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Structural Optimization and Biological Evaluation of Substituted Bisphenol A Derivatives as β-Amyloid Peptide Aggregation Inhibitors

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
inferredcites →https://doi.org/10.1002/jnr.20514openalex-snapshot
Homocysteic acid induces intraneuronal accumulation of neurotoxic Aβ42: Implications for the pathogenesis of Alzheimer's disease
inferredcites →https://doi.org/10.1002/pro.5560020312openalex-snapshot
Thioflavine T interaction with synthetic Alzheimer's disease β ‐amyloid peptides: Detection of amyloid aggregation in solution
inferredcites →https://doi.org/10.1016/0022-2836(92)90106-topenalex-snapshot
Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's disease
inferredcites →https://doi.org/10.1016/0896-6273(94)90458-8openalex-snapshot
Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
inferredcites →https://doi.org/10.1016/j.bbadis.2004.06.008openalex-snapshot
Anti-amyloidogenic activity of tannic acid and its activity to destabilize Alzheimer's β-amyloid fibrils in vitro
inferredcites →https://doi.org/10.1016/j.bbrc.2004.09.024openalex-snapshot
β-Amyloid-derived pentapeptide RIIGLa inhibits Aβ1–42 aggregation and toxicity
inferredcites →https://doi.org/10.1016/j.bbrc.2005.01.030openalex-snapshot
A hybrid molecule that prohibits amyloid fibrils and alleviates neuronal toxicity induced by β-amyloid (1–42)
inferredcites →https://doi.org/10.1016/j.bbrc.2009.01.090openalex-snapshot
Design and biological activity of β-sheet breaker peptide conjugates
inferredcites →https://doi.org/10.1016/j.ejmech.2009.04.013openalex-snapshot
Perspectives in designing anti aggregation agents as Alzheimer disease drugs
inferredcites →https://doi.org/10.1016/j.jns.2009.01.024openalex-snapshot
Galantamine inhibits β-amyloid aggregation and cytotoxicity
inferredcites →https://doi.org/10.1016/j.neuron.2005.01.040openalex-snapshot
Intraneuronal Aβ Causes the Onset of Early Alzheimer’s Disease-Related Cognitive Deficits in Transgenic Mice
inferredcites →https://doi.org/10.1016/s0006-291x(02)00706-4openalex-snapshot
The effect of gp130 stimulation on glutamate-induced excitotoxicity in primary hippocampal neurons
inferredcites →https://doi.org/10.1016/s0006-291x(02)02337-9openalex-snapshot
NMR and CD studies on the interaction of Alzheimer β-amyloid peptide (12–28) with β-cyclodextrin
inferredcites →https://doi.org/10.1016/s0166-2236(00)01749-5openalex-snapshot
Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?
inferredcites →https://doi.org/10.1016/s0969-2126(98)00075-6openalex-snapshot
Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase
inferredcites →https://doi.org/10.1016/s1367-5931(97)80018-xopenalex-snapshot
Inhibition of amyloid formation: a strategy to delay the onset of Alzheimer's disease
inferredcites →https://doi.org/10.1021/bi036254popenalex-snapshot
Two-Site Binding of β-Cyclodextrin to the Alzheimer Aβ(1−40) Peptide Measured with Combined PFG-NMR Diffusion and Induced Chemical Shifts
inferredcites →https://doi.org/10.1021/bi060955fopenalex-snapshot
Inhibitor Discovery Targeting the Intermediate Structure of β-Amyloid Peptide on the Conformational Transition Pathway: Implications in the Aggregation Mechanism of β-Amyloid Peptide
inferredcites →https://doi.org/10.1021/bi701415bopenalex-snapshot
Designing Peptide Inhibitors for Oligomerization and Toxicity of Alzheimer's β-Amyloid Peptide
inferredcites →https://doi.org/10.1021/ja991167zopenalex-snapshot
Reversible Random Coil to β-Sheet Transition and the Early Stage of Aggregation of the Aβ(12−28) Fragment from the Alzheimer Peptide
inferredcites →https://doi.org/10.1021/jm070559aopenalex-snapshot
Novel Class of Quinone-Bearing Polyamines as Multi-Target-Directed Ligands To Combat Alzheimer's Disease
inferredcites →https://doi.org/10.1038/399a023openalex-snapshot
