Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains. - Wikidata - awgldk - TriplyDB

Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains.

Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains.

http://www.wikidata.org/entity/Q47752760

about

Environment-transformable sequence-structure relationship: a general mechanism for proteotoxicity.Lysines in the RNA Polymerase II C-Terminal Domain Contribute to TAF15 Fibril Recruitment.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR.Pi-Pi contacts are an overlooked protein feature relevant to phase separation.FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions.It Pays To Be in Phase.Impact of membrane curvature on amyloid aggregation.Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS.Importance of Functional Loss of FUS in FTLD/ALS.Yeast as a Model to Unravel Mechanisms Behind FUS Toxicity in Amyotrophic Lateral Sclerosis.Matrin 3-dependent neurotoxicity is modified by nucleic acid binding and nucleocytoplasmic localization.Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains Structural characterization of the D290V mutation site in hnRNPA2 low-complexity-domain polymers New applications of solid-state NMR in structural biology Protein Phase Separation: A New Phase in Cell Biology Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation Liquid and Hydrogel Phases of PrP Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers Mutant UBQLN2 promotes toxicity by modulating intrinsic self-assembly Amyloid assembly and disassembly RNA-Binding Proteins in Amyotrophic Lateral Sclerosis The physiological and pathological biophysics of phase separation and gelation of RNA binding proteins in amyotrophic lateral sclerosis and fronto-temporal lobar degeneration The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization Phase transitioned nuclear Oskar promotes cell division of primordial germ cells

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P2860

Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains.

http://www.wikidata.org/entity/Q47752760

description

2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Structure of FUS Protein Fibri ...... ion of Low-Complexity Domains.

@en

Structure of FUS Protein Fibri ...... ion of Low-Complexity Domains.

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type

label

Structure of FUS Protein Fibri ...... ion of Low-Complexity Domains.

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Structure of FUS Protein Fibri ...... ion of Low-Complexity Domains.

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prefLabel

Structure of FUS Protein Fibri ...... ion of Low-Complexity Domains.

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Structure of FUS Protein Fibri ...... ion of Low-Complexity Domains.

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Structure of FUS Protein Fibri ...... ion of Low-Complexity Domains.

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Dylan T Murray

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Ivan Hung

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Kent R Thurber

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Masato Kato

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Steven L McKnight

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Yi Lin

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P2860

Intrinsically unstructured proteins and their functions

Nuclear speckles: a model for nuclear organelles

The 3D profile method for identifying fibril-forming segments of proteins

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy

Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

VMD: visual molecular dynamics

Scalable molecular dynamics with NAMD

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protein structure

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