Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.
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NMR solution structure of rat aβ(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's diseaseMulti-Target Directed Donepezil-Like Ligands for Alzheimer's DiseaseOverview of Alzheimer's Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal CompoundsAmyloid-beta (Aβ) D7H mutation increases oligomeric Aβ42 and alters properties of Aβ-zinc/copper assembliesModels of membrane-bound Alzheimer's Abeta peptide assembliesEffect of metals on kinetic pathways of amyloid-β aggregationCurcumin alters the salt bridge-containing turn region in amyloid β(1-42) aggregates.Peptide-Mediated Nanopore Detection of Uranyl Ions in Aqueous Media.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.Positive evolutionary selection of an HD motif on Alzheimer precursor protein orthologues suggests a functional role.Electrochemical and homogeneous electron transfers to the Alzheimer amyloid-beta copper complex follow a preorganization mechanism.Cytotoxicity of superoxide dismutase 1 in cultured cells is linked to Zn2+ chelation.Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formationMolecular-level examination of Cu2+ binding structure for amyloid fibrils of 40-residue Alzheimer's β by solid-state NMR spectroscopy.Molecular dynamics study of Zn(aβ) and Zn(aβ)2Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.Intra-membrane oligomerization and extra-membrane oligomerization of amyloid-β peptide are competing processes as a result of distinct patterns of motif interplay.Characterization of the Copper(II) Binding Sites in Human Carbonic Anhydrase II.Iron is a specific cofactor for distinct oxidation- and aggregation-dependent Aβ toxicity mechanisms in a Drosophila model.Zn(++) binding disrupts the Asp(23)-Lys(28) salt bridge without altering the hairpin-shaped cross-β Structure of Aβ(42) amyloid aggregates.Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study.Zinc modulates copper coordination mode in prion protein octa-repeat subdomains.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.Kinetic and structural characterization of amyloid-β peptide hydrolysis by human angiotensin-1-converting enzyme.Zn(II) ions substantially perturb Cu(II) ion coordination in amyloid-β at physiological pH.The tachykinin peptide neurokinin B binds copper forming an unusual [CuII(NKB)2] complex and inhibits copper uptake into 1321N1 astrocytoma cells.Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide.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.Werner coordination chemistry and neurodegeneration.The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway.Beta-amyloid oligomers: recent developments.Potentiating role of copper on spatial memory deficit induced by beta amyloid and evaluation of mitochondrial function markers in the hippocampus of rats.Zinc and Copper Differentially Modulate Amyloid Precursor Protein Processing by γ-Secretase and Amyloid-β Peptide Production.Energetic contributions of residues to the formation of early amyloid-β oligomers.The effect of Cu(2+) and Zn(2+) on the Aβ42 peptide aggregation and cellular toxicityA first-principle calculation of the XANES spectrum of Cu(2+) in water.
P2860
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P2860
Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh-hant
name
Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.
@en
Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.
@nl
type
label
Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.
@en
Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.
@nl
prefLabel
Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.
@en
Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.
@nl
P2093
P2860
P50
P356
P1476
Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.
@en
P2093
Cristina Potrich
Francesco Stellato
Massimiliano Comai
Wolfram Meyer-Klaucke
P2860
P304
10784-10792
P356
10.1074/JBC.M707109200
P407
P577
2008-01-30T00:00:00Z