Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes. - Test2 - elhamkhani - TriplyDB

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

http://www.wikidata.org/entity/Q37583853

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Rosetta Stone for Amyloid Fibrils: The Key Role of Ring-Like Oligomers in Amyloidogenesis.The Exceptional Vulnerability of Humans to Alzheimer's Disease.A clinicopathological approach to the diagnosis of dementia.The spread of prion-like proteins by lysosomes and tunneling nanotubes: Implications for neurodegenerative diseases.Emulation with Organic Memristive Devices of Impairment of LTP Mechanism in Neurodegenerative Disease Pathology.The A2V mutation as a new tool for hindering Aβ aggregation: A neutron and x-ray diffraction study Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid Fibrils Aβ seeds and prions: How close the fit?Monomer-dependent secondary nucleation in amyloid formation.High-resolution NMR in the native state.Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients.Amyloid-β and tau complexity - towards improved biomarkers and targeted therapies.Studies for Improving a Rat Model of Alzheimer's Disease: Icv Administration of Well-Characterized β-Amyloid 1-42 Oligomers Induce Dysfunction in Spatial Memory.Why are Functional Amyloids Non-Toxic in Humans?Synthesis of Thiophene-Based Optical Ligands That Selectively Detect Tau Pathology in Alzheimer's Disease.Hydrogen bonds are a primary driving force for de novo protein folding."Carboranyl-cysteine"-Synthesis, Structure and Self-Assembly Behavior of a Novel α-Amino Acid.Structural heterogeneity and intersubject variability of Aβ in familial and sporadic Alzheimer's disease.Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.Mesoporous Silica and Organosilica Nanoparticles: Physical Chemistry, Biosafety, Delivery Strategies, and Biomedical Applications.Amyloid polymorphisms constitute distinct clouds of conformational variants in different etiological subtypes of Alzheimer's disease.Protein-Based Inheritance: Epigenetics beyond the Chromosome.Microsecond Timescale Protein Dynamics: a Combined Solid-State NMR Approach.Toward a Soluble Model System for the Amyloid State.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.β-Amyloid and the Pathomechanisms of Alzheimer's Disease: A Comprehensive View.Amyloid fibril polymorphism - a challenge for molecular imaging and therapy.Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla.Lysosomal enzyme tripeptidyl peptidase 1 destabilizes fibrillar Aβ by multiple endoproteolytic cleavages within the β-sheet domain.Fibril structure of amyloid-β(1-42) by cryo-electron microscopy.Comprehensive and Methodical: Diagnostic and Management Approaches to Rapidly Progressive Dementia.Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T.The CSF neurofilament light signature in rapidly progressive neurodegenerative dementias.Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.Dissecting the behaviour of β-amyloid peptide variants during oligomerization and fibrillation.A long-lived Aβ oligomer resistant to fibrillization.Stabilizing amyloid-β peptide by the N-terminus capture is capable of preventing and eliminating amyloid-β oligomers.Molecular subtypes of Alzheimer's disease.Evolvability of Amyloidogenic Proteins in Human Brain.Depletion of amyloid-β peptides from solution by sequestration within fibril-seeded hydrogels.

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Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

http://www.wikidata.org/entity/Q37583853

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 04 January 2017

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

@cs

name

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

@en

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

@nl

type

label

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

@en

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

@nl

prefLabel

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

@en

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

@nl

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Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes.

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John Collinge

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Jun-Xia Lu

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Wai-Ming Yau

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Wei Qiang

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P2860

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

Antiparallel -sheet architecture in Iowa-mutant -amyloid fibrils

Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

Modeling an in-register, parallel "iowa" aβ fibril structure using solid-state NMR data from labeled samples with rosetta

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

A general model of prion strains and their pathogenicity

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

Distinct α-synuclein strains differentially promote tau inclusions in neurons

Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity

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217-221

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scholarly article

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10.1038/NATURE20814

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28052060

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Alzheimer's disease

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5233555

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