On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanisms
about
Digested disorder: Quarterly intrinsic disorder digest (January/February/March, 2013).Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Acceleration of α-synuclein aggregation by exosomes.Direct Detection of α-Synuclein Dimerization Dynamics: Single-Molecule Fluorescence Analysis.A novel pathway for amyloids self-assembly in aggregates at nanomolar concentration mediated by the interaction with surfaces.Review: Spreading the word: precise animal models and validated methods are vital when evaluating prion-like behaviour of alpha-synuclein.Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers.The Impact of N-terminal Acetylation of α-Synuclein on Phospholipid Membrane Binding and Fibril Structure.Nanoscale Dynamics of Amyloid β-42 Oligomers As Revealed by High-Speed Atomic Force Microscopy.Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification.Factors affecting the physical stability (aggregation) of peptide therapeutics.Structural insights from lipid-bilayer nanodiscs link α-Synuclein membrane-binding modes to amyloid fibril formationSupercritical angle Raman microscopy: a surface-sensitive nanoscale technique without field enhancementSolid supported lipid bilayers from artificial and natural lipid mixtures – long-term stable, homogeneous and reproducible
P2860
Q22061724-55E1F96F-AFBE-47E0-AA86-F788614A1B3BQ26823798-9C0A605E-BB2D-469F-93BC-6262F8D191BEQ35048929-3859460B-293B-4A75-973A-8D4292ABE198Q35529960-68768313-9CD5-4564-9046-0A19C8155502Q36327854-3C1F044A-C435-4FA3-8E86-D76643C1515DQ38669105-82CED4D0-2614-451C-9A8F-487B676915CCQ41142736-9C512EBC-45B2-4321-A611-EC0AE3A073E4Q41549497-CCFEBB74-EDC2-4B5E-8A27-7120DCF4067BQ46024871-88CB2CBE-026D-4D52-A9B4-3461049B38E3Q46242764-402FB565-842D-4580-8A56-5A4FF121A8C4Q46259884-92404526-44F9-4A68-AE3B-D62698056A81Q55122147-0E409B8C-95DC-483C-9A32-65289C72D892Q57149569-FBECCE66-E9CE-478E-B018-73A682ABB8F2Q58819456-954838DA-59C9-4389-82B4-34F44AAA16CB
P2860
On-surface aggregation of α-synuclein at nanomolar concentrations results in two distinct growth mechanisms
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
On-surface aggregation of α-sy ...... two distinct growth mechanisms
@ast
On-surface aggregation of α-sy ...... two distinct growth mechanisms
@en
type
label
On-surface aggregation of α-sy ...... two distinct growth mechanisms
@ast
On-surface aggregation of α-sy ...... two distinct growth mechanisms
@en
prefLabel
On-surface aggregation of α-sy ...... two distinct growth mechanisms
@ast
On-surface aggregation of α-sy ...... two distinct growth mechanisms
@en
P2093
P2860
P356
P1476
On-surface aggregation of α-sy ...... two distinct growth mechanisms
@en
P2093
Dorinel Verdes
Ennio Liverani
Michael Rabe
Nicholas P Reynolds
Roland Riek
Stefan Seeger
P2860
P304
P356
10.1021/CN3001312
P577
2013-01-22T00:00:00Z