Molecular dynamics study of the beta amyloid peptide of Alzheimer's disease and its divalent copper complexes.
about
Dimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyStructural heterogeneity in familial Alzheimer's disease mutants of amyloid-beta peptides.Energy landscapes of the monomer and dimer of the Alzheimer's peptide Abeta(1-28).Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states.Cu(2+) affects amyloid-β (1-42) aggregation by increasing peptide-peptide binding forces.A study of the α-helical intermediate preceding the aggregation of the amino-terminal fragment of the β amyloid peptide (Aβ(1-28))Zn(++) binding disrupts the Asp(23)-Lys(28) salt bridge without altering the hairpin-shaped cross-β Structure of Aβ(42) amyloid aggregates.Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics.Biophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.Divalent copper ion bound amyloid-β(40) and amyloid-β(42) alloforms are less preferred than divalent zinc ion bound amyloid-β(40) and amyloid-β(42) alloforms.Nature of the amyloid-beta monomer and the monomer-oligomer equilibrium.In silico and in vitro studies to elucidate the role of Cu2+ and galanthamine as the limiting step in the amyloid beta (1-42) fibrillation process.A folding transition underlies the emergence of membrane affinity in amyloid-β.Characterization of the polymorphic states of copper(II)-bound Aβ(1-16) peptides by computational simulations.Probing oligomerization of amyloid beta peptide in silico.Development of multifunctional heterocyclic Schiff base as a potential metal chelator: a comprehensive spectroscopic approach towards drug discovery.Trypsin Binding with Copper Ions Scavenges Superoxide: Molecular Dynamics-Based Mechanism Investigation.Ligand field molecular dynamics simulation of Pt(II)-phenanthroline binding to N-terminal fragment of amyloid-β peptide.Benchmarking of copper(II) LFMM parameters for studying amyloid-β peptides.Gas-phase doubly charged complexes of cyclic peptides with copper in +1, +2 and +3 formal oxidation states: formation, structures and electron capture dissociation.Fe(2+) binding on amyloid β-peptide promotes aggregation.Modeling Cu2+-Aβ complexes from computational approachesd-Amino Acid Pseudopeptides as Potential Amyloid-Beta Aggregation Inhibitors
P2860
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P2860
Molecular dynamics study of the beta amyloid peptide of Alzheimer's disease and its divalent copper complexes.
description
2007 nî lūn-bûn
@nan
2007 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի մարտին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Molecular dynamics study of th ...... its divalent copper complexes.
@ast
Molecular dynamics study of th ...... its divalent copper complexes.
@en
type
label
Molecular dynamics study of th ...... its divalent copper complexes.
@ast
Molecular dynamics study of th ...... its divalent copper complexes.
@en
prefLabel
Molecular dynamics study of th ...... its divalent copper complexes.
@ast
Molecular dynamics study of th ...... its divalent copper complexes.
@en
P356
P1476
Molecular dynamics study of th ...... its divalent copper complexes.
@en
P2093
Duilio F Raffa
P304
P356
10.1021/JP0689621
P407
P577
2007-03-22T00:00:00Z