Translating cell biology into therapeutic advances in Alzheimer's disease
inferredcites →https://doi.org/10.1038/nm0798-827openalex-snapshot
Aging renders the brain vulnerable to amyloid β-protein neurotoxicity
inferredcites →https://doi.org/10.1073/pnas.0501218102openalex-snapshot
Conformational transition of amyloid β-peptide
inferredcites →https://doi.org/10.1074/jbc.271.15.8545openalex-snapshot
Arrest of -Amyloid Fibril Formation by a Pentapeptide Ligand
inferredcites →https://doi.org/10.1074/jbc.m102223200openalex-snapshot
Amyloid β-Protein Oligomerization
inferredcites →https://doi.org/10.1074/jbc.m201750200openalex-snapshot
Oligomeric and Fibrillar Species of Amyloid-β Peptides Differentially Affect Neuronal Viability
inferredcites →https://doi.org/10.1093/toxsci/kfp025openalex-snapshot
Bisphenol A Disrupts Notch Signaling by Inhibiting Gamma-Secretase Activity and Causes Eye Dysplasia of Xenopus laevis
inferredcites →https://doi.org/10.1126/science.286.5441.916openalex-snapshot
The Presenilins in Alzheimer's Disease--Proteolysis Holds the Key
inferredcites →https://doi.org/10.1126/science.8191290openalex-snapshot
An Increased Percentage of Long Amyloid β Protein Secreted by Familial Amyloid β Protein Precursor (βApp 717 ) Mutants
inferredcites →https://doi.org/10.1152/physrev.2001.81.2.741openalex-snapshot
Alzheimer's Disease: Genes, Proteins, and Therapy
inferredcites →https://doi.org/10.2174/0929867024606731openalex-snapshot
Converting a Peptide into a Drug: Strategies to Improve Stability and Bioavailability
inferredcites →https://doi.org/10.2174/1389557013407098openalex-snapshot
beta-Amyloid Aggregation Inhibitors for the Treatment of Alzheimer Disease Dream or Reality?
inferredcites →https://doi.org/10.2174/156802607779318262openalex-snapshot
Disrupting β-Amyloid Aggregation for Alzheimer Disease Treatment

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/cssc.201100402openalex-snapshot
Synthesis of Renewable Bisphenols from Creosol
inferred← citeshttps://doi.org/10.1007/s00044-016-1620-0openalex-snapshot
QSAR, docking, and Molecular dynamic studies on the polyphenolic as inhibitors of β-amyloid aggregation
inferred← citeshttps://doi.org/10.1007/s00158-020-02506-6openalex-snapshot
Advancing building engineering through structural and topology optimization
inferred← citeshttps://doi.org/10.1007/s00158-023-03696-5openalex-snapshot
Topology optimization with optimal design subdomain selection
inferred← citeshttps://doi.org/10.1016/j.bmc.2011.01.021openalex-snapshot
‘Click peptide’ using production of monomer Aβ from the O-acyl isopeptide: Application to assay system of aggregation inhibitors and cellular cytotoxicity
inferred← citeshttps://doi.org/10.1016/j.bmc.2011.03.010openalex-snapshot
Inhibition of amyloid-β aggregation by coumarin analogs can be manipulated by functionalization of the aromatic center
inferred← citeshttps://doi.org/10.1016/j.bmc.2012.02.059openalex-snapshot
Inhibition of cholinesterase activity and amyloid aggregation by berberine-phenyl-benzoheterocyclic and tacrine-phenyl-benzoheterocyclic hybrids
inferred← citeshttps://doi.org/10.1016/j.bmc.2012.02.061openalex-snapshot
Design, synthesis and evaluation of isaindigotone derivatives as dual inhibitors for acetylcholinesterase and amyloid beta aggregation
inferred← citeshttps://doi.org/10.1016/j.bmc.2013.07.011openalex-snapshot
Synthesis and biological evaluation of berberine–thiophenyl hybrids as multi-functional agents: Inhibition of acetylcholinesterase, butyrylcholinesterase, and Aβ aggregation and antioxidant activity
inferred← citeshttps://doi.org/10.1016/j.bmc.2018.08.007openalex-snapshot
Synthesis and evaluation of 1,2,3,4-tetrahydro-1-acridone analogues as potential dual inhibitors for amyloid-beta and tau aggregation
inferred← citeshttps://doi.org/10.1016/j.bmcl.2013.01.076openalex-snapshot
