Reference health
Journey on Naphthoquinone and Anthraquinone Derivatives: New Insights in Alzheimer’s Disease
169/169 checkable references clean · checked 2026-08-21
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
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The 169 checked references that resolve
resolves10.1016/j.biopha.2018.02.052
Plumbagin ameliorates memory dysfunction in streptozotocin induced Alzheimer’s disease via activation of Nrf2/ARE pathway and inhibition of β-secretase
resolves10.1073/pnas.83.13.4913
Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.
resolves10.1196/annals.1306.012
Redox‐Active Metals, Oxidative Stress, and Alzheimer's Disease Pathology
resolves10.2174/1389450119666180820104723
Potential Enzymatic Targets in Alzheimer’s: A Comprehensive Review
resolves10.1039/C9MD00337A
Current and emerging therapeutic targets of alzheimer's disease for the design of multi-target directed ligands
resolves10.1002/brb3.1831
Memantine, Donepezil, or Combination Therapy—What is the best therapy for Alzheimer’s Disease? A Network Meta‐Analysis
resolves10.1146/annurev.ne.17.030194.002421
Normal and Abnormal Biology of the beta-Amyloid Precursor Protein
resolves10.1007/s00401-014-1347-2
The multifaceted nature of amyloid precursor protein and its proteolytic fragments: friends and foes
resolves10.1074/jbc.R115.677211
Amyloid Precursor Protein (APP) Metabolites APP Intracellular Fragment (AICD), Aβ42, and Tau in Nuclear Roles
resolves10.1038/349704a0
Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
resolves10.1093/hmg/10.16.1665
Pathogenic APP mutations near the gamma-secretase cleavage site differentially affect Abeta secretion and APP C-terminal fragment stability
resolves10.1007/s11055-017-0513-0
25 Years of the Amyloid Hypothesis of the Origin of Alzheimer’s Disease: Advances, Failures, and New Perspectives
resolves10.1016/S0006-291X(84)80190-4
Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
resolves10.1007/s10930-019-09854-3
Structure and Function of Alzheimer’s Amyloid βeta Proteins from Monomer to Fibrils: A Mini Review
resolves10.1074/jbc.M212785200
Specific Compositions of Amyloid-β Peptides as the Determinant of Toxic β-Aggregation
resolves10.1006/jmbi.2001.4970
Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis11Edited by F. Cohen
resolves10.1073/pnas.222681699
Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
resolves10.18388/abp.2005_3454
Molecular mechanisms initiating amyloid beta-fibril formation in Alzheimer's disease.
resolves10.1002/med.21622
BACE1 inhibitors: Current status and future directions in treating Alzheimer's disease
resolves10.1111/bph.14593
Targeting amyloid clearance in Alzheimer's disease as a therapeutic strategy
resolves10.1073/pnas.0509386103
Aβ and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer’s disease
resolves10.1007/s10787-019-00580-x
Activation of microglia and astrocytes: a roadway to neuroinflammation and Alzheimer’s disease
resolves10.1016/S0140-6736(76)91936-X
SELECTIVE LOSS OF CENTRAL CHOLINERGIC NEURONS IN ALZHEIMER'S DISEASE
resolves10.1016/j.neuron.2012.08.036
Acetylcholine as a Neuromodulator: Cholinergic Signaling Shapes Nervous System Function and Behavior
resolves10.3389/fnins.2019.00446
Exploring the Pathogenesis of Alzheimer Disease in Basal Forebrain Cholinergic Neurons: Converging Insights From Alternative Hypotheses
resolves10.1136/jnnp.66.2.137
The cholinergic hypothesis of Alzheimer's disease: a review of progress
resolves10.1023/A:1022869222652
Cholinesterases: New Roles in Brain Function and in Alzheimer's Disease
resolves10.3390/biom10010040
Alzheimer’s Disease Pharmacotherapy in Relation to Cholinergic System Involvement
resolves10.1021/ja020243m
Role of the Catalytic Triad and Oxyanion Hole in Acetylcholinesterase Catalysis: An ab initio QM/MM Study
resolves10.1358/dot.2003.39.1.740206
The role of acetylcholinesterase in the pathogenesis of Alzheimer's
disease
resolves10.1021/acsomega.9b03693
