The self-interaction of native TDP-43 C terminus inhibits its degradation and contributes to early proteinopathies.
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Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disordersTherapeutic and diagnostic challenges for frontotemporal dementiaALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43.A high-content screen identifies novel compounds that inhibit stress-induced TDP-43 cellular aggregation and associated cytotoxicity.Mitochondrial dysfunction and decrease in body weight of a transgenic knock-in mouse model for TDP-43.The influence of pathological mutations and proline substitutions in TDP-43 glycine-rich peptides on its amyloid properties and cellular toxicity.Aggregation properties of the small nuclear ribonucleoprotein U1-70K in Alzheimer disease.Self-assembled FUS binds active chromatin and regulates gene transcription.Inhibition of TDP-43 aggregation by nucleic acid bindingRNP2 of RNA recognition motif 1 plays a central role in the aberrant modification of TDP-43.UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y regulate TDP-43 protein ubiquitination.ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.Myofibrillar disruption and RNA-binding protein aggregation in a mouse model of limb-girdle muscular dystrophy 1DMass spectrometric analysis of accumulated TDP-43 in amyotrophic lateral sclerosis brains.The evolutionary scope and neurological disease linkage of yeast-prion-like proteins in humans.Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones.Caenorhabditis elegans as a model system for studying non-cell-autonomous mechanisms in protein-misfolding diseasesRegulated protein aggregation: stress granules and neurodegenerationTargeting TDP-43 in neurodegenerative diseases.Characterization and real-time imaging of the FTLD-related protein aggregation induced by amyloidogenic peptides.Profilin 1 mutants form aggregates that induce accumulation of prion-like TDP-43Delineating the membrane-disrupting and seeding properties of the TDP-43 amyloidogenic core.The N-Terminal Domain of ALS-Linked TDP-43 Assembles without Misfolding.TDP-43 self-interaction is modulated by redox-active compounds Auranofin, Chelerythrine and Riluzole.Regulatory Role of RNA Chaperone TDP-43 for RNA Misfolding and Repeat-Associated Translation in SCA31.Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.Senataxin mutations elicit motor neuron degeneration phenotypes and yield TDP-43 mislocalization in ALS4 mice and human patients
P2860
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P2860
The self-interaction of native TDP-43 C terminus inhibits its degradation and contributes to early proteinopathies.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
The self-interaction of native ...... utes to early proteinopathies.
@en
The self-interaction of native ...... utes to early proteinopathies.
@nl
type
label
The self-interaction of native ...... utes to early proteinopathies.
@en
The self-interaction of native ...... utes to early proteinopathies.
@nl
prefLabel
The self-interaction of native ...... utes to early proteinopathies.
@en
The self-interaction of native ...... utes to early proteinopathies.
@nl
P2093
P2860
P356
P1476
The self-interaction of native ...... butes to early proteinopathies
@en
P2093
C-K James Shen
Hsiang-Yu Chang
I-Fan Wang
Shin-Chen Hou
Tzong-Der Way
P2860
P2888
P356
10.1038/NCOMMS1766
P407
P577
2012-04-03T00:00:00Z