Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity. - Wikidata - wikimedia - TriplyDB

Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity.

Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity.

http://www.wikidata.org/entity/Q36098093

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Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease Exploring the accessible conformations of N-terminal acetylated α-synuclein Structural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic Pathways Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones Intrahippocampal administration of a domain antibody that binds aggregated amyloid-β reverses cognitive deficits produced by diet-induced obesity.Ortho-methylated 3-hydroxypyridines hinder hen egg-white lysozyme fibrillogenesis.The C-terminal threonine of Aβ43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils.Effect of metals on kinetic pathways of amyloid-β aggregation Transthyretin-derived peptides as β-amyloid inhibitors.Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.Alzheimer's disease: which type of amyloid-preventing drug agents to employ?Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assembly.The elusive nature and diagnostics of misfolded Aβ oligomers.Strong inhibition of beta-amyloid peptide aggregation realized by two-steps evolved peptides.Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis.Capillary electrophoresis for the analysis of the effect of sample preparation on early stages of Aβ1-40 aggregation.Amyloid polymorphism: structural basis and neurobiological relevance.High-resolution NMR characterization of low abundance oligomers of amyloid-β without purification Characterizing methyl-bearing side chain contacts and dynamics mediating amyloid β protofibril interactions using ¹³C(methyl)-DEST and lifetime line broadening.Soluble prion protein inhibits amyloid-β (Aβ) fibrillization and toxicity.Molecular plasticity regulates oligomerization and cytotoxicity of the multipeptide-length amyloid-β peptide pool Rational design of potent domain antibody inhibitors of amyloid fibril assembly.Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2.The neurodegeneration in Alzheimer disease and the prion protein Clusterin Binds to Aβ1-42 Oligomers with High Affinity and Interferes with Peptide Aggregation by Inhibiting Primary and Secondary Nucleation.Conformational Dynamics of Specific Aβ Oligomers Govern Their Ability To Replicate and Induce Neuronal Apoptosis Amyloid-β peptide-induced extracellular S100A9 depletion is associated with decrease of antimicrobial peptide activity in human THP-1 monocytes.The Anti-Prion Antibody 15B3 Detects Toxic Amyloid-β Oligomers Polymorphism of fibrillar structures depending on the size of assembled Aβ17-42 peptides.Oligomeropathies and pathogenesis of Alzheimer and Parkinson's diseases.Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.Biochemical and Electrophysiological Modification of Amyloid Transthyretin on Cardiomyocytes.Modeling the Aggregation Propensity and Toxicity of Amyloid-β Variants.Successive Stages of Amyloid-β Self-Assembly Characterized by Solid-State Nuclear Magnetic Resonance with Dynamic Nuclear Polarization.Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases.Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.

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Conformational differences between two amyloid β oligomers of similar size and dissimilar toxicity.

http://www.wikidata.org/entity/Q36098093

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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name

Conformational differences bet ...... size and dissimilar toxicity.

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Conformational differences bet ...... size and dissimilar toxicity.

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Conformational differences bet ...... size and dissimilar toxicity.

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Conformational differences bet ...... size and dissimilar toxicity.

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Conformational differences bet ...... size and dissimilar toxicity.

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Conformational differences bet ...... size and dissimilar toxicity.

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Journal of Biological Chemistry

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Conformational differences bet ...... size and dissimilar toxicity.

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Ali Reza A Ladiwala

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Darryl S Aucoin

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Jeffrey Litt

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Judianne Davis

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Peter M Tessier

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Ravi S Kane

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Steven O Smith

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Swarnim Ranjan

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William E Van Nostrand

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P2860

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

Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo

A specific amyloid-beta protein assembly in the brain impairs memory

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

A beta oligomers - a decade of discovery

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

Role of aggregation conditions in structure, stability, and toxicity of intermediates in the Abeta fibril formation pathway

Structural classification of toxic amyloid oligomers

Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils.

Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells.

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