Synthesis of tetrahydroxybiphenyls and tetrahydroxyterphenyls and their evaluation as amyloid-β aggregation inhibitors
inferred← citeshttps://doi.org/10.1016/j.ejmech.2017.02.042openalex-snapshot
Design, synthesis and evaluation of 2-arylethenyl- N -methylquinolinium derivatives as effective multifunctional agents for Alzheimer's disease treatment
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Structure–activity relations of rosmarinic acid derivatives for the amyloid β aggregation inhibition and antioxidant properties
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Review on Alzheimer's disease: Inhibition of amyloid beta and tau tangle formation
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Amyloid formation and inhibition of an all-beta protein: A study on fungal polygalacturonase
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Degradable epoxy resins prepared from diepoxide monomer with dynamic covalent disulfide linkage
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Aromatics to bis-triquinane: a tandem oxidative dearomatization of bis-phenol, cycloaddition, photorearrangement and a rapid entry into carbocyclic framework of Xeromphalinone E
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.2c00944openalex-snapshot
N-Benzyl Benzamide Derivatives as Selective Sub-Nanomolar Butyrylcholinesterase Inhibitors for Possible Treatment in Advanced Alzheimer’s Disease
inferred← citeshttps://doi.org/10.1021/acs.jpca.8b11251openalex-snapshot
Exploring Amyloid-β Dimer Structure Using Molecular Dynamics Simulations
inferred← citeshttps://doi.org/10.1021/acs.macromol.9b01441openalex-snapshot
Well-Defined Networks from DGEBF─The Importance of Regioisomerism in Epoxy Resin Networks
inferred← citeshttps://doi.org/10.1021/acsanm.2c00171openalex-snapshot
Sulfonated N-Doped Carbon Nanotubes as Magnetic Solid Acid Catalysts for the Synthesis of Diphenolic Acid
inferred← citeshttps://doi.org/10.1021/acschemneuro.3c00326openalex-snapshot
Photo-Induced Cross-Linking of Unmodified α-Synuclein Oligomers
inferred← citeshttps://doi.org/10.1021/acssuschemeng.4c02394openalex-snapshot
Hardener-Dependent Properties of Twice Renewable Epoxy Resins Combining Tailored Lignin Fractions and Recycled BPA
inferred← citeshttps://doi.org/10.1021/ja405239vopenalex-snapshot
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
inferred← citeshttps://doi.org/10.1021/jm200853topenalex-snapshot
Synthesis, Biological Evaluation, and Molecular Modeling of Donepezil and N-[(5-(Benzyloxy)-1-methyl-1H-indol-2-yl)methyl]-N-methylprop-2-yn-1-amine Hybrids as New Multipotent Cholinesterase/Monoamine Oxidase Inhibitors for the Treatment of Alzheimer’s Disease
inferred← citeshttps://doi.org/10.1038/aps.2017.28openalex-snapshot
Amyloid beta: structure, biology and structure-based therapeutic development
inferred← citeshttps://doi.org/10.1039/c2nr11508eopenalex-snapshot
Observation of molecular inhibition and binding structures of amyloid peptides
inferred← citeshttps://doi.org/10.1093/jpp/rgaf055openalex-snapshot
Mangiferin and norathyriol acting on Alzheimer’s disease biomarkers: acetylcholinesterase, β-secretase (BACE-1), and amyloid β-peptide
inferred← citeshttps://doi.org/10.1093/nsr/nww003openalex-snapshot
Applying high-performance computing in drug discovery and molecular simulation
inferred← citeshttps://doi.org/10.1097/mop.0b013e3283454167openalex-snapshot
Current World Literature
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Cognitive Enhancers (Nootropics). Part 3: Drugs Interacting with Targets other than Receptors or Enzymes. Disease-modifying Drugs
inferred← citeshttps://doi.org/10.3389/fphar.2018.00708openalex-snapshot
Design of Diarylheptanoid Derivatives as Dual Inhibitors Against Class IIa Histone Deacetylase and β-amyloid Aggregation
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