Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide. - Wikidata - wikimedia - TriplyDB

Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.

Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.

http://www.wikidata.org/entity/Q42040291

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Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal models Synthetic Flavonoids, Aminoisoflavones: Interaction and Reactivity with Metal-Free and Metal-Associated Amyloid-β Species A small molecule that displays marked reactivity toward copper- versus zinc-amyloid-β implicated in Alzheimer's disease.Inhibition of Beta-Amyloid Fibrillation by Luminescent Iridium(III) Complex Probes Reactivity of diphenylpropynone derivatives toward metal-associated amyloid-β species.Discovery of novel PDE9 inhibitors capable of inhibiting Aβ aggregation as potential candidates for the treatment of Alzheimer's disease.Insights into antiamyloidogenic properties of the green tea extract (-)-epigallocatechin-3-gallate toward metal-associated amyloid-β species Pulsed hydrogen-deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation.Inhibition of human high-affinity copper importer Ctr1 orthologous in the nervous system of Drosophila ameliorates Aβ42-induced Alzheimer's disease-like symptoms Design and synthesis of curcumin analogues for in vivo fluorescence imaging and inhibiting copper-induced cross-linking of amyloid beta species in Alzheimer's disease Werner coordination chemistry and neurodegeneration.The benzazole scaffold: a SWAT to combat Alzheimer's disease.Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer's disease.Biological metals and metal-targeting compounds in major neurodegenerative diseases.Selenoprotein P and selenoprotein M block Zn2+ -mediated Aβ42 aggregation and toxicity.Ultraviolet light triggers the conversion of Cu2+-bound Aβ42 aggregates into cytotoxic species in a copper chelation-independent manner.Sialic Acid Hydroxamate: A Potential Antioxidant and Inhibitor of Metal-Induced β-Amyloid Aggregates.Modulation of the Aβ peptide aggregation pathway by KP1019 limits Aβ-associated neurotoxicity.Small bifunctional chelators that do not disaggregate amyloid β fibrils exhibit reduced cellular toxicity.The effect of Cu(2+) and Zn(2+) on the Aβ42 peptide aggregation and cellular toxicity Gold complexes inhibit the aggregation of prion neuropeptides.Multifunctional iron-chelators with protective roles against neurodegenerative diseases.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.Intercepting the Breslow intermediate via Claisen rearrangement: synthesis of complex tertiary alcohols without organometallic reagents.How Zn can impede Cu detoxification by chelating agents in Alzheimer's disease: a proof-of-concept study.Multi-target-directed phenol-triazole ligands as therapeutic agents for Alzheimer's disease.Mutual interference of Cu and Zn ions in Alzheimer's disease: perspectives at the molecular level.Development of multifunctional heterocyclic Schiff base as a potential metal chelator: a comprehensive spectroscopic approach towards drug discovery.Self-assembled peptide-polyoxometalate hybrid nanospheres: two in one enhances targeted inhibition of amyloid β-peptide aggregation associated with Alzheimer's disease.New Hydroxyquinoline-Based Derivatives as Potent Modulators of Amyloid-β Aggregations.Coordination Chemistry of Bifunctional Chemical Agents Designed for Applications in 64Cu PET Imaging for Alzheimer's Disease.Evaluation of 64Cu-Based Radiopharmaceuticals that Target Aβ Peptide Aggregates as Diagnostic Tools for Alzheimer's Disease.Structural and Mechanistic Insights into Development of Chemical Tools to Control Individual and Inter-Related Pathological Features in Alzheimer's Disease.A bioinorganic view of Alzheimer's disease: when misplaced metal ions (re)direct the electrons to the wrong target.Self-assembled lipoprotein based gold nanoparticles for detection and photothermal disaggregation of β-amyloid aggregates.Inhibition of copper-mediated aggregation of human γD-crystallin by Schiff bases.Chelation-induced diradical formation as an approach to modulation of the amyloid-β aggregation pathway.Dual-function triazole-pyridine derivatives as inhibitors of metal-induced amyloid-β aggregation Azo-dyes based small bifunctional molecules for metal chelation and controlling amyloid formation

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P2860

Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.

http://www.wikidata.org/entity/Q42040291

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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name

Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.

@en

Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.

@nl

type

label

Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.

@en

Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.

@nl

prefLabel

Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.

@en

Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.

@nl

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Journal of the American Chemical Society

P1476

Bifunctional compounds for controlling metal-mediated aggregation of the aβ42 peptide.

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P2093

Anuj K Sharma

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Darren Finkelstein

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Jaekwang Kim

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Jungsu Kim

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Liviu M Mirica

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Nicholas J Hawco

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Nigam P Rath

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Stephanie T Pavlova

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P2860

Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio

beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease

Global prevalence of dementia: a Delphi consensus study

Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils

Stabilization of neurotoxic soluble beta-sheet-rich conformations of the Alzheimer's disease amyloid-beta peptide

The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics

Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease

A specific amyloid-beta protein assembly in the brain impairs memory

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6625-6636

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10.1021/JA210588M

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15

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134

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2012-04-06T00:00:00Z

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221977413

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22452395

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3368506

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