Metal ions and intrinsically disordered proteins and peptides: from Cu/Zn amyloid-β to general principles.
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On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesA Redox-Active, Compact Molecule for Cross-Linking Amyloidogenic Peptides into Nontoxic, Off-Pathway Aggregates: In Vitro and In Vivo Efficacy and Molecular Mechanisms.Structure-mechanism-based engineering of chemical regulators targeting distinct pathological factors in Alzheimer's disease.The Case for Abandoning Therapeutic Chelation of Copper Ions in Alzheimer's DiseaseMammalian Metallothionein-3: New Functional and Structural InsightsA rationally designed small molecule for identifying an in vivo link between metal-amyloid-β complexes and the pathogenesis of Alzheimer's disease.Interplay of histidine residues of the Alzheimer's disease Aβ peptide governs its Zn-induced oligomerization.Copper(I/II), α/β-Synuclein and Amyloid-β: Menage à Trois?Biological metals and metal-targeting compounds in major neurodegenerative diseases.Insights on the interaction of alpha-synuclein and metals in the pathophysiology of Parkinson's disease.Protein/Peptide Aggregation and Amyloidosis on Biointerfaces.Metallothioneins in Prion- and Amyloid-Related Diseases.Reactivity of U-associated osteopontin with lactoferrin: a one-to-many complex.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.Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Copper-zinc cross-modulation in prion protein binding.Interaction of apoNeuroglobin with heme-Aβ complexes relevant to Alzheimer's disease.Zinc(II) Binding Site to the Amyloid-β Peptide: Insights from Spectroscopic Studies with a Wide Series of Modified Peptides.Identification of key structural features of the elusive Cu-Aβ complex that generates ROS in Alzheimer's disease.How Zn can impede Cu detoxification by chelating agents in Alzheimer's disease: a proof-of-concept study.Identifying Cu(ii)-amyloid peptide binding intermediates in the early stages of aggregation by resonance Raman spectroscopy: a simulation study.A Near-Infrared Responsive Drug Sequential Release System for Better Eradicating Amyloid Aggregates.Minor Structural Variations of Small Molecules Tune Regulatory Activities toward Pathological Factors in Alzheimer's Disease.A Trishistidine Pseudopeptide with Ability to Remove Both CuΙ and CuΙΙ from the Amyloid-β Peptide and to Stop the Associated ROS Formation.Resistance of Cu(Aβ4-16) to Copper Capture by Metallothionein-3 Supports a Function for the Aβ4-42 Peptide as a Synaptic Cu(II) Scavenger.Free Superoxide is an Intermediate in the Production of H2O2 by Copper(I)-Aβ Peptide and O2.Effects of structural modifications on the metal binding, anti-amyloid activity, and cholinesterase inhibitory activity of chalcones.Cysteine and glutathione trigger the Cu-Zn swap between Cu(ii)-amyloid-β4-16 peptide and Zn7-metallothionein-3.MMP-7 cleaves amyloid β fragment peptides and copper ion inhibits the degradation.The Pathogenic A2V Mutant Exhibits Distinct Aggregation Kinetics, Metal Site Structure, and Metal Exchange of the Cu2+ -Aβ Complex.Introduction of a fluorescent probe to amyloid-β to reveal kinetic insights into its interactions with copper(II).A Functional Role for Aβ in Metal Homeostasis? N-Truncation and High-Affinity Copper Binding.Ascorbate Oxidation by Cu(Amyloid-β) Complexes: Determination of the Intrinsic Rate as a Function of Alterations in the Peptide Sequence Revealing Key Residues for Reactive Oxygen Species Production.On the Metal Cofactor in the Tyrosinase Family.The English (H6R) familial Alzheimer's disease mutation facilitates zinc-induced dimerization of the amyloid-β metal-binding domain.Looking at the Disordered Proteins through the Computational Microscope.Crystal structure of catena-poly[[[di-chlorido-copper(II)]-{μ-tert-butyl N-methyl-N-[4-(6-{[4-(pyridin-2-yl-κN)-1H-1,2,3-triazol-1-yl-κN3]meth-yl}-1,3-benzo-thia-zol-2-yl)phen-yl]carbamato}] aceto-nitrile monosolvate].Polyoxometalate-based nanozyme: Design of a multifunctional enzyme for multi-faceted treatment of Alzheimer’s diseaseConformational plasticity of the intrinsically disordered protein ASR1 modulates its function as a drought stress-responsive geneCopper in Alzheimer’s disease: Implications in amyloid aggregation and neurotoxicity
P2860
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P2860
Metal ions and intrinsically disordered proteins and peptides: from Cu/Zn amyloid-β to general principles.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年学术文章
@wuu
2014年学术文章
@zh
2014年学术文章
@zh-cn
2014年学术文章
@zh-hans
2014年学术文章
@zh-my
2014年学术文章
@zh-sg
2014年學術文章
@yue
2014年學術文章
@zh-hant
name
Metal ions and intrinsically d ...... yloid-β to general principles.
@en
Metal ions and intrinsically d ...... yloid-β to general principles.
@nl
type
label
Metal ions and intrinsically d ...... yloid-β to general principles.
@en
Metal ions and intrinsically d ...... yloid-β to general principles.
@nl
prefLabel
Metal ions and intrinsically d ...... yloid-β to general principles.
@en
Metal ions and intrinsically d ...... yloid-β to general principles.
@nl
P356
P1476
Metal ions and intrinsically d ...... yloid-β to general principles.
@en
P2093
Christelle Hureau
P304
P356
10.1021/AR400293H
P407
P577
2014-05-29T00:00:00Z