Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells.
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A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusionsALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formationHyperphosphorylation as a defense mechanism to reduce TDP-43 aggregationKinase Inhibitor Screening Identifies Cyclin-Dependent Kinases and Glycogen Synthase Kinase 3 as Potential Modulators of TDP-43 Cytosolic Accumulation during Cell Stress.Formation and spreading of TDP-43 aggregates in cultured neuronal and glial cells demonstrated by time-lapse imaging.The C-terminal TDP-43 fragments have a high aggregation propensity and harm neurons by a dominant-negative mechanismTDP-43 mediates degeneration in a novel Drosophila model of disease caused by mutations in VCP/p97.Cytoplasmic accumulation and aggregation of TDP-43 upon proteasome inhibition in cultured neurons.ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS.C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stressReview: transactive response DNA-binding protein 43 (TDP-43): mechanisms of neurodegeneration.Casein kinase II induced polymerization of soluble TDP-43 into filaments is inhibited by heat shock proteins.Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration.PABPN1 suppresses TDP-43 toxicity in ALS disease models.TDP-43 protein variants as biomarkers in amyotrophic lateral sclerosis.Aberrant assembly of RNA recognition motif 1 links to pathogenic conversion of TAR DNA-binding protein of 43 kDa (TDP-43)Developmentally Regulated RNA-binding Protein 1 (Drb1)/RNA-binding Motif Protein 45 (RBM45), a Nuclear-Cytoplasmic Trafficking Protein, Forms TAR DNA-binding Protein 43 (TDP-43)-mediated Cytoplasmic AggregatesIn vitro prion-like behaviour of TDP-43 in ALS.Cytoplasmic Relocalization of TAR DNA-Binding Protein 43 Is Not Sufficient to Reproduce Cellular Pathologies Associated with ALS In vitro.Protein aggregation in amyotrophic lateral sclerosis.Co-localization of Bunina bodies and TDP-43 inclusions in lower motor neurons in amyotrophic lateral sclerosis.Templated Aggregation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Seeding with TDP-43 Peptide Fibrils.Phosphorylation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Truncated Casein Kinase 1δ Triggers Mislocalization and Accumulation of TDP-43.The cleavage pattern of TDP-43 determines its rate of clearance and cytotoxicity.Distinct pathways leading to TDP-43-induced cellular dysfunctions.ALS-associated ataxin 2 polyQ expansions enhance stress-induced caspase 3 activation and increase TDP-43 pathological modificationsCell stress induces TDP-43 pathological changes associated with ERK1/2 dysfunction: implications in ALS.A cellular model to monitor proteasome dysfunction by alpha-synuclein.Methylene blue and dimebon inhibit aggregation of TDP-43 in cellular models.The heat shock response plays an important role in TDP-43 clearance: evidence for dysfunction in amyotrophic lateral sclerosisReducing TDP-43 aggregation does not prevent its cytotoxicity.Nucleus Accumbens 1, a Pox virus and Zinc finger/Bric-a-brac Tramtrack Broad protein binds to TAR DNA-binding protein 43 and has a potential role in Amyotrophic Lateral Sclerosis.Drosophila Answers to TDP-43 Proteinopathies.Adenoviral expression of TDP-43 and FUS genes and shRNAs for protein degradation pathways in rodent motoneurons in vitro and in vivo.Biological Spectrum of Amyotrophic Lateral Sclerosis Prions.Gain-of-function profilin 1 mutations linked to familial amyotrophic lateral sclerosis cause seed-dependent intracellular TDP-43 aggregation.Defective synthesis and release of astrocytic thrombospondin-1 mediates the neuronal TDP-43 proteinopathy, resulting in defects in neuronal integrity associated with chronic traumatic encephalopathy: in vitro studies.Biochemical and histopathological alterations in TAR DNA-binding protein-43 after acute ischemic stroke in rats.Molecular dissection of TDP-43 proteinopathies.Towards a TDP-43-Based Biomarker for ALS and FTLD.
P2860
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P2860
Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Phosphorylated and ubiquitinat ...... ecapitulated in SH-SY5Y cells.
@en
Phosphorylated and ubiquitinat ...... ecapitulated in SH-SY5Y cells.
@nl
type
label
Phosphorylated and ubiquitinat ...... ecapitulated in SH-SY5Y cells.
@en
Phosphorylated and ubiquitinat ...... ecapitulated in SH-SY5Y cells.
@nl
prefLabel
Phosphorylated and ubiquitinat ...... ecapitulated in SH-SY5Y cells.
@en
Phosphorylated and ubiquitinat ...... ecapitulated in SH-SY5Y cells.
@nl
P2093
P2860
P921
P1433
P1476
Phosphorylated and ubiquitinat ...... ecapitulated in SH-SY5Y cells.
@en
P2093
Francisco E Baralle
Haruhiko Akiyama
Masato Hasegawa
Tetsuaki Arai
P2860
P304
P356
10.1016/J.FEBSLET.2008.12.031
P407
P577
2008-12-25T00:00:00Z