Polyglutamine-induced ion channels: a possible mechanism for the neurotoxicity of Huntington and other CAG repeat diseases.
about
Amyloid-like aggregates of the yeast prion protein ure2 enter vertebrate cells by specific endocytotic pathways and induce apoptosis.Antimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studiesStructural convergence among diverse, toxic beta-sheet ion channels.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Evidence that Perutz's double-beta-stranded subunit structure for beta-amyloids also applies to their channel-forming structures in membranes.Alzheimer's disease: which type of amyloid-preventing drug agents to employ?From Alzheimer to Huntington: why is a structural understanding so difficult?Membrane Incorporation, Channel Formation, and Disruption of Calcium Homeostasis by Alzheimer's β-Amyloid Protein.Probing the Huntingtin 1-17 membrane anchor on a phospholipid bilayer by using all-atom simulationsAntimicrobial properties of amyloid peptides.The interaction of polyglutamine peptides with lipid membranes is regulated by flanking sequences associated with huntingtinModels of toxic beta-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic alzheimer beta-amyloid ion channels.Heat-induced fibrillation of BclXL apoptotic repressorPre-amyloid oligomers budding:a metastatic mechanism of proteotoxicity.Misfolded amyloid ion channels present mobile beta-sheet subunits in contrast to conventional ion channelsCalcium dyshomeostasis and neurotoxicity of Alzheimer's beta-amyloid protein.Low-n oligomers as therapeutic targets of Alzheimer's disease.Conformational behavior and aggregation of ataxin-3 in SDS.Channel formation by serum amyloid A: a potential mechanism for amyloid pathogenesis and host defense.Atomistic mechanisms of huntingtin N-terminal fragment insertion on a phospholipid bilayer revealed by molecular dynamics simulations.Cells exposed to a huntingtin fragment containing an expanded polyglutamine tract show no sign of ion channel formation: results arguing against the ion channel hypothesis.The composition of the polyglutamine-containing proteins influences their co-aggregation properties.
P2860
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P2860
Polyglutamine-induced ion channels: a possible mechanism for the neurotoxicity of Huntington and other CAG repeat diseases.
description
2000 nî lūn-bûn
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2000年の論文
@ja
2000年学术文章
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2000年学术文章
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2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
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2000年學術文章
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2000年學術文章
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name
Polyglutamine-induced ion chan ...... and other CAG repeat diseases.
@en
Polyglutamine-induced ion chan ...... and other CAG repeat diseases.
@nl
type
label
Polyglutamine-induced ion chan ...... and other CAG repeat diseases.
@en
Polyglutamine-induced ion chan ...... and other CAG repeat diseases.
@nl
prefLabel
Polyglutamine-induced ion chan ...... and other CAG repeat diseases.
@en
Polyglutamine-induced ion chan ...... and other CAG repeat diseases.
@nl
P2093
P2860
P1476
Polyglutamine-induced ion chan ...... and other CAG repeat diseases.
@en
P2093
P2860
P304
P356
10.1002/(SICI)1097-4547(20000515)60:4<490::AID-JNR7>3.0.CO;2-9
P577
2000-05-01T00:00:00Z