Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils - Test2 - elhamkhani - TriplyDB

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

http://www.wikidata.org/entity/Q27652925

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Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease Neurodegenerative diseases: expanding the prion concept Alzheimer's disease--a panorama glimpse The relationship between amyloid structure and cytotoxicity Development and application of STEM for the biological sciences Structural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic Pathways Molecular mechanisms for protein-encoded inheritance High-Resolution Solid-State NMR Structure of a 17.6 kDa Protein Minimalist design of water-soluble cross-beta architecture.X-ray Crystallographic Structure of an Artificial β-Sheet Dimer β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages Characteristics of Amyloid-Related Oligomers Revealed by Crystal Structures of Macrocyclic β-Sheet Mimics Towards a Pharmacophore for Amyloid Molecular basis of -amyloid oligomer recognition with a conformational antibody fragment Molecular basis for amyloid- polymorphism Antiparallel -sheet architecture in Iowa-mutant -amyloid fibrils Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue Molecular Basis of Substrate Recognition and Degradation by Human Presequence Protease A Fibril-Like Assembly of Oligomers of a Peptide Derived from β-Amyloid Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance Measurement of amyloid formation by turbidity assay-seeing through the cloud Molecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network Xanthene food dye, as a modulator of Alzheimer's disease amyloid-beta peptide aggregation and the associated impaired neuronal cell function.A multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35 Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity 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 Fibrils of Truncated Pyroglutamyl-Modified Aβ Peptide Exhibit a Similar Structure as Wildtype Mature Aβ Fibrils Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity The Japanese Mutant Aβ (ΔE22-Aβ1−39) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence: Seeding of Wild-Type Aβ1−40into Atypical Fibrils by ΔE22-Aβ1−39 Solid-state NMR structure determination from diagonal-compensated, sparsely nonuniform-sampled 4D proton-proton restraints.An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Monoclonal antibodies against Aβ42 fibrils distinguish multiple aggregation state polymorphisms in vitro and in Alzheimer disease brain.β-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Effects of surface interactions on peptide aggregate morphology.Stability tests on known and misfolded structures with discrete and all atom molecular dynamics simulations.Models of membrane-bound Alzheimer's Abeta peptide assemblies Beta-barrel models of soluble amyloid beta oligomers and annular protofibrils.

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P2860

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

http://www.wikidata.org/entity/Q27652925

description

2008 nî lūn-bûn

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2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

@ast

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

@en

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

@nl

type

label

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

@ast

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

@en

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

@nl

prefLabel

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

@ast

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

@en

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

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

P1476

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

@en

P2093

Anant K Paravastu

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

Richard D Leapman

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

Wai-Ming Yau

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

P2860

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

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

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

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

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Protein misfolding, functional amyloid, and human disease

Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host

Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.

Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils

Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

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Alzheimer's disease

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