Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.
about
Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectinAmyloid formation in light chain amyloidosisCuminaldehyde as the Major Component of Cuminum cyminum, a Natural Aldehyde with Inhibitory Effect on Alpha-Synuclein Fibrillation and CytotoxicitySalts enhance both protein stability and amyloid formation of an immunoglobulin light chainRole 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 protofibrilsInsight 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 cellsAtomic force fluorescence microscopy in the characterization of amyloid fibril assembly and oligomeric intermediatesAnnular structures as intermediates in fibril formation of Alzheimer Abeta17-42Light 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 stackingEffect 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.
P2860
Q21202837-1475740B-66E8-42E9-8D57-8AF68B39744EQ27022257-745C7960-2ED2-4C26-845C-1CDABD70322EQ28267154-FCC98AD2-38E1-4C14-8BE1-74128D151C4DQ30368702-8565F2BB-E1DD-408C-B2C8-2DEEAFD449F3Q30478679-7EDDE2D7-9899-4F0E-83C4-02DD6DD28C9DQ33647141-B784C4CE-4FEC-4842-8B52-314A42AF230EQ33916275-AF1A441D-F8A9-48B3-B6F1-416BB0B81533Q33936902-B9C8BA01-E5D6-494C-90F6-A11E0A535B42Q34416296-20C93645-B6F7-4A06-8C18-36D7F1E304BBQ34990429-18C380B0-05A0-453B-A4F6-75E288EB7A87Q35966921-ECF3F929-2D62-40FB-B0C8-2589E111520EQ37130014-98CA6DB6-A146-42F7-AB7A-2E262F573626Q37206082-74EB9844-11D1-48F0-96E4-372843C84CB2Q37426694-3CEFE6DB-5DF1-42D8-96BA-B3A2A93687F2Q37502618-F0414E0A-90CA-4FFB-A197-606BA6EA6559Q38223686-919E68AC-8242-406C-B90A-5E50BA89CE30Q38844934-D5322B76-19CF-4566-867D-22B6CFA75B57Q38851025-4806ED7C-27A5-446A-B7F8-8EFE8858F6A3Q39324732-01A439D4-B747-4601-B3E5-DBA45A8124A1Q40307309-2D301EED-4E1E-46AE-9C99-F9DA359D4F73Q41763155-F59E93B2-5722-4F5F-A9CE-FD19F1BA5271Q41985249-B0423520-89DD-4E57-AF96-78B2038677C8Q45301226-061E71EF-FE14-41E0-86B2-5E49FE71DDB2Q48709319-CECDCAEA-D196-4D72-B473-0A4A21169F4CQ51812016-D7A0D8B8-DC6A-4A12-BA9F-8B775591E0A6
P2860
Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
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
P2093
P2860
P356
P1476
Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy.
@en
P2093
Anthony L Fink
Feimeng Zhou
Sue A Carter
P2860
P304
24452-24459
P356
10.1074/JBC.M400004200
P407
P577
2004-03-31T00:00:00Z