Phenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site-specific binding.
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Wine polyphenols: potential agents in neuroprotectionFerulic Acid: A Hope for Alzheimer's Disease Therapy from PlantsDye-binding assays for evaluation of the effects of small molecule inhibitors on amyloid (aβ) self-assemblyA microliter-scale high-throughput screening system with quantum-dot nanoprobes for amyloid-β aggregation inhibitorsMethylated derivatives of myricetin enhance life span in Caenorhabditis elegans dependent on the transcription factor DAF-16.Structural determinants of Tau aggregation inhibitor potencyStructural Mechanism of the Interaction of Alzheimer Disease Aβ Fibrils with the Non-steroidal Anti-inflammatory Drug (NSAID) Sulindac SulfideSite-specific inhibitory mechanism for amyloid β42 aggregation by catechol-type flavonoids targeting the Lys residues.Consumption of green tea, but not black tea or coffee, is associated with reduced risk of cognitive decline.Growth and Accumulation of Secondary Metabolites in Perilla as Affected by Photosynthetic Photon Flux Density and Electrical Conductivity of the Nutrient Solution.Structure and mechanism of action of tau aggregation inhibitors.Mass spectrometry as an efficient tool for the characterization of amyloid β peptide 25-35 self-assembly species in aggregation and inhibition studies.Pharmacokinetics, Safety and Tolerability of Melissa officinalis Extract which Contained Rosmarinic Acid in Healthy Individuals: A Randomized Controlled TrialPhenolic compounds prevent the oligomerization of α-synuclein and reduce synaptic toxicity.Natural biomolecules and protein aggregation: emerging strategies against amyloidogenesisFine mapping of the amyloid β-protein binding site on myelin basic protein.Protein folding and aggregation into amyloid: the interference by natural phenolic compoundsStructure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta.Multi-Target-Directed Ligands and other Therapeutic Strategies in the Search of a Real Solution for Alzheimer's Disease.Cognitive-enhancing and antioxidant activities of the aqueous extract from Markhamia tomentosa (Benth.) K. Schum. stem bark in a rat model of scopolamine.Alzheimer's disease Aβ assemblies mediating rapid disruption of synaptic plasticity and memory.The role of molecular simulations in the development of inhibitors of amyloid β-peptide aggregation for the treatment of Alzheimer's diseaseNatural polyphenols binding to amyloid: a broad class of compounds to treat different human amyloid diseases.Perspectives on Inhibiting β-Amyloid Aggregation through Structure-Based Drug Design.Flavonoids are determinants of freezing tolerance and cold acclimation in Arabidopsis thalianaMechanisms for the inhibition of amyloid aggregation by small ligands.Potential of Different Coleus blumei Tissues for Rosmarinic Acid Production.Amyloid β-peptide 25-35 self-assembly and its inhibition: a model undecapeptide system to gain atomistic and secondary structure details of the Alzheimer's disease process and treatment.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Capping of aβ42 oligomers by small molecule inhibitors.Methyl 3,4-dihydroxybenzoate protects primary cortical neurons against Aβ₂₅₋₃₅-induced neurotoxicity through mitochondria pathway.Bioactive stilbenes from Vitis vinifera grapevine shoots extracts.Rosmarinic acid inhibits chemical hypoxia-induced cytotoxicity in primary cultured rat hepatocytes.Computer-assisted designed "selenoxy-chinolin": a new catalytic mechanism of the GPx-like cycle and inhibition of metal-free and metal-associated Aβ aggregation.Thymoquinone prevents β-amyloid neurotoxicity in primary cultured cerebellar granule neurons.Effects of antiparkinsonian agents on β-amyloid and α-synuclein oligomer formation in vitro.The cardioprotective effect of rosmarinic acid on acute myocardial infarction and genes involved in Ca2+ homeostasis.Study on the inter- and intra-peptide salt-bridge mechanism of Aβ23-28 oligomer interaction with small molecules: QM/MM method.Rifampicin is a candidate preventive medicine against amyloid-β and tau oligomers.Bioactive polyphenol interactions with β amyloid: a comparison of binding modelling, effects on fibril and aggregate formation and neuroprotective capacity.
P2860
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P2860
Phenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site-specific binding.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Phenolic compounds prevent amy ...... tion by site-specific binding.
@ast
Phenolic compounds prevent amy ...... tion by site-specific binding.
@en
type
label
Phenolic compounds prevent amy ...... tion by site-specific binding.
@ast
Phenolic compounds prevent amy ...... tion by site-specific binding.
@en
prefLabel
Phenolic compounds prevent amy ...... tion by site-specific binding.
@ast
Phenolic compounds prevent amy ...... tion by site-specific binding.
@en
P2093
P2860
P356
P1476
Phenolic compounds prevent amy ...... tion by site-specific binding.
@en
P2093
Akihiko Takashima
David B Teplow
Hisao Nishijo
Jun-ichi Takasaki
Kenjiro Ono
Masahito Yamada
Michael G Zagorski
P2860
P304
14631-14643
P356
10.1074/JBC.M111.325456
P407
P577
2012-03-05T00:00:00Z