Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts.
about
The toxicity of amyloid β oligomersOn the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesThe pathological roles of ganglioside metabolism in Alzheimer's disease: effects of gangliosides on neurogenesis.The role of calcium, lipid membranes and islet amyloid polypeptide in the onset of type 2 diabetes: innocent bystanders or partners in a crime?Membrane Incorporation, Channel Formation, and Disruption of Calcium Homeostasis by Alzheimer's β-Amyloid Protein.Short Peptides as Inhibitors of Amyloid AggregationAmyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces.Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspectiveProbing ion channel activity of human islet amyloid polypeptide (amylin).Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Molecular insights into cell toxicity of a novel familial amyloidogenic variant of β2-microglobulin.Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity.Clustering and internalization of toxic amylin oligomers in pancreatic cells require plasma membrane cholesterol.Partitioning and confinement of GM1 ganglioside induced by amyloid aggregates.Biochemical and Electrophysiological Modification of Amyloid Transthyretin on Cardiomyocytes.Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation.Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases.The Role of Cholesterol in Driving IAPP-Membrane Interactions.Change of dynamics of raft-model membrane induced by amyloid-β protein binding.Toxic HypF-N Oligomers Selectively Bind the Plasma Membrane to Impair Cell Adhesion Capability.Oleuropein aglycone stabilizes the monomeric α-synuclein and favours the growth of non-toxic aggregates.Azurin interaction with the lipid raft components ganglioside GM-1 and caveolin-1 increases membrane fluidity and sensitivity to anti-cancer drugs
P2860
Q24631757-8C5D2974-EB58-4EB9-8052-6A27AE729228Q27022467-EC92BD81-09CB-424C-B879-7A66CE7DC137Q34512696-B69173B2-7077-4899-B629-7417C17083B0Q34718166-7417086A-DF36-4744-95C7-E8263B655871Q34923956-C915445F-1C28-42D2-9905-5C73DCAF577FQ35127036-1B96F521-8F43-4FD6-B087-456C8E67CED5Q35139664-EBA0F6F7-E4A6-418C-807E-5BCFF5809E4EQ35737643-2B793D37-0FFF-4D8A-9BD6-A98548F34653Q36269079-C8739602-5F07-4FB7-828D-A9D5B1863332Q36299680-53E8FCBD-7769-4D82-B8C9-C671418A82ADQ36327915-FF048A58-A6E9-4356-BA27-4AE5BD104920Q37117146-12072134-EC98-49E1-BF61-2DD015CD6E18Q37120813-F7B45D7A-A175-49F1-B647-D469BBD9F4D2Q37672295-B7B297F6-CF26-43F0-84C4-6542A55920F3Q37803276-E5A839CA-D4B9-4032-8002-D2373BEA1086Q38734920-75611027-AE3C-4B6C-9BAD-E505BE13438CQ39176826-436F72F6-5CDD-4F0D-AD41-207A2DCE29ACQ39223596-28122DD9-A01A-42B7-8F73-7CB8F3284AB5Q39384630-6EF4B1B7-BB2D-46E4-934C-A296FEE433FAQ39385143-FAF3BF4D-B2BA-4D0D-B34C-CC03AAACE78EQ41074727-A6C2A357-B5C5-41E9-BCDF-CC0F0AE00986Q42182958-B3B1B10C-4F54-4989-B8FE-450FE2628ED6Q43533162-33FA1C19-94F2-47D6-86C8-6694CB17DAAEQ51730305-C7C2414B-ABD6-497D-A542-4F9CADA7CB70Q55341800-2EC77660-E96E-46B8-88E8-E11A4BABF620Q58884356-DAB0D272-FEE5-4944-BC28-0BC4FB20F23B
P2860
Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts.
@en
Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts.
@nl
type
label
Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts.
@en
Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts.
@nl
prefLabel
Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts.
@en
Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts.
@nl
P2860
P1433
P1476
Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts.
@en
P2093
Katsumi Matsuzaki
Masaki Wakabayashi
P2860
P304
P356
10.1016/J.FEBSLET.2009.07.044
P407
P577
2009-08-03T00:00:00Z