Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation - Wikidata - wikimedia - TriplyDB

Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation

Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation

http://www.wikidata.org/entity/Q34279026

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Mapping out the multistage fibrillation of glucagon Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation Mechanistic insight into the relationship between N-terminal acetylation of α-synuclein and fibril formation rates by NMR and fluorescence Structural Analysis and Aggregation Propensity of Pyroglutamate Aβ(3-40) in Aqueous Trifluoroethanol Aqueous, Unfolded OmpA Forms Amyloid-Like Fibrils upon Self-Association.Biophysics of α-synuclein membrane interactions.Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions.Amyloid triangles, squares, and loops of apolipoprotein C-III.The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils.Coarse-grained model for colloidal protein interactions, B(22), and protein cluster formation.Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of α-synuclein, and enhances its secretion and nuclear localization in cells.Transmission electron microscopy characterization of fluorescently labelled amyloid β 1-40 and α-synuclein aggregates Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer Amyloid fibrillation of insulin under water-limited conditions Alpha-synuclein function and dysfunction on cellular membranes.Regulation and aggregation of intrinsically disordered peptides Cytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptide Self-Assembly of Aβ40, Aβ42 and Aβ43 Peptides in Aqueous Mixtures of Fluorinated Alcohols.A desolvation model for trifluoroethanol-induced aggregation of enhanced green fluorescent protein.Highly neurotoxic monomeric α-helical prion protein.Aggregation of α-synuclein is kinetically controlled by intramolecular diffusion.Curcumin prevents aggregation in α-synuclein by increasing reconfiguration rate.Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.Identification of minimally interacting modules in an intrinsically disordered protein.Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants Pyroglutamate-Modified Amyloid-β(3-42) Shows α-Helical Intermediates before Amyloid Formation.Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments.Interplay between desolvation and secondary structure in mediating cosolvent and temperature induced alpha-synuclein aggregation Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granules Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril Formation Exposure to bacterial endotoxin generates a distinct strain of α-synuclein fibril.N-terminal acetylation stabilizes N-terminal helicity in lipid- and micelle-bound α-synuclein and increases its affinity for physiological membranes.Role of α-synuclein penetration into the membrane in the mechanisms of oligomer pore formation.Insight into α-synuclein plasticity and misfolding from differential micelle binding.Shedding light on protein folding landscapes by single-molecule fluorescence.Folding and misfolding of alpha-synuclein on membranes.Macroautophagy and the proteasome are differently involved in the degradation of alpha-synuclein wild type and mutated A30P in an in vitro inducible model (PC12/TetOn).

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Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation

http://www.wikidata.org/entity/Q34279026

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2010 nî lūn-bûn

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2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2010年の論文

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Identification of a helical in ...... ed alpha-synuclein aggregation

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Identification of a helical in ...... ed alpha-synuclein aggregation

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Identification of a helical in ...... ed alpha-synuclein aggregation

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Identification of a helical in ...... ed alpha-synuclein aggregation

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

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Identification of a helical in ...... ed alpha-synuclein aggregation

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P2093

Carla C Rospigliosi

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David Eliezer

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Trudy F Ramlall

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Valerie L Anderson

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Watt W Webb

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P2860

Parkinson's disease: from monogenic forms to genetic susceptibility factors

Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease

Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes

Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations

A broken alpha -helix in folded alpha -Synuclein.

Structure and dynamics of micelle-bound human alpha-synuclein.

Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein.

Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy

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.

Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation

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