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30 results

Paper Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue. rel 2.06

TDP-43 increased TDP-43 inclusion formation in response to stressful

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Paper The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD. rel 1.81

TDP-43 CTF cell culture models. Furthermore, TDP-43 CTF expression

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Paper TDP-43 pathology is associated with increased tau burdens and seeding. rel 1.51

TDP-43 pathology TDP-43: AD(LATE-NC-). Accumulating evidence

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Paper The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominant-negative mechanism. rel 1.51

TDP-43, consequently reducing the nuclear TDP-43. In addition

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Paper Disease-linked TDP-43 hyperphosphorylation suppresses TDP-43 condensation and aggregation. rel 1.32

TDP-43, but suppress accumulation of TDP-43 in membrane

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Paper Detection and quantification of novel C-terminal TDP-43 fragments in ALS-TDP. rel 1.29

TDP-43 peptide ratio in ALS-TDP brain compared to normal

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Paper TDP-43 seeding induces cytoplasmic aggregation heterogeneity and nuclear loss of function of TDP-43. rel 1.27

TDP-43 pathology in human neurons. These findings identify TDP

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Paper Rsp5/NEDD4 and ESCRT regulate TDP-43 toxicity and turnover via an endolysosomal clearance mechanism. rel 1.24

TDP-43 endolysosomal clearance. TDP-43 colocalized and bound Rsp5/NEDD4

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Paper Rsp5/NEDD4 and ESCRT regulate TDP-43 toxicity and turnover via an endolysosomal clearance mechanism. rel 1.24

TDP-43 endolysosomal clearance. TDP-43 colocalized and bound Rsp5/NEDD4

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Paper TDP-43 pathology: From noxious assembly to therapeutic removal. rel 1.16

TDP-43 dysfunction and aggregation. The formation of TDP-43

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Paper Cytoplasmic TDP-43 is involved in cell fate during stress recovery. rel 1.16

TDP-43) is an RNA processing protein central to the pathogenesis

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Paper Location and function of TDP-43 in platelets, alterations in neurodegenerative diseases and arising considerations for current plasma biobank protocols. rel 1.16

TDP-43 proteoform and many neuron- and astrocyte-expressed TDP

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Paper TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease. rel 1.06

TDP-43 and phospho-tau showed that the TDP-43

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Paper TDP-43 promotes tau accumulation and selective neurotoxicity in bigenic Caenorhabditis elegans. rel 1.05

TDP-43. Determining the relationship between co-morbid TDP-43

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Paper TDP-43 nuclear loss in FTD/ALS causes widespread alternative polyadenylation changes. rel 1.05

TDP-43 is depleted from the nucleus of neurons in the brain

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Paper Does a loss of TDP-43 function cause neurodegeneration? rel 0.94

TDP-43) was discovered to be in the intracellular aggregates

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Paper Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration. rel 0.86

TDP-43). Here we identify that TDP-43 regulates expression

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Paper How do the RNA-binding proteins TDP-43 and FUS relate to amyotrophic lateral sclerosis and frontotemporal degeneration, and to each other? rel 0.83

TDP-43 and FUS) in amyotrophic lateral sclerosis (ALS) and frontotemporal

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Paper Understanding In Vitro Pathways to Drug Discovery for TDP-43 Proteinopathies. rel 0.77

TDP-43 mutation (TDP-43 M337V). The sodium arsenite model

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Paper Disease animal models of TDP-43 proteinopathy and their pre-clinical applications. rel 0.74

TDP-43 proteinopathy have been established. TDP-43 proteinopathy is the histologic

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Paper TDP-43 Triggers Mitochondrial DNA Release via mPTP to Activate cGAS/STING in ALS. rel 0.72

TDP-43 Triggers Mitochondrial DNA Release via mPTP to Activate

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Paper Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43. rel 0.71

TDP-43 encodes an alternative-splicing regulator with tandem RNA-recognition

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Paper Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP. rel 0.62

TDP-43. We also demonstrate that endogenous TDP-43 and FUS do not have

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Paper 10.1093/brain/awz099 rel 0.62

TDP-43 encephalopathy (LATE). LATE neuropathological change (LATE-NC) is defined

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Paper The new missense G376V-TDP-43 variant induces late-onset distal myopathy but not amyotrophic lateral sclerosis. rel 0.62

TDP-43)-positive inclusions in neurons are a hallmark of several

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Paper The new missense G376V-TDP-43 variant induces late-onset distal myopathy but not amyotrophic lateral sclerosis. rel 0.62

TDP-43)-positive inclusions in neurons are a hallmark of several

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Paper Diffuse argyrophilic grain disease with TDP-43 proteinopathy and neuronal intermediate filament inclusion disease: FTLD with mixed tau, TDP-43 and FUS pathologies. rel 0.62

TDP-43 or FUS - forms pathological inclusions in neurons and glia

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Paper ALS-causing cleavages of TDP-43 abolish its RRM2 structure and unlock CTD for enhanced aggregation and toxicity. rel 0.62

TDP-43 is cleaved into various fragments. Two major groups

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Paper The RNA-binding motif 45 (RBM45) protein accumulates in inclusion bodies in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP) patients. rel 0.55

TDP-43 or FUS pathology (FTLD-TDP and FTLD-FUS). Using

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Paper Pathogenic TARDBP mutations in amyotrophic lateral sclerosis and frontotemporal dementia: disease-associated pathways. rel 0.52

TDP-43, has also been identified as the main component

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