Fresh and nonfibrillar amyloid beta protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for AbetaP-channel-mediated cellular toxicity
about
Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networksBiophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFMToxic fibrillar oligomers of amyloid-β have cross-β structure.Neurotoxic amyloid beta oligomeric assemblies recreated in microfluidic platform with interstitial level of slow flowModels of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process.Benchmarking implicit solvent folding simulations of the amyloid beta(10-35) fragmentThe interplay between PolyQ and protein context delays aggregation by forming a reservoir of protofibrils.Amyloid-beta-induced ion flux in artificial lipid bilayers and neuronal cells: resolving a controversyAmyloid ion channels: a common structural link for protein-misfolding diseaseFormation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells.Structural convergence among diverse, toxic beta-sheet ion channels.Aberrant subcellular neuronal calcium regulation in aging and Alzheimer's diseaseAlzheimer's disease and metals: a review of the involvement of cellular membrane receptors in metallosignalling.Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions.Detection of amyloid beta aggregates in the brain of BALB/c mice after Chlamydia pneumoniae infection.Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure.Amyloid beta ion channel: 3D structure and relevance to amyloid channel paradigm.Misfolded amyloid ion channels present mobile beta-sheet subunits in contrast to conventional ion channelsAmyloid pore-channel hypothesis: effect of ethanol on aggregation state using frog oocytes for an Alzheimer's disease study.Micelle formation by a fragment of human islet amyloid polypeptide.Effect of sterols on beta-amyloid peptide (AbetaP 1-40) channel formation and their properties in planar lipid membranes.Single-cell screening of cytosolic [Ca(2+)] reveals cell-selective action by the Alzheimer's Aβ peptide ion channel.Nonspecific interaction of prefibrillar amyloid aggregates with glutamatergic receptors results in Ca2+ increase in primary neuronal cells.Protein folding and misfolding on surfaces.Efficiency of histidine-associating compounds for blocking the alzheimer's Abeta channel activity and cytotoxicity.
P2860
Q24622558-B0B10768-7ACB-455E-9E2B-06D507E28A48Q30427825-C8E38B37-4B95-4936-88B9-F6E6B92710C7Q30448740-C59B097D-4E64-4BF2-B2BE-96384D6B6106Q30514124-8056CF50-67A2-476E-BA9B-6981AE4299E7Q30540162-0A32B697-8A57-42C5-A1C2-C24D31CA7712Q31113748-9CD0DE1A-779A-4D2D-8B45-7AB389A66EF7Q31149897-9BFAF38F-B56F-41D5-9CED-F9784B331B01Q33268282-403228E7-0E3E-42C1-B491-A2F96A6D21FAQ33827991-532F4A69-9647-465B-8E0A-A718725B9728Q33906626-3D9235CF-07DD-4B72-9716-ADE5CB9F7F00Q33911387-252F9BA6-96BC-4923-8BA0-3D1941F4D62AQ34013023-53F33337-2D64-4817-AB9E-57E0D63A6C51Q34547754-97DF45E2-7FC5-49DF-8491-4FBBF59C9E74Q34725385-F4C58216-149D-4990-AF30-C2ACBCC1853AQ35691850-15AC47E1-3E31-4CDE-BEB4-BCABA3CDEDA3Q36087554-779523F8-C16A-4B9F-BD90-95C368D5C27DQ36295920-759C81D2-8185-4A97-B924-C25C6F6D4D2DQ36842093-69EF4F69-8114-42EC-8126-7C5C2705FC1CQ37443832-F0C8E41E-D153-4374-AD0F-560385F2392CQ38232297-0EB0D5BE-F2DA-4894-9C85-D2FEA66BCEB0Q40237012-E9F7E5B1-B7C2-4F93-A95C-7A8A97586C15Q40277927-5E4CF7FC-703F-4C56-ADE0-6F3F5E5DB10AQ43144744-FB7B4143-A087-48B3-8DC2-F9AB3E2DD59DQ43154901-76EA8C03-D5CD-4823-8199-984B9B6FA6B1Q43187852-DECD0B05-2D81-43BD-A020-9FDA4EFCE04DQ43248443-45B35B95-AF84-455C-8076-7905413FF006
P2860
Fresh and nonfibrillar amyloid beta protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: evidence for AbetaP-channel-mediated cellular toxicity
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Fresh and nonfibrillar amyloid ...... nel-mediated cellular toxicity
@ast
Fresh and nonfibrillar amyloid ...... nel-mediated cellular toxicity
@en
Fresh and nonfibrillar amyloid ...... nel-mediated cellular toxicity
@nl
type
label
Fresh and nonfibrillar amyloid ...... nel-mediated cellular toxicity
@ast
Fresh and nonfibrillar amyloid ...... nel-mediated cellular toxicity
@en
Fresh and nonfibrillar amyloid ...... nel-mediated cellular toxicity
@nl
prefLabel
Fresh and nonfibrillar amyloid ...... nel-mediated cellular toxicity
@ast
Fresh and nonfibrillar amyloid ...... nel-mediated cellular toxicity
@en
Fresh and nonfibrillar amyloid ...... nel-mediated cellular toxicity
@nl
P2093
P356
P1433
P1476
Fresh and nonfibrillar amyloid ...... nel-mediated cellular toxicity
@en
P2093
P304
P356
10.1096/FASEBJ.14.9.1244
P407
P577
2000-06-01T00:00:00Z