A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions (Q24632492)

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English	A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions	scientific article

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27 January 2020

A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions (English)

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27 January 2020

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Yoshiaki Furukawa

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27 January 2020

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Kumi Kaneko

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Shoji Watanabe

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27 January 2020

Nobuyuki Nukina

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24 March 2011

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9

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Journal of Biological Chemistry

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286

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18664-18672

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27 January 2020

Structural insights into TDP-43 in nucleic-acid binding and domain interactions

1 reference

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Functional amyloid formation within mammalian tissue

1 reference

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

1 reference

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Protein misfolding, functional amyloid, and human disease

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TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis

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TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

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Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice

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Prion-like transmission of protein aggregates in neurodegenerative diseases

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TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration

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Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells

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TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration

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Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin

1 reference

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Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43.

1 reference

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TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity

1 reference

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Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

1 reference

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Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies

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Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells

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1 reference

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12 December 2020

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10.1074/JBC.M111.231209

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Consolidated OpenCitations Corpus – April 2017

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27 January 2020

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