Substoichiometric levels of Cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-{beta} from Alzheimer disease.
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Overview of Alzheimer's Disease and Some Therapeutic Approaches Targeting Aβ by Using Several Synthetic and Herbal CompoundsMetals and Neuronal Metal Binding Proteins Implicated in Alzheimer's DiseaseCopper-2 Ingestion, Plus Increased Meat Eating Leading to Increased Copper Absorption, Are Major Factors Behind the Current Epidemic of Alzheimer's DiseaseDivalent Copper as a Major Triggering Agent in Alzheimer's DiseaseCopper chelator induced efficient episodic memory recovery in a non-transgenic Alzheimer's mouse modelNumerical Simulations Reveal Randomness of Cu(II) Induced Aβ Peptide Dimerization under Conditions Present in Glutamatergic SynapsesEffect of metals on kinetic pathways of amyloid-β aggregationThe Case for Abandoning Therapeutic Chelation of Copper Ions in Alzheimer's DiseaseAlzheimer's Aβ peptides with disease-associated N-terminal modifications: influence of isomerisation, truncation and mutation on Cu2+ coordination.Synthetic Flavonoids, Aminoisoflavones: Interaction and Reactivity with Metal-Free and Metal-Associated Amyloid-β SpeciesCu(2+) affects amyloid-β (1-42) aggregation by increasing peptide-peptide binding forces.Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.Misfolded proteins in Alzheimer's disease and type II diabetes.Cu(II) enhances the effect of Alzheimer's amyloid-β peptide on microglial activationEffect of Copper and Zinc on the Single Molecule Self-Affinity of Alzheimer's Amyloid-β Peptides.Methionine oxidation perturbs the structural core of the prion protein and suggests a generic misfolding pathwayTruncated Amyloid-β(11-40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly.Nanoprobing of the effect of Cu(2+) cations on misfolding, interaction and aggregation of amyloid β peptide.The cellular prion protein traps Alzheimer's Aβ in an oligomeric form and disassembles amyloid fibers.A central role for dityrosine crosslinking of Amyloid-β in Alzheimer's disease.Thamnolia vermicularis extract improves learning ability in APP/PS1 transgenic mice by ameliorating both Aβ and Tau pathologies.Unique effect of Cu(II) in the metal-induced amyloid formation of β-2-microglobulinInteractions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity.Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases.Biophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.Biological metals and metal-targeting compounds in major neurodegenerative diseases.Histidine-Rich Oligopeptides To Lessen Copper-Mediated Amyloid-β Toxicity.Understanding copper sensitivity in zebrafish (Danio rerio) through the intracellular localization of copper transporters in a hepatocyte cell-line ZFL and the tissue expression profiles of copper transporters.The effect of Cu(2+) and Zn(2+) on the Aβ42 peptide aggregation and cellular toxicityRecent Progress in Alzheimer's Disease Research, Part 1: Pathology.Proteomic analysis of the copper ion-induced stress response in a human embryonic carcinoma cell line.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.Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation.Copper inducing Aβ42 rather than Aβ40 nanoscale oligomer formation is the key process for Aβ neurotoxicity.Reciprocal modulation of Aβ42 aggregation by copper and homocysteine.Copper prevents amyloid-β(1-42) from forming amyloid fibrils under near-physiological conditions in vitro.Cu(II) mediates kinetically distinct, non-amyloidogenic aggregation of amyloid-beta peptides.Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease.Development and Application of a Nonbonded Cu(2+) Model That Includes the Jahn-Teller Effect
P2860
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P2860
Substoichiometric levels of Cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-{beta} from Alzheimer disease.
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
Substoichiometric levels of Cu ...... {beta} from Alzheimer disease.
@en
type
label
Substoichiometric levels of Cu ...... {beta} from Alzheimer disease.
@en
prefLabel
Substoichiometric levels of Cu ...... {beta} from Alzheimer disease.
@en
P2093
P2860
P356
P1476
Substoichiometric levels of Cu ...... {beta} from Alzheimer disease.
@en
P2093
Claire J Sarell
John H Viles
Shane R Wilkinson
P2860
P304
41533-41540
P356
10.1074/JBC.M110.171355
P407
P577
2010-10-25T00:00:00Z