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Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

http://www.wikidata.org/entity/Q34100591

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β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides Overview of Alzheimer's Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal Compounds 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 Towards a Pharmacophore for Amyloid Molecular basis of -amyloid oligomer recognition with a conformational antibody fragment High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C.X-ray Crystallographic Structures of Trimers and Higher-Order Oligomeric Assemblies of a Peptide Derived from Aβ 17–36 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 Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis Amyloid-β protofibrils: size, morphology and synaptotoxicity of an engineered mimic Large aggregates are the major soluble Aβ species in AD brain fractionated with density gradient ultracentrifugation Fibrils of Truncated Pyroglutamyl-Modified Aβ Peptide Exhibit a Similar Structure as Wildtype Mature Aβ Fibrils Recent progress in understanding Alzheimer's β-amyloid structures.Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers A safe, blood-brain barrier permeable triphenylmethane dye inhibits amyloid-β neurotoxicity by generating nontoxic aggregates Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFM Toxic fibrillar oligomers of amyloid-β have cross-β structure.Nano-assembly of amyloid β peptide: role of the hairpin fold.Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy.Amino acids with hydrogen-bonding side chains have an intrinsic tendency to sample various turn conformations in aqueous solution.Simultaneous changes of spatial memory and spine density after intrahippocampal administration of fibrillar aβ1-42 to the rat brain Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Fibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulations Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.A retrospective analysis of the Alzheimer's disease vaccine progress - The critical need for new development strategies.Comparative studies of disordered proteins with similar sequences: application to Aβ40 and Aβ42 Curcumin Binding to Beta Amyloid: A Computational Study.Two distinct amyloid beta-protein (Abeta) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses.Probing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopy Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Isolating toxic insulin amyloid reactive species that lack β-sheets and have wide pH stability Intracellular selection of peptide inhibitors that target disulphide-bridged Aβ42 oligomers The elusive nature and diagnostics of misfolded Aβ oligomers.A monoclonal antibody against synthetic Aβ dimer assemblies neutralizes brain-derived synaptic plasticity-disrupting Aβ.Role of key aromatic residues in the ligand-binding domain of alpha7 nicotinic receptors in the agonist action of beta-amyloid.Amyloid polymorphism: structural basis and neurobiological relevance.Antiparallel β-Sheet Structure within the C-Terminal Region of 42-Residue Alzheimer's Amyloid-β Peptides When They Form 150-kDa Oligomers.Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes.

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Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

http://www.wikidata.org/entity/Q34100591

description

2010 nî lūn-bûn

@nan

2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին 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

Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

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Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

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Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

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type

label

Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

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Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

@en

Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

@nl

prefLabel

Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

@ast

Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

@en

Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

@nl

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PNAS.1001740107

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

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Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineering

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P2093

Anders Sandberg

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

Bertil Macao

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Christopher M Dobson

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

Frida Ekholm-Petterson

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

Lars Lannfelt

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

Leila M Luheshi

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

Sofia Söllvander

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

Teresa Pereira de Barros

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

P2860

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

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

The Alzheimer's peptides Abeta40 and 42 adopt distinct conformations in water: a combined MD / NMR study

Stabilization of a -hairpin in monomeric Alzheimer's amyloid- peptide inhibits amyloid formation

Protein misfolding, functional amyloid, and human disease

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

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

Abeta oligomers induce neuronal oxidative stress through an N-methyl-D-aspartate receptor-dependent mechanism that is blocked by the Alzheimer drug memantine.

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins

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15595-15600

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10.1073/PNAS.1001740107

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35

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107

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Christofer Lendel

Tuomas P. J. Knowles

Anatoly Dubnovitsky

Henrik Biverstal

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2010-08-16T00:00:00Z

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45660013

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20713699

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Alzheimer's disease

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2932621

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