TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA
about
The TDP-43 N-terminal domain structure at high resolutionNMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional DynamicsRRM domain of ALS/FTD-causing FUS characteristic of irreversible unfolding spontaneously self-assembles into amyloid fibrils.Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.ALS-associated mutant FUS induces selective motor neuron degeneration through toxic gain of function.A novel Drosophila model of TDP-43 proteinopathies: N-terminal sequences combined with the Q/N domain induce protein functional loss and locomotion defectsPoint mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions.Prion-like propagation as a pathogenic principle in frontotemporal dementia.The N-terminal dimerization is required for TDP-43 splicing activity.Autophagy Dysregulation in ALS: When Protein Aggregates Get Out of Hand.The structural integrity of TDP-43 N-terminus is required for efficient aggregate entrapment and consequent loss of protein function.A molecular mechanism realizing sequence-specific recognition of nucleic acids by TDP-43.An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds.Biological Spectrum of Amyotrophic Lateral Sclerosis Prions.Comparative analysis of thermal unfolding simulations of RNA recognition motifs (RRMs) of TAR DNA-binding protein 43 (TDP-43).Environment-transformable sequence-structure relationship: a general mechanism for proteotoxicity.The N-Terminal Domain of ALS-Linked TDP-43 Assembles without Misfolding.A single N-terminal phosphomimic disrupts TDP-43 polymerization, phase separation, and RNA splicing.Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.Analysis of the substrate recognition state of TDP-43 to single-stranded DNA using fluorescence correlation spectroscopy.
P2860
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P2860
TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA
description
2014 nî lūn-bûn
@nan
2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
TDP-43 N terminus encodes a no ...... be shifted by binding to ssDNA
@ast
TDP-43 N terminus encodes a no ...... be shifted by binding to ssDNA
@en
TDP-43 N terminus encodes a no ...... be shifted by binding to ssDNA
@nl
type
label
TDP-43 N terminus encodes a no ...... be shifted by binding to ssDNA
@ast
TDP-43 N terminus encodes a no ...... be shifted by binding to ssDNA
@en
TDP-43 N terminus encodes a no ...... be shifted by binding to ssDNA
@nl
prefLabel
TDP-43 N terminus encodes a no ...... be shifted by binding to ssDNA
@ast
TDP-43 N terminus encodes a no ...... be shifted by binding to ssDNA
@en
TDP-43 N terminus encodes a no ...... be shifted by binding to ssDNA
@nl
P2860
P356
P1476
TDP-43 N terminus encodes a no ...... be shifted by binding to ssDNA
@en
P2093
Liang-Zhong Lim
P2860
P304
18619-18624
P356
10.1073/PNAS.1413994112
P407
P577
2014-12-12T00:00:00Z