Interaction between amyloid-beta (1-42) peptide and phospholipid bilayers: a molecular dynamics study.
about
Dimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Roles for dysfunctional sphingolipid metabolism in Alzheimer's disease neuropathogenesis.A molecular dynamics study of the early stages of amyloid-beta(1-42) oligomerization: the role of lipid membranes.Monitoring of single vesicle cytochrome-c release illuminates BAK as a novel target of Aβ oligomers.Binding of β-amyloid (1-42) peptide to negatively charged phospholipid membranes in the liquid-ordered state: modeling and experimental studiesStudy of structural stability and damaging effect on membrane for four Aβ42 dimers.Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled AβDiscrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.Structures of beta-amyloid peptide 1-40, 1-42, and 1-55-the 672-726 fragment of APP-in a membrane environment with implications for interactions with gamma-secretaseBiochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.The role of molecular simulations in the development of inhibitors of amyloid β-peptide aggregation for the treatment of Alzheimer's diseaseMolecular understanding of a potential functional link between antimicrobial and amyloid peptides.Molecular dynamics simulations reveal the protective role of cholesterol in β-amyloid protein-induced membrane disruptions in neuronal membrane mimics.Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.Role of norepinephrine in Aβ-related neurotoxicity: dual interactions with Tyr10 and SNK(26-28) of Aβ.Dewetting transition assisted clearance of (NFGAILS) amyloid fibrils from cell membranes by graphene.Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer.Scaling and alpha-helix regulation of protein relaxation in a lipid bilayer.Stability of transmembrane amyloid β-peptide and membrane integrity tested by molecular modeling of site-specific Aβ42 mutations.Conformational behavior and aggregation of ataxin-3 in SDS.Molecular dynamics simulation studies of the structural response of an isolated Aβ1-42 monomer localized in the vicinity of the hydrophilic TiO 2 surface.Kinetic pathways to peptide aggregation on surfaces: the effects of β-sheet propensity and surface attraction.Investigation of the interaction of amyloid β peptide (11-42) oligomers with a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membrane using molecular dynamics simulation.The molecular behavior of a single β-amyloid inside a dipalmitoylphosphatidylcholine bilayer at three different temperatures: An atomistic simulation study: Aβ interaction with DPPC: Atomistic simulation.Molecular insight into amyloid oligomer destabilizing mechanism of flavonoid derivative 2-(4′ benzyloxyphenyl)-3-hydroxy-chromen-4-one through docking and molecular dynamics simulations
P2860
Q27305237-413B99A2-9CF5-490D-B6D6-FE28EAED6BD9Q33893017-0E8C4891-D5DF-44F6-8C3A-B17E30458535Q34007818-4360353F-D745-4593-8304-A4B1BF79E020Q34013248-441E7B37-945A-4996-9632-F180FF5B5E0CQ35313093-1B070527-B344-424B-B13F-28179E1D7EF0Q36150783-EB2709FA-D351-436A-A80F-8E4D3F0B7822Q36395898-AC412751-6B8C-48EB-8377-F03B35C50CD7Q36653725-56035EDE-73F4-409C-8DAE-F81D11CDF991Q36881483-E8D2B6EF-54F9-47B2-9A94-D453D7DC2ECDQ37013734-0F26E3BB-C114-4B7B-AE84-A464A38C1905Q37469347-7E63EFCC-6FC2-4225-98E3-2A8CF28FE583Q38016898-826F5109-290E-402B-BE10-BB34E1F40AF8Q38061633-1BECA575-3770-4C21-A073-4368F69759F6Q38238202-E4AF54BB-1591-4FC6-86FC-C44432F60E46Q38267422-042C891C-A76A-4828-9D54-E1410570C427Q38666447-70E5C9DF-8A61-4E63-8D39-BF5103EE0742Q38722235-10C64095-93B4-400E-8007-8A4A5E309F75Q39078176-4C178AAE-F0D2-4C7A-945D-B94EB8678673Q39384630-5E0A6FCB-5DF2-4455-BD33-B183B8ECE21FQ40748042-C107D562-0F65-40F5-B958-94B6163217FAQ41705451-CEE8137D-F96F-46BE-9E1F-2A2B33597D2BQ41970717-F85A1FC5-D7F8-44E3-A8D7-20A334D3DD9CQ43081476-197DB297-C63C-4055-97C3-2726CC549AF1Q46367449-1D0150E3-A68F-4050-8E2F-7A7EA18B19ACQ46755515-25A3FDE3-3912-4FC7-8705-1FDC4E7C2021Q47201808-DDD54E90-AC93-4604-BD58-F3C3A9666540Q48043847-D3FB76D6-6A17-433F-BEC2-9A2215A90424Q57781259-CF80628D-4B17-45E7-8E70-A72DE1AB2A32
P2860
Interaction between amyloid-beta (1-42) peptide and phospholipid bilayers: a molecular dynamics study.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on February 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Interaction between amyloid-be ...... s: a molecular dynamics study.
@en
Interaction between amyloid-beta
@nl
type
label
Interaction between amyloid-be ...... s: a molecular dynamics study.
@en
Interaction between amyloid-beta
@nl
prefLabel
Interaction between amyloid-be ...... s: a molecular dynamics study.
@en
Interaction between amyloid-beta
@nl
P2860
P1433
P1476
Interaction between amyloid-be ...... s: a molecular dynamics study.
@en
P2093
Charles H Davis
Max L Berkowitz
P2860
P304
P356
10.1016/J.BPJ.2008.09.053
P407
P577
2009-02-01T00:00:00Z