TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis. - sprookjes - yvandenbroek - TriplyDB

TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis.

TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis.

http://www.wikidata.org/entity/Q37039451

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The genetics and neuropathology of frontotemporal lobar degeneration Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis Structural insights into TDP-43 in nucleic-acid binding and domain interactions TDP-43: a new player on the AD field?Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis Enhancement of proteasome activity by a small-molecule inhibitor of USP14 Loss of murine TDP-43 disrupts motor function and plays an essential role in embryogenesis.Astrocyte pathology and the absence of non-cell autonomy in an induced pluripotent stem cell model of TDP-43 proteinopathy.TDP-43 expression in mouse models of amyotrophic lateral sclerosis and spinal muscular atrophy.Transgenic rat model of neurodegeneration caused by mutation in the TDP gene.Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.Profiling the genes affected by pathogenic TDP-43 in astrocytes Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS A screen to identify cellular modulators of soluble levels of an amyotrophic lateral sclerosis (ALS)-causing mutant SOD1.TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor.Positive florbetapir PET amyloid imaging in a subject with frequent cortical neuritic plaques and frontotemporal lobar degeneration with TDP43-positive inclusions.The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Mutant induced pluripotent stem cell lines recapitulate aspects of TDP-43 proteinopathies and reveal cell-specific vulnerability.TDP-43 is a culprit in human neurodegeneration, and not just an innocent bystander.Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo Modulation of brain hemichannels and gap junction channels by pro-inflammatory agents and their possible role in neurodegeneration TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity.Clinical and pathological continuum of multisystem TDP-43 proteinopathies.Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: the TDP-43 diseases.Early Cognitive/Social Deficits and Late Motor Phenotype in Conditional Wild-Type TDP-43 Transgenic Mice.TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells.Basic mechanisms of neurodegeneration: a critical update.Regulation of mRNA transport, localization and translation in the nervous system of mammals (Review).Acute and chronically increased immunoreactivity to phosphorylation-independent but not pathological TDP-43 after a single traumatic brain injury in humans.TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.RNA-binding proteins with prion-like domains in ALS and FTLD-U.Interaction between pathogenic proteins in neurodegenerative disorders.Significance and limitation of the pathological classification of TDP-43 proteinopathy.An acetylation switch controls TDP-43 function and aggregation propensity.Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients.Prion-like disorders: blurring the divide between transmissibility and infectivity.Caspase-cleaved TAR DNA-binding protein-43 is a major pathological finding in Alzheimer's disease.Caspase-cleaved TAR DNA-binding protein-43 in Pick's disease.

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TDP-43 proteinopathies: neurodegenerative protein misfolding diseases without amyloidosis.

http://www.wikidata.org/entity/Q37039451

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 05 December 2007

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

TDP-43 proteinopathies: neurod ...... diseases without amyloidosis.

@en

TDP-43 proteinopathies: neurod ...... diseases without amyloidosis.

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type

label

TDP-43 proteinopathies: neurod ...... diseases without amyloidosis.

@en

TDP-43 proteinopathies: neurod ...... diseases without amyloidosis.

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prefLabel

TDP-43 proteinopathies: neurod ...... diseases without amyloidosis.

@en

TDP-43 proteinopathies: neurod ...... diseases without amyloidosis.

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TDP-43 proteinopathies: neurod ...... diseases without amyloidosis.

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Kunihiro Uryu

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Linda K Kwong

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Virginia M-Y Lee

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P2860

Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping

Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia

Higher order arrangement of the eukaryotic nuclear bodies.

Heterogeneity of ubiquitin pathology in frontotemporal lobar degeneration: classification and relation to clinical phenotype

The prevalence and causes of dementia in people under the age of 65 years

Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene.

Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21

Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17

TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing

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41-51

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scholarly article

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10.1159/000109758

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1

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16

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John Q. Trojanowski

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2007-12-05T00:00:00Z

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240273810

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18097159

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neurodegeneration