Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region.
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Interaction of RNA with a C-terminal fragment of the amyotrophic lateral sclerosis-associated TDP43 reduces cytotoxicityThe TDP-43 N-terminal domain structure at high resolutionThe dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation.Selective forelimb impairment in rats expressing a pathological TDP-43 25 kDa C-terminal fragment to mimic amyotrophic lateral sclerosis.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesNuclear TAR DNA-binding protein 43: A new target for amyotrophic lateral sclerosis treatmentFunctional genomic screen of human stem cell differentiation reveals pathways involved in neurodevelopment and neurodegeneration.TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNATargeting RNA binding proteins involved in neurodegeneration.Valproate Attenuates 25-kDa C-Terminal Fragment of TDP-43-Induced Neuronal Toxicity via Suppressing Endoplasmic Reticulum Stress and Activating Autophagy.ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.Comparison of parallel high-throughput RNA sequencing between knockout of TDP-43 and its overexpression reveals primarily nonreciprocal and nonoverlapping gene expression changes in the central nervous system of DrosophilaTDP-43 is intercellularly transmitted across axon terminalsExposure to ALS-FTD-CSF generates TDP-43 aggregates in glioblastoma cells through exosomes and TNTs-like structure.Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation and inclusion formation.Aberrant assembly of RNA recognition motif 1 links to pathogenic conversion of TAR DNA-binding protein of 43 kDa (TDP-43)Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion.A novel Drosophila model of TDP-43 proteinopathies: N-terminal sequences combined with the Q/N domain induce protein functional loss and locomotion defectsPrion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones.Evolutionarily conserved heterogeneous nuclear ribonucleoprotein (hnRNP) A/B proteins functionally interact with human and Drosophila TAR DNA-binding protein 43 (TDP-43).Synaptic control of local translation: the plot thickens with new characters.Targeting TDP-43 in neurodegenerative diseases.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.Characterization and real-time imaging of the FTLD-related protein aggregation induced by amyloidogenic peptides.Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.Neurodegeneration and RNA-binding proteins.Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.Disease-associated mutations of TDP-43 promote turnover of the protein through the proteasomal pathway.Prions on the run: How extracellular vesicles serve as delivery vehicles for self-templating protein aggregatesNew routes in frontotemporal dementia drug discovery.Autophagy and Its Impact on Neurodegenerative Diseases: New Roles for TDP-43 and C9orf72.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.Platelet phosphorylated TDP-43: an exploratory study for a peripheral surrogate biomarker development for Alzheimer's disease.Robustness and Vulnerability of the Autoregulatory System That Maintains Nuclear TDP-43 Levels: A Trade-off Hypothesis for ALS Pathology Based on in Silico Data.TAR DNA-binding protein 43 (TDP-43) liquid-liquid phase separation is mediated by just a few aromatic residues.
P2860
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P2860
Cellular model of TAR DNA-binding protein 43 (TDP-43) aggregation based on its C-terminal Gln/Asn-rich region.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Cellular model of TAR DNA-bind ...... -terminal Gln/Asn-rich region.
@en
type
label
Cellular model of TAR DNA-bind ...... -terminal Gln/Asn-rich region.
@en
prefLabel
Cellular model of TAR DNA-bind ...... -terminal Gln/Asn-rich region.
@en
P2093
P2860
P356
P1476
Cellular model of TAR DNA-bind ...... -terminal Gln/Asn-rich region.
@en
P2093
Corrado Guarnaccia
Francisco E Baralle
Laura De Conti
Mauricio Budini
Valentina Romano
P2860
P304
P356
10.1074/JBC.M111.288720
P407
P577
2012-01-10T00:00:00Z