Physical and structural basis for polymorphism in amyloid fibrils - Wikidata - awgldk - TriplyDB

Physical and structural basis for polymorphism in amyloid fibrils

Physical and structural basis for polymorphism in amyloid fibrils

http://www.wikidata.org/entity/Q34559641

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Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance Measurement of amyloid formation by turbidity assay-seeing through the cloud 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 Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.High-speed atomic force microscopy reveals structural dynamics of amyloid β1-42 aggregates.Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Stability of Iowa mutant and wild type Aβ-peptide aggregates Amyloid polymorphism: structural basis and neurobiological relevance.On the lack of polymorphism in Aβ-peptide aggregates derived from patient brains pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils.N-terminal lipid conjugation of amyloid β(1-40) leads to the formation of highly ordered N-terminally extended fibrils.A novel pathway for amyloids self-assembly in aggregates at nanomolar concentration mediated by the interaction with surfaces.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Zinc-binding structure of a catalytic amyloid from solid-state NMR.Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core What amyloid ligands can tell us about molecular polymorphism and disease.Not All β-Sheets Are the Same: Amyloid Infrared Spectra, Transition Dipole Strengths, and Couplings Investigated by 2D IR Spectroscopy.Chiral recognition in amyloid fiber growth.Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: insights from AFM experiments and computational analyses.The activities of amyloids from a structural perspective.Modulation of amyloid assembly by glycosaminoglycans: from mechanism to biological significance.Nanoscale Structure and Spectroscopic Probing of Aβ1-40 Fibril Bundle Formation Mapping the Broad Structural and Mechanical Properties of Amyloid Fibrils.RepA-WH1 prionoid: Clues from bacteria on factors governing phase transitions in amyloidogenesis.Successive Stages of Amyloid-β Self-Assembly Characterized by Solid-State Nuclear Magnetic Resonance with Dynamic Nuclear Polarization.Polymorphism of amyloid-like fibrils can be defined by the concentration of seeds.Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid Fibrils 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.Nucleation of polymorphic amyloid fibrils.Reduced Lipid Bilayer Thickness Regulates the Aggregation and Cytotoxicity of Amyloid-β.Aggregate Size-Dependence of Amyloid Adsorption onto Charged Interfaces.Recent progress on understanding the mechanisms of amyloid nucleation.NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Toward a Soluble Model System for the Amyloid State.Amyloidogenesis of Tau protein.Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T.

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Physical and structural basis for polymorphism in amyloid fibrils

http://www.wikidata.org/entity/Q34559641

description

2014 nî lūn-bûn

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2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2014 թվականի սեպտեմբերին 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

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Physical and structural basis for polymorphism in amyloid fibrils

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Physical and structural basis for polymorphism in amyloid fibrils

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Physical and structural basis for polymorphism in amyloid fibrils

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type

label

Physical and structural basis for polymorphism in amyloid fibrils

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Physical and structural basis for polymorphism in amyloid fibrils

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Physical and structural basis for polymorphism in amyloid fibrils

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prefLabel

Physical and structural basis for polymorphism in amyloid fibrils

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Physical and structural basis for polymorphism in amyloid fibrils

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Physical and structural basis for polymorphism in amyloid fibrils

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Protein Science

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Physical and structural basis for polymorphism in amyloid fibrils

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P2860

Functional amyloid formation within mammalian tissue.

The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis

Structure of the cross-beta spine of amyloid-like fibrils

Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils

Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure

Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure

High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy

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

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1528-1539

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scholarly article

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10.1002/PRO.2544

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11

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23

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2014-09-13T00:00:00Z

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25179159

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4241104

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