Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization - Wikidata - awgldk - TriplyDB

Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization

Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization

http://www.wikidata.org/entity/Q28588090

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Inside out: the role of nucleocytoplasmic transport in ALS and FTLD Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis The new (dis)order in RNA regulation Dysregulated axonal RNA translation in amyotrophic lateral sclerosis Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease G3BP-Caprin1-USP10 complexes mediate stress granule condensation and associate with 40S subunits Dynamics of the formation of a hydrogel by a pathogenic amyloid peptide: islet amyloid polypeptide.Phase Transition in Postsynaptic Densities Underlies Formation of Synaptic Complexes and Synaptic Plasticity ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure.Phase separation in biology; functional organization of a higher order The contribution of intrinsically disordered regions to protein function, cellular complexity, and human disease Flavivirus Infection Uncouples Translation Suppression from Cellular Stress Responses Determinants of Amyloid Formation for the Yeast Termination Factor Nab3 Are aberrant phase transitions a driver of cellular aging?RNA Remodeling Activity of DEAD Box Proteins Tuned by Protein Concentration, RNA Length, and ATP Arginine Demethylation of G3BP1 Promotes Stress Granule Assembly Polar Positioning of Phase-Separated Liquid Compartments in Cells Regulated by an mRNA Competition Mechanism.Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain Polymers.Prions, amyloids, and RNA: Pieces of a puzzle.RNA metabolism in neurodegenerative disease.Modelling amyotrophic lateral sclerosis: progress and possibilities An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.RNA stores tau reversibly in complex coacervates C. elegans SUP-46, an HNRNPM family RNA-binding protein that prevents paternally-mediated epigenetic sterility.Genetic interaction of hnRNPA2B1 and DNAJB6 in a Drosophila model of multisystem proteinopathy.Interaction of tau with the RNA-Binding Protein TIA1 Regulates tau Pathophysiology and Toxicity.Coexisting Liquid Phases Underlie Nucleolar Subcompartments.Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein.Mechanistic insights into mammalian stress granule dynamics.Granulostasis: Protein Quality Control of RNP Granules.Dysregulation of RNA Binding Protein Aggregation in Neurodegenerative Disorders.Altered mRNP granule dynamics in FTLD pathogenesis.Rabies Virus Infection Induces the Formation of Stress Granules Closely Connected to the Viral Factories.Formation and Maturation of Phase-Separated Liquid Droplets by RNA-Binding Proteins.Retrotransposon activation contributes to neurodegeneration in a Drosophila TDP-43 model of ALS Rapidly Translated Polypeptides Are Preferred Substrates for Cotranslational Protein Degradation.The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules.The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei.Higher-order oligomerization promotes localization of SPOP to liquid nuclear speckles.

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P2860

Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization

http://www.wikidata.org/entity/Q28588090

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2015 nî lūn-bûn

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2015 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2015 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

Phase separation by low comple ...... es pathological fibrillization

@ast

Phase separation by low comple ...... es pathological fibrillization

@en

Phase separation by low comple ...... es pathological fibrillization

@nl

type

label

Phase separation by low comple ...... es pathological fibrillization

@ast

Phase separation by low comple ...... es pathological fibrillization

@en

Phase separation by low comple ...... es pathological fibrillization

@nl

prefLabel

Phase separation by low comple ...... es pathological fibrillization

@ast

Phase separation by low comple ...... es pathological fibrillization

@en

Phase separation by low comple ...... es pathological fibrillization

@nl

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Phase separation by low comple ...... es pathological fibrillization

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Amandine Molliex

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Anderson P Kanagaraj

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Hong Joo Kim

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Jamshid Temirov

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P2860

Mobility measurement by analysis of fluorescence photobleaching recovery kinetics

Altered ribostasis: RNA-protein granules in degenerative disorders

Eukaryotic stress granules are cleared by autophagy and Cdc48/VCP function

Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS

Relating sequence encoded information to form and function of intrinsically disordered proteins

Getting RNA and protein in phase

Structure-based design of a pathway-specific nuclear import inhibitor

In Vitro Reconstitution of a Cellular Phase-Transition Process that Involves the mRNA Decapping Machinery

Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex.

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