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

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

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

http://www.wikidata.org/entity/Q24631702

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The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway Characterizing affinity epitopes between prion protein and β-amyloid using an epitope mapping immunoassay Interaction between soluble Aβ-(1-40) monomer and Aβ-(1-42) fibrils probed by paramagnetic relaxation enhancement Expression and purification of 15N- and 13C-isotope labeled 40-residue human Alzheimer's β-amyloid peptide for NMR-based structural analysis Amyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta pores The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy Friends or Foes: Matrix Metalloproteinases and Their Multifaceted Roles in Neurodegenerative Diseases Vitamin D and Alzheimer's Disease: Neurocognition to Therapeutics Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeutics Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease Dye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (aβ) self-assembly Dietary DHA supplementation in an APP/PS1 transgenic rat model of AD reduces behavioral and Aβ pathology and modulates Aβ oligomerization Structural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic Pathways Mapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerization Characteristics of Amyloid-Related Oligomers Revealed by Crystal Structures of Macrocyclic β-Sheet Mimics Molecular basis of -amyloid oligomer recognition with a conformational antibody fragment Out-of-register -sheets suggest a pathway to toxic amyloid aggregates Antiparallel -sheet architecture in Iowa-mutant -amyloid fibrils Atomic View of a Toxic Amyloid Small Oligomer Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue A Fibril-Like Assembly of Oligomers of a Peptide Derived from β-Amyloid Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance Copper chelator induced efficient episodic memory recovery in a non-transgenic Alzheimer's mouse model Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide Fibrils of Truncated Pyroglutamyl-Modified Aβ Peptide Exhibit a Similar Structure as Wildtype Mature Aβ Fibrils Bridging Type 2 Diabetes and Alzheimer's Disease: Assembling the Puzzle Pieces in the Quest for the Molecules With Therapeutic and Preventive Potential Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formation An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Structural basis of β-amyloid-dependent synaptic dysfunctions.Recent progress in understanding Alzheimer's β-amyloid structures.Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers Comparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin.Structural Mechanism of the Interaction of Alzheimer Disease Aβ Fibrils with the Non-steroidal Anti-inflammatory Drug (NSAID) Sulindac Sulfide Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.Revealing protein structures in solid-phase peptide synthesis by 13C solid-state NMR: evidence of excessive misfolding for Alzheimer's β.Techniques for Monitoring Protein Misfolding and Aggregation in Vitro and in Living Cells Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFM

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

http://www.wikidata.org/entity/Q24631702

description

2010 nî lūn-bûn

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2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2010 թվականի մայիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

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

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

@en

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

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type

label

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

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

@en

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

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prefLabel

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

@ast

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

@en

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

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Nature Structural & Molecular Biology

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

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Darryl Aucoin

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James I Elliott

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Judianne Davis

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Mahiuddin Ahmed

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Saburo Aimoto

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Shivani Ahuja

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Steven O Smith

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Takeshi Sato

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

William E Van Nostrand

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

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beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease

Amyloid plaque core protein in Alzheimer disease and Down syndrome

Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Soluble amyloid beta peptide concentration as a predictor of synaptic change in Alzheimer's disease

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

The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

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

Globular amyloid beta-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease

Common mechanisms of amyloid oligomer pathogenesis in degenerative disease

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

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561-7

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1293881

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10.1038/NSMB.1799

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43100108

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1047928194

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20383142

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structural biology

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2922021

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