"Structural characterization of the minimal segment of TDP-43 competent for aggregation".
about
The TDP-43 N-terminal domain structure at high resolutionALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.Electrostatic Repulsion Governs TDP-43 C-terminal Domain AggregationTwo mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation.Zinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates.TDP-43 aggregation mirrors TDP-43 knockdown, affecting the expression levels of a common set of proteins.Physiological functions and pathobiology of TDP-43 and FUS/TLS proteins.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.The N-terminal dimerization is required for TDP-43 splicing activity.TDP-43 loss of cellular function through aggregation requires additional structural determinants beyond its C-terminal Q/N prion-like domainThe structural integrity of TDP-43 N-terminus is required for efficient aggregate entrapment and consequent loss of protein function.An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds.TDP-43 self-interaction is modulated by redox-active compounds Auranofin, Chelerythrine and Riluzole.Towards a TDP-43-Based Biomarker for ALS and FTLD.The proteinopathy of D169G and K263E mutants at the RNA Recognition Motif (RRM) domain of tar DNA-binding protein (tdp43) causing neurological disorders: A computational study.TAR DNA-binding protein 43 (TDP-43) liquid-liquid phase separation is mediated by just a few aromatic residues.Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation
P2860
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P2860
"Structural characterization of the minimal segment of TDP-43 competent for aggregation".
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
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
2014年论文
@zh
2014年论文
@zh-cn
name
"Structural characterization of the minimal segment of TDP-43 competent for aggregation".
@en
type
label
"Structural characterization of the minimal segment of TDP-43 competent for aggregation".
@en
prefLabel
"Structural characterization of the minimal segment of TDP-43 competent for aggregation".
@en
P50
P1476
"Structural characterization of the minimal segment of TDP-43 competent for aggregation"
@en
P2093
Francisco E Baralle
P356
10.1016/J.ABB.2014.01.007
P407
P577
2014-01-15T00:00:00Z