Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease
about
Amyloids assemble as part of recognizable structures during oogenesis in Xenopus.Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.Engineering therapeutic protein disaggregases.FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcriptionThe effects of glutamine/asparagine content on aggregation and heterologous prion induction by yeast prion-like domains.Designer protein disaggregases to counter neurodegenerative disease.RNA-binding proteins with prion-like domains in health and disease.Prions on the run: How extracellular vesicles serve as delivery vehicles for self-templating protein aggregatesPhase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics.Aβ seeds and prions: How close the fit?Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1.XIST RNA: a window into the broader role of RNA in nuclear chromosome architecture.Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity.Targeted Genetic Screen in Amyotrophic Lateral Sclerosis Reveals Novel Genetic Variants with Synergistic Effect on Clinical Phenotype.A Genetic Tool to Track Protein Aggregates and Control Prion Inheritance.RNA-binding proteins in neurodegeneration: mechanisms in aggregate.Liquidizing FUS via prion-like domain phosphorylation.Prion-like Domains Program Ewing's Sarcoma.Phosphorylation and nuclear transit modulate the balance between normal function and terminal aggregation of the yeast RNA-binding protein Ssd1.The wisdom of crowds: regulating cell function through condensed states of living matter.Epigenetic inheritance, prions and evolution.A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins.Context-Dependent and Disease-Specific Diversity in Protein Interactions within Stress Granules.Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies.RNA buffers the phase separation behavior of prion-like RNA binding proteins.Autophagy as a common pathway in amyotrophic lateral sclerosis.Prion-like Domains in Eukaryotic Viruses.Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like DomainsThe RNA-Recognition Motifs of TAR DNA-Binding Protein 43 May Play a Role in the Aberrant Self-Assembly of the ProteinAtomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregationAmyloid assembly and disassemblyUbiquilin 2: Shuttling Clients Out of Phase?
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Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease
description
2016 nî lūn-bûn
@nan
2016 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年学术文章
@wuu
2016年学术文章
@zh-cn
2016年学术文章
@zh-hans
2016年学术文章
@zh-my
2016年学术文章
@zh-sg
2016年學術文章
@yue
name
Prion-like domains as epigenet ...... s of neurodegenerative disease
@ast
Prion-like domains as epigenet ...... s of neurodegenerative disease
@en
Prion-like domains as epigenet ...... s of neurodegenerative disease
@nl
type
label
Prion-like domains as epigenet ...... s of neurodegenerative disease
@ast
Prion-like domains as epigenet ...... s of neurodegenerative disease
@en
Prion-like domains as epigenet ...... s of neurodegenerative disease
@nl
prefLabel
Prion-like domains as epigenet ...... s of neurodegenerative disease
@ast
Prion-like domains as epigenet ...... s of neurodegenerative disease
@en
Prion-like domains as epigenet ...... s of neurodegenerative disease
@nl
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P3181
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P1476
Prion-like domains as epigenet ...... s of neurodegenerative disease
@en
P2093
Oliver D King
P2860
P3181
P356
10.1016/J.BRAINRES.2016.02.037
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P5008
P577
2016-09-15T00:00:00Z