Metal ions as modulators of protein conformation and misfolding in neurodegeneration
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Metals and Neuronal Metal Binding Proteins Implicated in Alzheimer's DiseaseThe prokaryotic zinc-finger: structure, function and comparison with the eukaryotic counterpartStructure-mechanism-based engineering of chemical regulators targeting distinct pathological factors in Alzheimer's disease.Advances in the molecular understanding of biological zinc transport.Probing the kinetic stabilities of Friedreich's ataxia clinical variants using a solid phase GroEL chaperonin capture platform.Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals.Neurodegeneration in Friedreich's ataxia: from defective frataxin to oxidative stressImproving cytocompatibility of Co28Cr6Mo by TiO2 coating: gene expression study in human endothelial cellsDirect observation of the dynamics of single metal ions at the interface with solids in aqueous solutions.The role of metal ions in amyloid formation: general principles from model peptides.Metallothioneins in Prion- and Amyloid-Related Diseases.Amyloid fibril systems reduce, stabilize and deliver bioavailable nanosized iron.S100A6 amyloid fibril formation is calcium-modulated and enhances superoxide dismutase-1 (SOD1) aggregation.Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non-fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)?Copper prevents amyloid-β(1-42) from forming amyloid fibrils under near-physiological conditions in vitro.Small molecules present in the cerebrospinal fluid metabolome influence superoxide dismutase 1 aggregationPrecise, fast and flexible determination of protein interactions by affinity capillary electrophoresis. Part 2: cations.Analysis of human blood plasma and hen egg white by chiroptical spectroscopic methods (ECD, VCD, ROA).Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase.Effect of Zn(2+) ions on the assembly of amylin oligomers: insight into the molecular mechanisms.Coordination of Zn(2+) and Cu(2+) to the membrane disrupting fragment of amylin.Water-induced correlation between single ions imaged at the solid-liquid interface.
P2860
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P2860
Metal ions as modulators of protein conformation and misfolding in neurodegeneration
description
im Oktober 2012 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в жовтні 2012
@uk
name
Metal ions as modulators of protein conformation and misfolding in neurodegeneration
@en
Metal ions as modulators of protein conformation and misfolding in neurodegeneration
@nl
type
label
Metal ions as modulators of protein conformation and misfolding in neurodegeneration
@en
Metal ions as modulators of protein conformation and misfolding in neurodegeneration
@nl
prefLabel
Metal ions as modulators of protein conformation and misfolding in neurodegeneration
@en
Metal ions as modulators of protein conformation and misfolding in neurodegeneration
@nl
P2093
P1476
Metal ions as modulators of protein conformation and misfolding in neurodegeneration
@en
P2093
Cláudio M. Gomes
Hugo M. Botelho
Sónia S. Leal
P304
P356
10.1016/J.CCR.2012.04.004
P577
2012-10-01T00:00:00Z