Quantification of the binding properties of Cu2+ to the amyloid beta peptide: coordination spheres for human and rat peptides and implication on Cu2+-induced aggregation
about
Histidine-containing host-defence skin peptides of anurans bind Cu2+. An electrospray ionisation mass spectrometry and computational modelling study.Reevaluation of copper(I) affinity for amyloid-β peptides by competition with ferrozine--an unusual copper(I) indicator.Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.Calorimetric investigation of copper binding in the N-terminal region of the prion protein at low copper loading: evidence for an entropically favorable first binding event.Substantial contribution of the two imidazole rings of the His13-His14 dyad to Cu(II) binding in amyloid-β(1-16) at physiological pH and its significance.Characterization of the Copper(II) Binding Sites in Human Carbonic Anhydrase II.Nanoprobing of the effect of Cu(2+) cations on misfolding, interaction and aggregation of amyloid β 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 amyloid precursor protein: a biochemical enigma in brain development, function and disease.Biophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.Translation of Pre-Clinical Studies into Successful Clinical Trials for Alzheimer's Disease: What are the Roadblocks and How Can They Be Overcome?On the involvement of copper binding to the N-terminus of the amyloid Beta Peptide of Alzheimer's disease: a computational study on model systems.Reciprocal modulation of Aβ42 aggregation by copper and homocysteine.Calorimetric investigation of copper(II) binding to Aβ peptides: thermodynamics of coordination plasticity.Metal-catalyzed oxidation of Aβ and the resulting reorganization of Cu binding sites promote ROS production.Link between Affinity and Cu(II) Binding Sites to Amyloid-β Peptides Evaluated by a New Water-Soluble UV-Visible Ratiometric Dye with a Moderate Cu(II) Affinity.Exploring the boundaries of direct detection and characterization of labile isomers - a case study of copper(ii)-dipeptide systems.Molecular Simulations of Human and Mouse Aβ1-16 at Different pH Values: Structural Characteristics toward Understanding Cu(2+) -Coordinated Amyloid Beta Spheres.Histidine-rich branched peptides as Cu(II) and Zn(II) chelators with potential therapeutic application in Alzheimer's disease.NMR Methods to Study Effects of Additives on Phase Separation of Thermoresponsive Polymer
P2860
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P2860
Quantification of the binding properties of Cu2+ to the amyloid beta peptide: coordination spheres for human and rat peptides and implication on Cu2+-induced aggregation
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Quantification of the binding ...... on on Cu2+-induced aggregation
@en
Quantification of the binding ...... on on Cu2+-induced aggregation
@nl
type
label
Quantification of the binding ...... on on Cu2+-induced aggregation
@en
Quantification of the binding ...... on on Cu2+-induced aggregation
@nl
prefLabel
Quantification of the binding ...... on on Cu2+-induced aggregation
@en
Quantification of the binding ...... on on Cu2+-induced aggregation
@nl
P2093
P2860
P356
P1476
Quantification of the binding ...... on on Cu2+-induced aggregation
@en
P2093
Christopher G Dudzik
Glenn L Millhauser
John D Simon
Tessa M Carducci
William D Bush
P2860
P304
11261-11271
P356
10.1021/JP103272V
P407
P577
2010-09-01T00:00:00Z