Modulating amyloid self-assembly and fibril morphology with Zn(II)
about
Challenges and breakthroughs in recent research on self-assemblySynthesis and structural investigations of N-alkylated beta-peptidosulfonamide-peptide hybrids of the amyloidogenic amylin(20-29) sequence: Implications of supramolecular folding for the design of peptide-based bionanomaterials.A potential role for alterations of zinc and zinc transport proteins in the progression of Alzheimer's disease.Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states.Molecular dynamics study of Zn(aβ) and Zn(aβ)2Engineering metal ion coordination to regulate amyloid fibril assembly and toxicity.Zinc-binding structure of a catalytic amyloid from solid-state NMR.Controlling amyloid growth in multiple dimensions.Copper(II)-bis-histidine coordination structure in a fibrillar amyloid β-peptide fragment and model complexes revealed by electron spin echo envelope modulation spectroscopyLow micromolar zinc accelerates the fibrillization of human tau via bridging of Cys-291 and Cys-322.Peptide membranes in chemical evolution.Context dependence of protein misfolding and structural strains in neurodegenerative diseases.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.The role of metal ions in amyloid formation: general principles from model peptides.The case for involvement of spiroplasma in the pathogenesis of transmissible spongiform encephalopathies.Dynamic self-assembly of coordination polymers in aqueous solution.Peptide self-assembly triggered by metal ions.A minimal conformational switching-dependent model for amyloid self-assembly.Amyloid scaffolds as alternative chlorosomes.Catalytic diversity in self-propagating peptide assemblies.The role of zinc in Alzheimer's disease.On the stability of the soluble amyloid aggregates.Peptides organized as bilayer membranes.Amyloidogenic peptides at hydrophobic-hydrophilic interfaces: coordination affinities and the chelate effect dictate the competitive binding of Cu2+ and Zn2+.Zn induced structural aggregation patterns of β-amyloid peptides by first-principle simulations and XAS measurements.Identifying the minimal copper- and zinc-binding site sequence in amyloid-beta peptides.One-step synthesis of natural silk sericin-based microcapsules with bionic structures.Characterizing Structural Stability of Amyloid Motif Fibrils Mediated by Water Molecules.Kinetic Analysis of Nanostructures Formed by Enzyme-Instructed Intracellular Assemblies against Cancer Cells.Quantum confined peptide assemblies with tunable visible to near-infrared spectral range
P2860
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P2860
Modulating amyloid self-assembly and fibril morphology with Zn(II)
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Modulating amyloid self-assembly and fibril morphology with Zn(II)
@ast
Modulating amyloid self-assembly and fibril morphology with Zn(II)
@en
type
label
Modulating amyloid self-assembly and fibril morphology with Zn(II)
@ast
Modulating amyloid self-assembly and fibril morphology with Zn(II)
@en
prefLabel
Modulating amyloid self-assembly and fibril morphology with Zn(II)
@ast
Modulating amyloid self-assembly and fibril morphology with Zn(II)
@en
P2093
P2860
P356
P1476
Modulating amyloid self-assembly and fibril morphology with Zn(II)
@en
P2093
David G Lynn
Jacob E Shokes
Jijun Dong
P2860
P304
P356
10.1021/JA055973J
P407
P577
2006-03-01T00:00:00Z