Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.
about
Amyloid-beta-induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networksAmyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta poresMolecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes MellitusMicrobial amyloids--functions and interactions within the hostTransient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseFunction and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescenceCharacteristics of Amyloid-Related Oligomers Revealed by Crystal Structures of Macrocyclic β-Sheet MimicsMolecular basis of -amyloid oligomer recognition with a conformational antibody fragmentCrystal structure of a conformation-dependent rabbit IgG Fab specific for amyloid prefibrillar oligomersNeurotoxicity of prion peptides mimicking the central domain of the cellular prion proteinLarge aggregates are the major soluble Aβ species in AD brain fractionated with density gradient ultracentrifugationAmyloid oligomer neurotoxicity, calcium dysregulation, and lipid raftsPrion protein-mediated toxicity of amyloid-β oligomers requires lipid rafts and the transmembrane LRP1Beta-barrel models of soluble amyloid beta oligomers and annular protofibrils.Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent.Amyloid Beta annular protofibrils in cell processes and synapses accumulate with aging and Alzheimer-associated genetic modificationAtomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.Techniques for Monitoring Protein Misfolding and Aggregation in Vitro and in Living CellsAggregation of Aß(25-35) on DOPC and DOPC/DHA bilayers: an atomic force microscopy studyTwo disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomer-induced membrane permeability.Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells.Brain amyloid-β oligomers in ageing and Alzheimer's disease.Effect of metals on kinetic pathways of amyloid-β aggregationFibrillar oligomers nucleate the oligomerization of monomeric amyloid beta but do not seed fibril formationPolymorphic structures of Alzheimer's β-amyloid globulomers.Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.Structural determination of Abeta25-35 micelles by molecular dynamics simulations.A yeast toxic mutant of HET-s((218-289)) prion displays alternative intermediates of amyloidogenesisAn equilibrium model for linear and closed-loop amyloid fibril formation.Effect of synthetic aβ peptide oligomers and fluorinated solvents on Kv1.3 channel properties and membrane conductance.Intracellular amyloid and the neuronal origin of Alzheimer neuritic plaquesDistinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrilsRole of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Multivariate analyses of amyloid-beta oligomer populations indicate a connection between pore formation and cytotoxicityThe formation of tau pore-like structures is prevalent and cell specific: possible implications for the disease phenotypes.Abeta42 neurotoxicity is mediated by ongoing nucleated polymerization process rather than by discrete Abeta42 species.Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formationMembrane Incorporation, Channel Formation, and Disruption of Calcium Homeostasis by Alzheimer's β-Amyloid Protein.Amyloid-β annular protofibrils evade fibrillar fate in Alzheimer disease brainIsolation and characterization of antibody fragments selective for toxic oligomeric tau
P2860
Q24622558-8ED46AAF-E26C-4891-84E8-B41446057AB2Q26738355-660F1C12-9B7C-4782-9A45-7F576C72415CQ26774381-46D97075-9F5D-4BFC-8F87-67A5F58A43B1Q26827214-615D308A-228E-478D-8D0B-B49BDAC76F09Q26827421-C3168E62-294A-44DB-845E-0DC012F62293Q27026292-1A9D11C6-8DBB-4D94-9F77-B9795251BF34Q27667459-3F224BB3-A54D-4C6C-A839-FB4C6220D498Q27670832-3FD14977-23BE-4F80-86EF-270A0061BF1AQ27671820-A3657890-C180-4867-8068-5BD165110813Q28535083-F5EEA9D8-9B10-41CB-854A-C0004B13461CQ28732085-4E7E3BF0-A5C3-44ED-AEFF-7DDA71E933ECQ28742804-369C791F-EE8A-4FAA-A93F-F7270F822B69Q28910209-04A29079-6858-4B1B-B972-3E67F2E05D64Q30156038-E00D3B4A-4994-4547-AD26-D8ECB44F71C7Q30156880-7041B36D-BF46-48B5-82DF-8A6BF13B9837Q30157432-55F65485-FD7A-4B40-8D2A-825AF24BE579Q30391127-39D12E01-A1F3-49D0-B4F6-5FE9415262A3Q30420104-8753017D-6C21-40B1-BB5C-09F3703206F7Q30421208-44AA40FF-41BD-495D-B020-22792F2BB0D3Q30434734-EE18B3A0-0761-4B4E-8933-92A08BF28613Q30533868-6D8A2E49-2420-416C-962B-8344294ADF37Q30539133-4C77B599-C6EE-4277-A338-716EC706828BQ33649803-5DBB96B7-F999-4A1B-885E-749CC9BA0F7AQ33673470-FB91D9CB-F1A6-4715-88E1-E9788062BAE1Q33936902-D3122434-9198-4FED-B046-86D4ED776F16Q33946695-5D2854D9-8E9C-4925-812B-382140DB6E38Q33999447-2B13C6CD-F0C8-4131-834F-5DF7AE5E1CF2Q34062349-88787974-3103-45D1-A4F2-E7DAC752B11EQ34149516-DB9BE856-0786-4248-A384-7A27C919DE86Q34259659-0DE793BF-26E4-49A4-A6B8-5B4980A9D69AQ34266573-9604E678-B4E2-4ECE-879D-933FCB9F4619Q34416296-55B64F0B-0973-4E98-ABE0-1428D3102409Q34434154-57E77733-B3EA-4C90-9685-54DA0709EA2CQ34450675-180CADB2-AD47-422C-B39E-97C0BD641514Q34506434-72429075-E75F-42C2-B6D9-C581FF9724A1Q34624507-A5345064-7C01-4AE9-8D80-BEB3086D869DQ34685007-71FA1480-7D86-4981-8173-5E3D4D2CB6A5Q34923956-8E859F76-D12E-47A2-A2AD-DE724DFF6588Q35063033-E0E42509-4DE4-46BF-9768-A76D008CB136Q35137455-579217E5-FE9F-4B38-9744-7581DB05AA1C
P2860
Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Annular protofibrils are a str ...... inct type of amyloid oligomer.
@ast
Annular protofibrils are a str ...... inct type of amyloid oligomer.
@en
type
label
Annular protofibrils are a str ...... inct type of amyloid oligomer.
@ast
Annular protofibrils are a str ...... inct type of amyloid oligomer.
@en
prefLabel
Annular protofibrils are a str ...... inct type of amyloid oligomer.
@ast
Annular protofibrils are a str ...... inct type of amyloid oligomer.
@en
P2093
P2860
P356
P1476
Annular protofibrils are a str ...... inct type of amyloid oligomer.
@en
P2093
Anna Pensalfini
Charles Glabe
Elizabeth Head
Floyd Sarsoza
James Hall
Larry Margol
Rakez Kayed
Yuri Sokolov
P2860
P304
P356
10.1074/JBC.M808591200
P407
P577
2008-12-18T00:00:00Z