Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer. - Test2 - elhamkhani - TriplyDB

Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.

Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.

http://www.wikidata.org/entity/Q30157440

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Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks Amyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta pores Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus Microbial amyloids--functions and interactions within the host Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease Function and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescence 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 Crystal structure of a conformation-dependent rabbit IgG Fab specific for amyloid prefibrillar oligomers Neurotoxicity of prion peptides mimicking the central domain of the cellular prion protein Large aggregates are the major soluble Aβ species in AD brain fractionated with density gradient ultracentrifugation Amyloid oligomer neurotoxicity, calcium dysregulation, and lipid rafts Prion protein-mediated toxicity of amyloid-β oligomers requires lipid rafts and the transmembrane LRP1 Beta-barrel models of soluble amyloid beta oligomers and annular protofibrils.Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent.Amyloid Beta annular protofibrils in cell processes and synapses accumulate with aging and Alzheimer-associated genetic modification Atomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.Techniques for Monitoring Protein Misfolding and Aggregation in Vitro and in Living Cells Aggregation of Aß(25-35) on DOPC and DOPC/DHA bilayers: an atomic force microscopy study Two disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomer-induced membrane permeability.Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells.Brain amyloid-β oligomers in ageing and Alzheimer's disease.Effect of metals on kinetic pathways of amyloid-β aggregation Fibrillar oligomers nucleate the oligomerization of monomeric amyloid beta but do not seed fibril formation Polymorphic structures of Alzheimer's β-amyloid globulomers.Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.Structural determination of Abeta25-35 micelles by molecular dynamics simulations.A yeast toxic mutant of HET-s((218-289)) prion displays alternative intermediates of amyloidogenesis An equilibrium model for linear and closed-loop amyloid fibril formation.Effect of synthetic aβ peptide oligomers and fluorinated solvents on Kv1.3 channel properties and membrane conductance.Intracellular amyloid and the neuronal origin of Alzheimer neuritic plaques Distinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrils Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Multivariate analyses of amyloid-beta oligomer populations indicate a connection between pore formation and cytotoxicity The formation of tau pore-like structures is prevalent and cell specific: possible implications for the disease phenotypes.Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species.Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formation Membrane Incorporation, Channel Formation, and Disruption of Calcium Homeostasis by Alzheimer's β-Amyloid Protein.Amyloid-β annular protofibrils evade fibrillar fate in Alzheimer disease brain Isolation and characterization of antibody fragments selective for toxic oligomeric tau

P2860

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P2860

Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.

http://www.wikidata.org/entity/Q30157440

description

2008 nî lūn-bûn

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2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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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

Annular protofibrils are a str ...... inct type of amyloid oligomer.

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Annular protofibrils are a str ...... inct type of amyloid oligomer.

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type

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Annular protofibrils are a str ...... inct type of amyloid oligomer.

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Annular protofibrils are a str ...... inct type of amyloid oligomer.

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Annular protofibrils are a str ...... inct type of amyloid oligomer.

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Annular protofibrils are a str ...... inct type of amyloid oligomer.

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P1433

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P1433

Journal of Biological Chemistry

P1476

Annular protofibrils are a str ...... inct type of amyloid oligomer.

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P2093

Anna Pensalfini

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Charles Glabe

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

Elizabeth Head

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

Floyd Sarsoza

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

James Hall

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

Larry Margol

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

Rakez Kayed

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Yuri Sokolov

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P2860

Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice

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

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

A common fold mediates vertebrate defense and bacterial attack

Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum

Expression of normal sequence pathogenic proteins for neurodegenerative disease contributes to disease risk: 'permissive templating' as a general mechanism underlying neurodegeneration

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

P304

4230-4237

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10.1074/JBC.M808591200

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P433

7

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P478

284

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2008-12-18T00:00:00Z

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23679563

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19098006

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2640961

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