The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominant-negative mechanism
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Does a loss of TDP-43 function cause neurodegeneration?TDP-43 Proteinopathy and ALS: Insights into Disease Mechanisms and Therapeutic Targets.Astrocyte pathology and the absence of non-cell autonomy in an induced pluripotent stem cell model of TDP-43 proteinopathy.Partial loss of TDP-43 function causes phenotypes of amyotrophic lateral sclerosis.Distinct partitioning of ALS associated TDP-43, FUS and SOD1 mutants into cellular inclusionsLoss of function CHCHD10 mutations in cytoplasmic TDP-43 accumulation and synaptic integrityFormation and spreading of TDP-43 aggregates in cultured neuronal and glial cells demonstrated by time-lapse imaging.The future of blood-based biomarkers for Alzheimer's disease.Nuclear TAR DNA-binding protein 43: A new target for amyotrophic lateral sclerosis treatmentDual vulnerability of TDP-43 to calpain and caspase-3 proteolysis after neurotoxic conditions and traumatic brain injuryThe tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Conserved acidic amino acid residues in a second RNA recognition motif regulate assembly and function of TDP-43.RNP2 of RNA recognition motif 1 plays a central role in the aberrant modification of TDP-43.Allele-specific knockdown of ALS-associated mutant TDP-43 in neural stem cells derived from induced pluripotent stem cellsValproate Attenuates 25-kDa C-Terminal Fragment of TDP-43-Induced Neuronal Toxicity via Suppressing Endoplasmic Reticulum Stress and Activating Autophagy.Low molecular weight species of TDP-43 generated by abnormal splicing form inclusions in amyotrophic lateral sclerosis and result in motor neuron death.Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration.PABPN1 suppresses TDP-43 toxicity in ALS disease models.Will posttranslational modifications of brain proteins provide novel serological markers for dementias?Targeted depletion of TDP-43 expression in the spinal cord motor neurons leads to the development of amyotrophic lateral sclerosis-like phenotypes in mice.Mechanisms of disease in frontotemporal lobar degeneration: gain of function versus loss of function effectsExposure to ALS-FTD-CSF generates TDP-43 aggregates in glioblastoma cells through exosomes and TNTs-like structure.Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease modelsThe truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates.Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation.Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion.A novel Drosophila model of TDP-43 proteinopathies: N-terminal sequences combined with the Q/N domain induce protein functional loss and locomotion defectsRNA-binding proteins in neurodegenerative disease: TDP-43 and beyond.The ALS disease-associated mutant TDP-43 impairs mitochondrial dynamics and function in motor neurons.Dendritic retraction, but not atrophy, is consistent in amyotrophic lateral sclerosis-comparison between Onuf's neurons and other sacral motor neurons.Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate stateTDP-43 autoregulation: implications for disease.Protein misdirection inside and outside motor neurons in Amyotrophic Lateral Sclerosis (ALS): a possible clue for therapeutic strategiesMolecular pathology and genetic advances in amyotrophic lateral sclerosis: an emerging molecular pathway and the significance of glial pathology.Stress granules in neurodegeneration--lessons learnt from TAR DNA binding protein of 43 kDa and fused in sarcoma.Protein aggregation in amyotrophic lateral sclerosis.TDP-43 knockdown impairs neurite outgrowth dependent on its target histone deacetylase 6.TDP-43-The key to understanding amyotrophic lateral sclerosis.Exosome secretion is a key pathway for clearance of pathological TDP-43.TDP-43/FUS in motor neuron disease: Complexity and challenges.
P2860
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P2860
The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominant-negative mechanism
description
2010 nî lūn-bûn
@nan
2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The C-terminal TDP-43 fragment ...... a dominant-negative mechanism
@ast
The C-terminal TDP-43 fragment ...... a dominant-negative mechanism
@en
type
label
The C-terminal TDP-43 fragment ...... a dominant-negative mechanism
@ast
The C-terminal TDP-43 fragment ...... a dominant-negative mechanism
@en
prefLabel
The C-terminal TDP-43 fragment ...... a dominant-negative mechanism
@ast
The C-terminal TDP-43 fragment ...... a dominant-negative mechanism
@en
P2093
P2860
P1433
P1476
The C-terminal TDP-43 fragment ...... a dominant-negative mechanism
@en
P2093
Catheryne Whittle
Chunxing Yang
Linghua Qiu
Lucheng Cao
Schahram Akbarian
Weijia Tan
Zuoshang Xu
P2860
P304
P356
10.1371/JOURNAL.PONE.0015878
P407
P577
2010-12-31T00:00:00Z