Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion.
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TDP-35 sequesters TDP-43 into cytoplasmic inclusions through binding with RNAPathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disordersThe TDP-43 N-terminal domain structure at high resolutionElucidation of the Aggregation Pathways of Helix-Turn-Helix Peptides: Stabilization at the Turn Region Is Critical for Fibril Formation.The influence of pathological mutations and proline substitutions in TDP-43 glycine-rich peptides on its amyloid properties and cellular toxicity.Sequestration of cellular interacting partners by protein aggregates: implication in a loss-of-function pathology.An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution.ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation.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 defectsTDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells.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.Characterization and real-time imaging of the FTLD-related protein aggregation induced by amyloidogenic peptides.Full-length TDP-43 forms toxic amyloid oligomers that are present in frontotemporal lobar dementia-TDP patients.An acridine derivative, [4,5-bis{(N-carboxy methyl imidazolium)methyl}acridine] dibromide, shows anti-TDP-43 aggregation effect in ALS disease models.ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain.The N-terminal dimerization is required for TDP-43 splicing activity.An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds.HSP90 recognizes the N-terminus of huntingtin involved in regulation of huntingtin aggregation by USP19.Pathological hydrogen peroxide triggers the fibrillization of wild-type SOD1 via sulfenic acid modification of Cys-111.Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation
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P2860
Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion.
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 20 May 2013
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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
Structural transformation of t ...... ion and cytoplasmic inclusion.
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Structural transformation of t ...... ion and cytoplasmic inclusion.
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type
label
Structural transformation of t ...... ion and cytoplasmic inclusion.
@en
Structural transformation of t ...... ion and cytoplasmic inclusion.
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prefLabel
Structural transformation of t ...... ion and cytoplasmic inclusion.
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Structural transformation of t ...... ion and cytoplasmic inclusion.
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P2093
P2860
P356
P1476
Structural transformation of t ...... ion and cytoplasmic inclusion.
@en
P2093
Chen-Jie Zhou
Hai-Yin Li
Hong-Yu Hu
Jian-Hua He
Lei-Lei Jiang
Mei-Xia Che
Mu-Yun Xie
P2860
P304
19614-19624
P356
10.1074/JBC.M113.463828
P407
P577
2013-05-20T00:00:00Z