TDP-43 loss of cellular function through aggregation requires additional structural determinants beyond its C-terminal Q/N prion-like domain
about
The extreme N-terminus of TDP-43 mediates the cytoplasmic aggregation of TDP-43 and associated toxicity in vivoThe TDP-43 N-terminal domain structure at high resolutionThe neurogenetics of alternative splicingProtein Homeostasis in Amyotrophic Lateral Sclerosis: Therapeutic Opportunities?PABPN1 suppresses TDP-43 toxicity in ALS disease models.Aggregation of AcMNPV LEF-10 and Its Impact on Viral Late Gene Expression.A novel Drosophila model of TDP-43 proteinopathies: N-terminal sequences combined with the Q/N domain induce protein functional loss and locomotion defectsZinc binding to RNA recognition motif of TDP-43 induces the formation of amyloid-like aggregates.Old versus New Mechanisms in the Pathogenesis of ALS.Exosome secretion is a key pathway for clearance of pathological TDP-43.TDP-43 aggregation mirrors TDP-43 knockdown, affecting the expression levels of a common set of proteins.Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions.TDP-43 affects splicing profiles and isoform production of genes involved in the apoptotic and mitotic cellular pathwaysStructural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.TDP-43 and Cytoskeletal Proteins in ALS.New routes in frontotemporal dementia drug discovery.Autophagy and Its Impact on Neurodegenerative Diseases: New Roles for TDP-43 and C9orf72.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.Anti-AMPA GluA3 antibodies in Frontotemporal dementia: a new molecular target.Major hnRNP proteins act as general TDP-43 functional modifiers both in Drosophila and human neuronal cells.The 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.The N-Terminal Domain of ALS-Linked TDP-43 Assembles without Misfolding.Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.RhoGAPp190: A potential player in tbph-mediated neurodegeneration in Drosophila.
P2860
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P2860
TDP-43 loss of cellular function through aggregation requires additional structural determinants beyond its C-terminal Q/N prion-like domain
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
TDP-43 loss of cellular functi ...... terminal Q/N prion-like domain
@en
type
label
TDP-43 loss of cellular functi ...... terminal Q/N prion-like domain
@en
prefLabel
TDP-43 loss of cellular functi ...... terminal Q/N prion-like domain
@en
P2093
P2860
P356
P1476
TDP-43 loss of cellular functi ...... terminal Q/N prion-like domain
@en
P2093
Francisco E Baralle
Mauricio Budini
Valentina Romano
Zainuddin Quadri
P2860
P356
10.1093/HMG/DDU415
P577
2014-08-13T00:00:00Z