Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. - Wikidata - wikimedia - TriplyDB

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.

http://www.wikidata.org/entity/Q37278078

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Versatile Structures of α-Synuclein Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils More than a Rumor Spreads in Parkinson's Disease Structural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet Core Structural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core.Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.Site-Specific Fluorescence Polarization for Studying the Disaggregation of α-Synuclein Fibrils by Small Molecules.Water Distribution, Dynamics, and Interactions with Alzheimer's β-Amyloid Fibrils Investigated by Solid-State NMR.Elucidating the structure of an infectious protein.Zinc-binding structure of a catalytic amyloid from solid-state NMR.A small-angle X-ray scattering study of alpha-synuclein from human red blood cells Cross-talk between amyloidogenic proteins in type-2 diabetes and Parkinson's disease.The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction.The Synucleinopathies: Twenty Years On.Not All β-Sheets Are the Same: Amyloid Infrared Spectra, Transition Dipole Strengths, and Couplings Investigated by 2D IR Spectroscopy.Novel conformation-selective alpha-synuclein antibodies raised against different in vitro fibril forms show distinct patterns of Lewy pathology in Parkinson's disease.Potential Pathways of Abnormal Tau and α-Synuclein Dissemination in Sporadic Alzheimer's and Parkinson's Diseases.The activities of amyloids from a structural perspective.Impulse control disorder, lysosomal malfunction and ATP13A2 insufficiency in Parkinsonism.Structural Biology of PrP Prions.Alpha-synuclein and iron: two keys unlocking Parkinson's disease.Designer protein disaggregases to counter neurodegenerative disease.New NMR tools for protein structure and function: Spin tags for dynamic nuclear polarization solid state NMR.Implications of peptide assemblies in amyloid diseases.MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins.Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid Fibrils Monomer-dependent secondary nucleation in amyloid formation.Cryo-EM structures of tau filaments from Alzheimer's disease.Mapping of Surface-Exposed Epitopes of In Vitro and In Vivo Aggregated Species of Alpha-Synuclein.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Structural Ensembles of Membrane-bound α-Synuclein Reveal the Molecular Determinants of Synaptic Vesicle Affinity.Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy.Getting in charge of β-synuclein fibrillation.A pH-dependent switch promotes β-synuclein fibril formation via glutamate residues.Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini.Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy.The involvement of dityrosine crosslinking in α-synuclein assembly and deposition in Lewy Bodies in Parkinson's disease.Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth.

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Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.

http://www.wikidata.org/entity/Q37278078

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 28 March 2016

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.

@en

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.

@nl

type

label

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.

@en

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.

@nl

prefLabel

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.

@en

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.

@nl

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Nature Structural & Molecular Biology

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Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

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Alexander M Barclay

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Amy Kendall

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Chad M Rienstra

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Charles D Schwieters

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Deborah A Berthold

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Dustin J Covell

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Gemma Comellas

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Gerald Stubbs

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Jae K Kim

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Joseph M Courtney

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P2860

MolProbity: all-atom structure validation for macromolecular crystallography

Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein

Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core

Dipole tensor-based atomic-resolution structure determination of a nanocrystalline protein by solid-state NMR

Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy

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

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

Protein production by auto-induction in high density shaking cultures

Alpha-synuclein in Lewy bodies

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409-415

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scholarly article

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10.1038/NSMB.3194

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5

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23

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Andrew J Nieuwkoop

William Nicholas Wan

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2016-03-28T00:00:00Z

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27018801

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