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We propose that TDP-43 has a novel role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts.
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Study found that TDP-43 N-terminal domain forms a dimer or tetramer under normal conditions and inhibits TDP-43 aggregation. Disruption of dimerization can result in loss of TDP-43 splicing activity. These data provide insights into the physiological function of TDP-43 and its related proteinopathies.
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The results imply that ERp57 has a protective role against pathological events induced by mutant SOD1 and they link ERp57 to the misfolding of TDP-43 in amyotrophic lateral sclerosis.
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This report here an age-related increase and formation of ubiquitinated TDP-43 cytoplasmic inclusions after stroke.
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Study reports end-stage hippocampal sclerosis-aging to be characterized by quantifiable measures of neuron loss location, extent and severity in association with presence of dentate TDP-43 inclusions.
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Overexpression of FUS or TDP-43 causes inhibition of the ubiquitin proteasome system (UPS) and toxicity, both of which are mitigated by overexpression of the Hsp40 chaperone.
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the present analysis highlighting the structural and functional aspects of wild and mutant tdp43 will form the basis to gain insight into the proteinopathy of tdp43 and the related structure-based drug discovery. Thus, tdp43 can be used as target to develop novel therapeutic approaches or drug designing.
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The C-terminal domain of TDP-43 contains approximately 50 disease-related mutations, with no clear physicochemical link between them. This study proposes that they may disrupt liquid-liquid phase separation indirectly by interfering with the key aromatic residues identified here.
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the progression of frontotemporal lobar degeneration-TAR DNA-binding 43 protein reflects the templated cell-to-cell transneuronal spread of pathological TDP-43.
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TDP-43 deposition leads to targeted RNA instability in amyotrophic lateral sclerosis and frontotemporal dementia
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CHCHD10 mutations have a role in cytoplasmic TDP-43 accumulation and synaptic integrity
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Study confirms the high expression of hTDP-43 in the CNS, increased microgliosis and motor deficits, exhibiting further prominent ALS/FTLD pathologies, such as cytoplasmic and insoluble TDP-43 in TAR6/6 mice. This model represents not only pathological TDP-43 expression but also disease-relevant posttranslational changes.
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The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis.
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Findings highlight that the phosphatase regulator, GADD34, also functions as a kinase scaffold in response to chronic oxidative stress and recruits CK1 and oxidized TDP-43 to facilitate its phosphorylation, as seen in TDP-43 proteinopathies.
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We identified impaired RNA metabolism, secondary to TDP-43 loss of function, as a possible pathological mechanism of HSPB8 toxicity, leading to muscle and nerve degeneration
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the introduction of SOD1(G93A) and TDP43(A315T), established Amyotrophic lateral sclerosis (ALS)-related mutations, changed the subcellular expression and localization of RNAs within the neurons, showing a spatial specificity to either the soma or the axon. Altogether, we provide here the first combined inclusive profile of mRNA and miRNA expression in two ALS models at the subcellular level
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These data provide structural detail for the established mechanistic role of the well-folded TDP-43 NTD in splicing and link this function to liquid-liquid phase separation.
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TDP43 alters most splicing events with splicing factor SRSF3 in triple-negative breast cancer.
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Of the whole cohort of patients with Motor Neuron Disease and Frontotemporal Dementia, 1 patient harboured a mutation in the TAR DNA-binding protein (TARDBP) gene.
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Study demonstrated TDP-43/pTDP-43 deposition in skin nerves in ALS patients. Although the mechanisms underlying TDP-43 in ALS are currently unknown, its detection is of interest, and the deposition may occur not only in ALS but also during the aging process which is based on observations of the present study.
