Sequestration of a β-hairpin for control of α-synuclein aggregation - Wikidata - wikimedia - TriplyDB

Sequestration of a β-hairpin for control of α-synuclein aggregation

Sequestration of a β-hairpin for control of α-synuclein aggregation

http://www.wikidata.org/entity/Q27689470

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Unveiling transient protein-protein interactions that modulate inhibition of alpha-synuclein aggregation by beta-synuclein, a pre-synaptic protein that co-localizes with alpha-synuclein.Flow-cytometric screening of aggregation-inhibitors using a fluorescence-assisted intracellular method.Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.Quantitative thermophoretic study of disease-related protein aggregates X-ray Crystallographic Structure of Oligomers Formed by a Toxic β-Hairpin Derived from α-Synuclein: Trimers and Higher-Order Oligomers.Modulating the Amyloidogenesis of α-Synuclein Coupling of the non-amyloid-component (NAC) domain and the KTK(E/Q)GV repeats stabilize the α-synuclein fibrils.β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor A β-hairpin-binding protein for three different disease-related amyloidogenic proteins.Structured States of Disordered Proteins from Genomic Sequences Alternative conformations of the Tau repeat domain in complex with an engineered binding protein.Binding Interactions of Agents That Alter α-Synuclein Aggregation.Impact of subunit linkages in an engineered homodimeric binding protein to α-synuclein.A Hexamer of a Peptide Derived from Aβ16-36.Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T.Effects of different force fields on the structural character of α synuclein β-hairpin peptide (35-56) in aqueous environment.CONAN: A Tool to Decode Dynamical Information from Molecular Interaction Maps.Elucidating the Structures of Amyloid Oligomers with Macrocyclic β-Hairpin Peptides: Insights into Alzheimer's Disease and Other Amyloid Diseases.Contact between the β1 and β2 Segments of α-Synuclein that Inhibits Amyloid Formation.X-ray Crystallographic Structure of a Compact Dodecamer from a Peptide Derived from Aβ16-36.Targeting Amyloid Aggregation: An Overview of Strategies and Mechanisms Elucidating the multi-targeted anti-amyloid activity and enhanced islet amyloid polypeptide binding of -wrapins

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Sequestration of a β-hairpin for control of α-synuclein aggregation

http://www.wikidata.org/entity/Q27689470

description

2014 nî lūn-bûn

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2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2014 թվականի ապրիլին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

@zh-hant

2014年論文

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2014年論文

@zh-mo

2014年論文

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2014年论文

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name

Sequestration of a β-hairpin for control of α-synuclein aggregation

@ast

Sequestration of a β-hairpin for control of α-synuclein aggregation

@en

Sequestration of a β-hairpin for control of α-synuclein aggregation

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type

label

Sequestration of a β-hairpin for control of α-synuclein aggregation

@ast

Sequestration of a β-hairpin for control of α-synuclein aggregation

@en

Sequestration of a β-hairpin for control of α-synuclein aggregation

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prefLabel

Sequestration of a β-hairpin for control of α-synuclein aggregation

@ast

Sequestration of a β-hairpin for control of α-synuclein aggregation

@en

Sequestration of a β-hairpin for control of α-synuclein aggregation

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Angewandte Chemie International Edition

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Sequestration of a β-hairpin for control of α-synuclein aggregation

@en

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Aziz Gauhar

http://www.w3.org/2001/XMLSchema#string

Ewa A Mirecka

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Hamed Shaykhalishahi

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Şerife Akgül

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P2860

Stabilization of a -hairpin in monomeric Alzheimer's amyloid- peptide inhibits amyloid formation

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Selection and characterization of Affibody ligands binding to Alzheimer amyloid beta peptides.

Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein

Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.

Induced fit, conformational selection and independent dynamic segments: an extended view of binding events

Investigation of alpha-synuclein fibril structure by site-directed spin labeling.

In vivo demonstration that alpha-synuclein oligomers are toxic.

Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein.

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4227-30

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scholarly article

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10.1002/ANIE.201309001

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16

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53

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Dieter Willbold

Matthias Stoldt

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2014-04-14T00:00:00Z

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260755106

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24623599

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