High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide.
about
NMR solution structure of rat aβ(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's diseaseMetals and Neuronal Metal Binding Proteins Implicated in Alzheimer's DiseaseMechanisms of amyloid formation revealed by solution NMRBinding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-beta peptide.Metals and cholesterol: two sides of the same coin in Alzheimer's disease pathology.Curcumin alters the salt bridge-containing turn region in amyloid β(1-42) aggregates.Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.The amyloid-beta peptide of Alzheimer's disease binds Cu(I) in a linear bis-his coordination environment: insight into a possible neuroprotective mechanism for the amyloid-beta peptideDesign of small molecules that target metal-A{beta} species and regulate metal-induced A{beta} aggregation and neurotoxicity.Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formationMolecular dynamics study of Zn(aβ) and Zn(aβ)2Amyloid beta protein-induced zinc sequestration leads to synaptic loss via dysregulation of the ProSAP2/Shank3 scaffold.Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.Zn(++) binding disrupts the Asp(23)-Lys(28) salt bridge without altering the hairpin-shaped cross-β Structure of Aβ(42) amyloid aggregates.Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species.Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study.The modulation of metal bio-availability as a therapeutic strategy for the treatment of Alzheimer's disease.The structure of the amyloid-beta peptide high-affinity copper II binding site in Alzheimer disease.Structures and free energy landscapes of aqueous zinc(II)-bound amyloid-β(1-40) and zinc(II)-bound amyloid-β(1-42) with dynamics.Zn(II) ions substantially perturb Cu(II) ion coordination in amyloid-β at physiological pH.Therapeutics for Alzheimer's disease based on the metal hypothesisPharmacotherapeutic targets in Alzheimer's diseaseAmyloid plaques in PSAPP mice bind less metal than plaques in human Alzheimer's disease.Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide.Mapping brain metals to evaluate therapies for neurodegenerative disease.Novel drug targets based on metallobiology of Alzheimer's disease.Insights into the thermodynamics of copper association with amyloid-β, α-synuclein and prion proteins.Interactions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity.The role of metallobiology and amyloid-β peptides in Alzheimer's disease.Biophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway.Effect of zinc binding on β-amyloid structure and dynamics: implications for Aβ aggregation.Probing Alzheimer amyloid peptide aggregation using a cell-free fluorescent protein refolding method.Zinc and Copper Differentially Modulate Amyloid Precursor Protein Processing by γ-Secretase and Amyloid-β Peptide Production.Cellular polyamines promote amyloid-beta (Aβ) peptide fibrillation and modulate the aggregation pathways.Development of bifunctional stilbene derivatives for targeting and modulating metal-amyloid-β species.Small molecule modulators of copper-induced Abeta aggregationInteraction of PiB-derivative metal complexes with beta-amyloid peptides: selective recognition of the aggregated forms.The role of zinc in Alzheimer's disease.
P2860
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P2860
High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid beta-peptide.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
High-resolution NMR studies of ...... heimer's amyloid beta-peptide.
@en
High-resolution NMR studies of ...... heimer's amyloid beta-peptide.
@nl
type
label
High-resolution NMR studies of ...... heimer's amyloid beta-peptide.
@en
High-resolution NMR studies of ...... heimer's amyloid beta-peptide.
@nl
prefLabel
High-resolution NMR studies of ...... heimer's amyloid beta-peptide.
@en
High-resolution NMR studies of ...... heimer's amyloid beta-peptide.
@nl
P2860
P50
P1433
P1476
High-resolution NMR studies of ...... heimer's amyloid beta-peptide.
@en
P2860
P356
10.1111/J.1742-4658.2006.05563.X
P407
P577
2007-01-01T00:00:00Z