Radiating amyloid fibril formation on the surface of lipid membranes through unit-assembly of oligomeric species of α-synuclein.
about
A flash in the pan: dissecting dynamic amyloid intermediates using fluorescenceRepA-WH1, the agent of an amyloid proteinopathy in bacteria, builds oligomeric pores through lipid vesicles.Seeking a mechanism for the toxicity of oligomeric α-synucleinβ2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHEffects of impaired membrane interactions on α-synuclein aggregation and neurotoxicityAtomic Force Microscopy Characterization of Protein Fibrils Formed by the Amyloidogenic Region of the Bacterial Protein MinE on Mica and a Supported Lipid Bilayer.Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.Membrane remodeling by α-synuclein and effects on amyloid formation.Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicityMolecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.EGCG-mediated Protection of the Membrane Disruption and Cytotoxicity Caused by the 'Active Oligomer' of α-Synuclein.Molecular inscription of environmental information into protein suprastructures: temperature effects on unit assembly of α-synuclein oligomers into polymorphic amyloid fibrils.Morphological Evaluation of Meta-stable Oligomers of α-Synuclein with Small-Angle Neutron Scattering
P2860
Q26997922-323EB2B9-4F73-476F-A64C-08A38397F709Q27332087-BD6AE79E-47CF-4514-AD6D-B66B22DD7A28Q28080551-A5F4AF96-5F69-4A4C-A5A7-655A26B57ABBQ28541669-522A1699-3154-4EE9-A830-546579BA05FAQ35691076-F0A663D7-2364-469E-8945-F4EF58A7DCFBQ35839930-DE9A33DC-FDE4-4994-952B-1E0C7E4B8BFCQ35978258-95527CA4-B7DF-4170-BFCF-BC62D1202C7DQ37383252-33630F90-D673-469A-AB93-C0CC13584A8EQ37576386-8543B983-E9FB-4474-84ED-B3C4F4CE786EQ39384630-745C2704-CED5-4E36-BD6B-D192B24DC923Q47147437-4950BB49-AC5F-4A52-86A8-091FCC678DB2Q53356650-80E535F2-6AA7-498D-9086-BAEF9EA0CA38Q58700494-06C60C61-B3D6-46AB-8626-645256A2A642
P2860
Radiating amyloid fibril formation on the surface of lipid membranes through unit-assembly of oligomeric species of α-synuclein.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Radiating amyloid fibril forma ...... omeric species of α-synuclein.
@ast
Radiating amyloid fibril forma ...... omeric species of α-synuclein.
@en
type
label
Radiating amyloid fibril forma ...... omeric species of α-synuclein.
@ast
Radiating amyloid fibril forma ...... omeric species of α-synuclein.
@en
prefLabel
Radiating amyloid fibril forma ...... omeric species of α-synuclein.
@ast
Radiating amyloid fibril forma ...... omeric species of α-synuclein.
@en
P2093
P2860
P1433
P1476
Radiating amyloid fibril forma ...... omeric species of α-synuclein.
@en
P2093
Chul-Suk Hong
Daekyun Lee
Jee-Eun Yang
Seung R Paik
Seunho Jung
Soonkoo Lee
Taeghwan Hyeon
Yong Il Park
P2860
P304
P356
10.1371/JOURNAL.PONE.0047580
P407
P50
P577
2012-10-15T00:00:00Z