Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation. - Wikidata - awgldk - TriplyDB

Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation.

Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation.

http://www.wikidata.org/entity/Q34602533

about

The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity Mapping out the multistage fibrillation of glucagon The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes Function and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescence A Nanobody Binding to Non-Amyloidogenic Regions of the Protein Human Lysozyme Enhances Partial Unfolding but Inhibits Amyloid Fibril Formation Synaptopathies: synaptic dysfunction in neurological disorders - A review from students to students The phosphorylation of α-synuclein: development and implication for the mechanism and therapy of the Parkinson's disease MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.Biophysics of α-synuclein membrane interactions.Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing α-synuclein oligomeric species toxicity Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction.Wildtype and A30P mutant alpha-synuclein form different fibril structures.α-Synuclein oligomers induced by docosahexaenoic acid affect membrane integrity.Structural transitions and interactions in the early stages of human glucagon amyloid fibrillation Mutant huntingtin, abnormal mitochondrial dynamics, defective axonal transport of mitochondria, and selective synaptic degeneration in Huntington's disease Mechanisms of protein oligomerization: inhibitor of functional amyloids templates α-synuclein fibrillation.Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells.Native chemical ligation of thioamide-containing peptides: development and application to the synthesis of labeled α-synuclein for misfolding studies Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants The conformational ensembles of α-synuclein and tau: combining single-molecule FRET and simulations.Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy.On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanisms A small-angle X-ray scattering study of alpha-synuclein from human red blood cells The interplay between lipids and dopamine on α-synuclein oligomerization and membrane binding.Role of α-synuclein penetration into the membrane in the mechanisms of oligomer pore formation.The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction.Aggregation of amyloids in a cellular context: modelling and experiment.Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering.Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery.α-Synuclein and neuronal cell death.α-Synuclein oligomers: an amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions.Misfolding of amyloidogenic proteins and their interactions with membranes.The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.Impaired intracellular trafficking defines early Parkinson's disease Investigating increasingly complex macromolecular systems with small-angle X-ray scattering.On the lag phase in amyloid fibril formation.Human cystatin C monomer, dimer, oligomer, and amyloid structures are related to health and disease.How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro.Considerably Unfolded Transthyretin Monomers Preceed and Exchange with Dynamically Structured Amyloid Protofibrils.

P2860

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P2860

Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation.

http://www.wikidata.org/entity/Q34602533

description

2011 nî lūn-bûn

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2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Low-resolution structure of a ...... cumulates during fibrillation.

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Low-resolution structure of a ...... cumulates during fibrillation.

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Low-resolution structure of a ...... cumulates during fibrillation.

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Low-resolution structure of a ...... cumulates during fibrillation.

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Low-resolution structure of a ...... cumulates during fibrillation.

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Low-resolution structure of a ...... cumulates during fibrillation.

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Low-resolution structure of a ...... cumulates during fibrillation.

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Low-resolution structure of a ...... cumulates during fibrillation.

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Low-resolution structure of a ...... cumulates during fibrillation.

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P1433

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PNAS.1013225108

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Low-resolution structure of a ...... cumulates during fibrillation.

@en

P2093

Lise Giehm

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P2860

Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing

A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils

Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct.

Granular assembly of alpha-synuclein leading to the accelerated amyloid fibril formation with shear stress.

A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy.

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers.

Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy.

Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease.

Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease.

Methionine oxidation, alpha-synuclein and Parkinson's disease.

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3246-3251

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scholarly article

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10.1073/PNAS.1013225108

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8

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108

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Bente Vestergaard

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2011-02-07T00:00:00Z

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49817104

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21300904

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3044375

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