Neurodegenerative disease: amyloid pores from pathogenic mutations.
about
Functional amyloid formation within mammalian tissue.Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratioMapping out the multistage fibrillation of glucagonalphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35Molecular determinants of α-synuclein mutants' oligomerization and membrane interactionsThe N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranesDirect visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brainBiological markers of amyloid beta-related mechanisms in Alzheimer's diseaseThe toxicity of amyloid β oligomersMembrane curvature induction and tubulation are common features of synucleins and apolipoproteins.Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behaviorLipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in miceFenton chemistry and oxidative stress mediate the toxicity of the beta-amyloid peptide in a Drosophila model of Alzheimer's diseaseMisfolded CuZnSOD and amyotrophic lateral sclerosisVersatile Structures of α-SynucleinCommon mechanisms involved in Alzheimer's disease and type 2 diabetes: a key role of chronic bacterial infection and inflammationElectrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomicsPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Mechanisms of protein-folding diseases at a glanceChemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosisTangles, Toxicity, and Tau Secretion in AD - New Approaches to a Vexing ProblemStructural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studiesAβ42-oligomer Interacting Peptide (AIP) neutralizes toxic amyloid-β42 species and protects synaptic structure and function.Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the MechanismRepA-WH1, the agent of an amyloid proteinopathy in bacteria, builds oligomeric pores through lipid vesicles.Dynamic -Helix Structure of Micelle-bound Human AmylinAmyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicityDifferent 3D domain-swapped oligomeric cyanovirin-N structures suggest trapped folding intermediatesAtomic View of a Toxic Amyloid Small OligomerTafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascadeCuminaldehyde as the Major Component of Cuminum cyminum, a Natural Aldehyde with Inhibitory Effect on Alpha-Synuclein Fibrillation and CytotoxicityDopamine and paraquat enhance α-synuclein-induced alterations in membrane conductanceComplete phenotypic recovery of an Alzheimer's disease model by a quinone-tryptophan hybrid aggregation inhibitorA multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35Passive immunization reduces behavioral and neuropathological deficits in an alpha-synuclein transgenic model of Lewy body diseaseAmyloid oligomer neurotoxicity, calcium dysregulation, and lipid raftsIdentification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid PeptideThe stability of cylindrin β-barrel amyloid oligomer models-a molecular dynamics study.Beta-barrel models of soluble amyloid beta oligomers and annular protofibrils.Effect of beta-sheet propensity on peptide aggregation.
P2860
Q21092782-42C85D7C-EE15-433C-826B-FA9C2972D800Q24298670-D60AB498-0CC8-4920-97A7-2A2B512DD34AQ24300977-CA5ED878-8CF7-48A0-A13F-3DF07BA23793Q24307407-DB203515-B277-4298-9167-648ED111BD4EQ24312185-F879244D-B7A0-4FA8-8771-76F9AB29FC68Q24316619-65FCC835-9EA5-4EAC-8D61-6DC55748281BQ24321216-78AC31AE-FBF3-4F5A-AEDE-196522E0D991Q24622136-290A4600-1C41-4003-A835-D4E5A7BDC898Q24631757-97017B3D-3289-42AA-ABD5-E04F228F127DQ24633488-AC9F2838-244A-40DF-849D-7489AD393797Q24645994-6B80B78D-6DD3-4AE3-B458-084B79488BF2Q24649564-CEDE798C-47CC-4FE9-9844-830B837BC4E2Q24656549-A66EA668-67A7-443A-AD33-04B0873EE9A4Q24683677-715A212A-A84E-4FF9-AD40-4B2E91C955A5Q26744659-77C45C39-BACC-4093-9DCC-17EC65EDCF53Q26766681-D2B93FD2-76EB-4910-BAC9-2612BBF8B78CQ26822552-6117840E-97F5-421E-BD9A-A39FC281D99DQ26823798-C1756468-3AFF-4C8F-AFDC-30E7198DFC3EQ27003095-3CEA43CF-27C7-47DB-95D2-8B8094F27A23Q27004511-24568536-5916-4191-B20A-9B8F717E1109Q27004724-AF92D1EC-7080-458E-B153-9F30488E34E0Q27010584-4DF69219-8888-470B-862E-C60F1052D7D2Q27308119-76117C58-FC28-46C4-A4B5-C752DA3B16A3Q27315907-98328CCB-9465-41E3-BEE2-93CD0BECA51FQ27332087-5ADE164B-86AB-4B57-9A70-9EA55D193E54Q27653951-69244F89-FFF3-4542-AB6B-5FB095B138A7Q27674676-625437D2-5339-469B-B98F-09215DF5A736Q27677513-D2871F14-067F-4183-9EE0-15D324B58CABQ27677948-6F35D804-415F-4859-81FC-044617CD1AC7Q27679360-DD3592A7-A534-430E-A4CA-ABC7C8E974ACQ28267154-6E0448C1-15E2-4948-87C8-8777F30818F8Q28392011-C0E4E2AB-7C08-477C-8ECF-3DAFD97CF466Q28474363-11DAC5BC-33A4-42CA-AB15-71FFF6214D91Q28478191-D9038947-5A1F-4073-80E6-1EACE71C8F25Q28740551-57B3FB19-8A8B-4FFE-8491-9F6CAA50449CQ28742804-B7AB290B-5CB0-4023-9A57-A2C94C52D3DAQ28821551-B0878A31-6FE6-4952-A23B-A3986E25B07EQ30155110-B2C31757-4C2C-45BB-95FB-B73A3FD85166Q30156038-C810A71F-3C47-4FF5-A5EA-A3DA1CAEE775Q30157299-93ACAC6F-57BC-48EB-BFBC-67770E1A787A
P2860
Neurodegenerative disease: amyloid pores from pathogenic mutations.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
Neurodegenerative disease: amyloid pores from pathogenic mutations.
@en
Neurodegenerative disease: amyloid pores from pathogenic mutations.
@nl
type
label
Neurodegenerative disease: amyloid pores from pathogenic mutations.
@en
Neurodegenerative disease: amyloid pores from pathogenic mutations.
@nl
prefLabel
Neurodegenerative disease: amyloid pores from pathogenic mutations.
@en
Neurodegenerative disease: amyloid pores from pathogenic mutations.
@nl
P2093
P356
P1433
P1476
Neurodegenerative disease: amyloid pores from pathogenic mutations.
@en
P2093
Benjamin M Petre
Dean Hartley
Peter T Lansbury
Thomas Walz
P2888
P356
10.1038/418291A
P407
P577
2002-07-01T00:00:00Z
P5875
P6179
1011410794