 mediates mislocalization of TDP-43 in amyotrophic lateral sclerosis.CK2-An Emerging Target for Neurological and Psychiatric Disorders.TDP-43 Phosphorylation by casein kinase Iε promotes oligomerization and enhances toxicity in vivo.Post-translational Modifications and Protein Quality Control in Motor Neuron and Polyglutamine Diseases.Acetylation-induced TDP-43 pathology is suppressed by an HSF1-dependent chaperone program.The structural integrity of TDP-43 N-terminus is required for efficient aggregate entrapment and consequent loss of protein function.Drosophila Answers to TDP-43 Proteinopathies.An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds.Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity.Cell injury and premature neurodegeneration in focal malformations of cortical development.The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS.The N Termini of TAR DNA-Binding Protein 43 (TDP43) C-Terminal Fragments Influence Degradation, Aggregation Propensity, and Morphology
P2860
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P2860
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
description
2011 nî lūn-bûn
@nan
2011 թուականին հրատարակուած գիտական յօդուած
@hyw
2011 թվականին 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
@wuu
name
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
@ast
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
@en
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
@nl
type
label
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
@ast
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
@en
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
@nl
prefLabel
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
@ast
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
@en
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
@nl
P2093
P2860
P1433
P1476
Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
@en
P2093
Benjamin Pang-hsien Tu
Chiou-Yang Tang
Hsiu-Chiang Chiu
Huei-Ying Li
P2860
P304
P356
10.1371/JOURNAL.PONE.0023075
P407
P577
2011-01-01T00:00:00Z