Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy. - Wikidata - wikimedia - TriplyDB

Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.

Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.

http://www.wikidata.org/entity/Q44824206

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Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectin Amyloid formation in light chain amyloidosis Cuminaldehyde as the Major Component of Cuminum cyminum, a Natural Aldehyde with Inhibitory Effect on Alpha-Synuclein Fibrillation and Cytotoxicity Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain Role of endocytic inhibitory drugs on internalization of amyloidogenic light chains by cardiac fibroblasts.Quantifying prefibrillar amyloids in vitro by using a "thioflavin-like" spectroscopic method.Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity.Polymorphic structures of Alzheimer's β-amyloid globulomers.Distinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrils Insight into amyloid structure using chemical probes.Detection of high-molecular-weight amyloid serum protein complexes using biological on-line tracer sedimentation.Tanshinones inhibit amyloid aggregation by amyloid-β peptide, disaggregate amyloid fibrils, and protect cultured cells Atomic force fluorescence microscopy in the characterization of amyloid fibril assembly and oligomeric intermediates Annular structures as intermediates in fibril formation of Alzheimer Abeta17-42 Light chain amyloidosis - current findings and future prospects.Misfolding of amyloidogenic proteins and their interactions with membranes.ThT 101: a primer on the use of thioflavin T to investigate amyloid formation.Viewing Extrinsic Proteotoxic Stress Through the Lens of Amyloid Cardiomyopathy.A kinetic model for beta-amyloid adsorption at the air/solution interface and its implication to the beta-amyloid aggregation process.Sampling the self-assembly pathways of KFFE hexamers.Aggregation pathways of the amyloid β(1-42) peptide depend on its colloidal stability and ordered β-sheet stacking Effect of dehydration on the aggregation kinetics of two amyloid peptides.Mutant huntingtin alters Tau phosphorylation and subcellular distribution.Hexafluoroisopropanol induces self-assembly of β-amyloid peptides into highly ordered nanostructures.Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core.

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P2860

Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.

http://www.wikidata.org/entity/Q44824206

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

2004年學術文章

@zh-hant

name

Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.

@en

Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.

@nl

type

label

Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.

@en

Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.

@nl

prefLabel

Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.

@en

Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.

@nl

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P1433

Journal of Biological Chemistry

P1476

Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.

@en

P2093

Anthony L Fink

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

Feimeng Zhou

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

Min Zhu

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

Shubo Han

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

Sue A Carter

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

P2860

alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

Review: history of the amyloid fibril

Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation

Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein

Monitoring biomolecular interactions by time-lapse atomic force microscopy.

Review: immunoglobulin light chain amyloidosis--the archetype of structural and pathogenic variability.

The channel hypothesis of Alzheimer's disease: current status.

A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy.

Light chains of human immunoglobulins.

Aggregation and neurotoxicity of alpha-synuclein and related peptides.

P304

24452-24459

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scholarly article

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10.1074/JBC.M400004200

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23

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279

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2004-03-31T00:00:00Z

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8643940

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15056656

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