The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates.
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The extreme N-terminus of TDP-43 mediates the cytoplasmic aggregation of TDP-43 and associated toxicity in vivoPathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disordersThe crystal structure of TDP-43 RRM1-DNA complex reveals the specific recognition for UG- and TG-rich nucleic acidsFormation and spreading of TDP-43 aggregates in cultured neuronal and glial cells demonstrated by time-lapse imaging.Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.Disease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-lifeTrinucleotide expansion in disease: why is there a length threshold?A network of RNA and protein interactions in Fronto Temporal Dementia.TDP-43 as a possible biomarker for frontotemporal lobar degeneration: a systematic review of existing antibodiesRBM45 homo-oligomerization mediates association with ALS-linked proteins and stress granulesStructural analysis of disease-related TDP-43 D169G mutation: linking enhanced stability and caspase cleavage efficiency to protein accumulation.Mass spectrometric analysis of accumulated TDP-43 in amyotrophic lateral sclerosis brains.Detection of TDP-43 oligomers in frontotemporal lobar degeneration-TDP.A novel Drosophila model of TDP-43 proteinopathies: N-terminal sequences combined with the Q/N domain induce protein functional loss and locomotion defectsAn insoluble frontotemporal lobar degeneration-associated TDP-43 C-terminal fragment causes neurodegeneration and hippocampus pathology in transgenic miceIn vitro prion-like behaviour of TDP-43 in ALS.Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate stateTargeting TDP-43 in neurodegenerative diseases.Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates.Old versus New Mechanisms in the Pathogenesis of ALS.Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions.Templated Aggregation of TAR DNA-binding Protein of 43 kDa (TDP-43) by Seeding with TDP-43 Peptide Fibrils.Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients.Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.TDP-43 and Cytoskeletal Proteins in ALS.ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.Profilin 1 mutants form aggregates that induce accumulation of prion-like TDP-43An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds.Platelet phosphorylated TDP-43: an exploratory study for a peripheral surrogate biomarker development for Alzheimer's disease.TDP-43 misexpression causes defects in dendritic growth.Comparative analysis of thermal unfolding simulations of RNA recognition motifs (RRMs) of TAR DNA-binding protein 43 (TDP-43).Structural Rearrangement upon Fragmentation of the Stability Core of the ALS-Linked Protein TDP-43.TDP-43 self-interaction is modulated by redox-active compounds Auranofin, Chelerythrine and Riluzole.A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation, and RNA splicing.Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.Patient-derived frontotemporal lobar degeneration brain extracts induce formation and spreading of TDP-43 pathology in vivoThe RNA-Recognition Motifs of TAR DNA-Binding Protein 43 May Play a Role in the Aberrant Self-Assembly of the Protein
P2860
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P2860
The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
The truncated C-terminal RNA r ...... ming proteinaceous aggregates.
@ast
The truncated C-terminal RNA r ...... ming proteinaceous aggregates.
@en
type
label
The truncated C-terminal RNA r ...... ming proteinaceous aggregates.
@ast
The truncated C-terminal RNA r ...... ming proteinaceous aggregates.
@en
prefLabel
The truncated C-terminal RNA r ...... ming proteinaceous aggregates.
@ast
The truncated C-terminal RNA r ...... ming proteinaceous aggregates.
@en
P2093
P2860
P356
P1476
The truncated C-terminal RNA r ...... ming proteinaceous aggregates.
@en
P2093
Chien-Hao Chiang
Hanna S Yuan
James C K Shen
Jhe-Ruei Liang
Pan-Hsien Kuo
Shuying Wang
Yi-Ting Wang
P2860
P304
P356
10.1074/JBC.M112.438564
P407
P50
P577
2013-01-31T00:00:00Z