Discovery of Helminthosporin, an Anthraquinone Isolated
from
<i>Rumex abyssinicus</i>
Jacq as a Dual
Cholinesterase Inhibitor
resolves10.3389/fneur.2013.00083
The Importance of Tau Phosphorylation for Neurodegenerative Diseases
resolves10.17533/udea.vitae.17322
Naphthoquinones: biological properties and synthesis of lawsone and derivates - a structured review
resolves10.1016/j.bmcl.2004.01.002
Design, synthesis and evaluation of novel 1,4-naphthoquinone derivatives as antifungal and anticancer agents
resolves10.1007/BF02974272
Synthesis and evaluation of antitumor activity of novel 1,4-Naphthoquinone derivatives (IV)
resolves10.1021/jo401842d
Copper(II)-Catalyzed Sequential C,N-Difunctionalization of 1,4-Naphthoquinone for the Synthesis of Benzo[<i>f</i>]indole-4,9-diones under Base-Free Condition
resolves10.1021/ol501329t
Synthesis of Isochromene-Type Scaffolds via Single-Flask Diels–Alder-[4 + 2]-Annulation Sequence of a Silyl-Substituted Diene with Menadione
resolves10.1021/ol302987h
A Facile Access to Enantioenriched Isoindolines <i>via</i> One-Pot Sequential Cu(I)-Catalyzed Asymmetric 1,3-Dipolar Cycloaddition/Aromatization
resolves10.1039/b913252j
Green photochemistry: photo-Friedel–Crafts acylations of 1,4-naphthoquinone in room temperature ionic liquids
resolves10.1002/chem.200600993
Highly Enantioselective Epoxidation of 2‐Methylnaphthoquinone (Vitamin K<sub>3</sub>) Mediated by New <i>Cinchona</i> Alkaloid Phase‐Transfer Catalysts
resolves10.1371/journal.pone.0011101
Complete Phenotypic Recovery of an Alzheimer's Disease Model by a Quinone-Tryptophan Hybrid Aggregation Inhibitor
resolves10.1016/j.neuropharm.2008.06.065
Shikonins attenuate microglial inflammatory responses by inhibition of ERK, Akt, and NF-κB: neuroprotective implications
resolves10.1021/tx000224v
Neuroprotection in the MPTP Parkinsonian C57BL/6 Mouse Model by a Compound Isolated from Tobacco
resolves10.1016/j.phrs.2016.01.021
Medicinal plants in Brazil: Pharmacological studies, drug discovery, challenges and perspectives
resolves10.2174/138955709788167592
Natural Products and their Analogues as Efficient Anticancer Drugs
resolves10.2174/1570179412666150817220343
Natural Naphthoquinones with Great Importance in Medicinal Chemistry
resolves10.2174/157341209787314936
Noteworthy Secondary Metabolites Naphthoquinones – their Occurrence, Pharmacological Properties and Analysis
resolves10.1016/S1570-0232(04)00651-8
Separation methods of quinonoid constituents of plants used in Oriental traditional medicines
resolves10.1016/j.toxlet.2005.04.001
Prooxidant activity of resveratrol in the presence of copper ions: Mutagenicity in plasmid DNA
resolves10.1016/S0009-2797(00)00143-5
Anti-oxidant, pro-oxidant properties of tannic acid and its binding to DNA
resolves10.1016/j.intimp.2009.03.022
Anti-inflammatory effects of plumbagin are mediated by inhibition of NF-kappaB activation in lymphocytes
resolves10.1111/j.1471-4159.2009.06552.x
Plumbagin, a novel Nrf2/ARE activator, protects against cerebral ischemia
resolves10.1021/jf050721n
Phenolic Acids, Syringaldehyde, and Juglone in Fruits of Different Cultivars of<i> Juglans regia</i> L.
resolves10.1021/tx034132s
Cytotoxic Action of Juglone and Plumbagin: A Mechanistic Study Using HaCaT Keratinocytes
resolves10.1139/y2012-134
Anticancer activity and mechanism of juglone on human cervical carcinoma HeLa cells
resolves10.1016/S0304-3835(98)00035-4
Inhibitory effects of plumbagin and juglone on azoxymethane-induced intestinal carcinogenesis in rats
resolves10.1007/s10886-009-9609-5
Milieu-Dependent Pro- and Antioxidant Activity of Juglone May Explain Linear and Nonlinear Effects on Seedling Development
resolves10.3892/mmr.2017.7806
Juglone potentiates TRAIL-induced apoptosis in human melanoma cells via activating the ROS-p38-p53 pathway
resolves10.3892/or.2017.5878
Juglone reduces growth and migration of U251 glioblastoma cells and disrupts angiogenesis
resolves10.1016/j.theochem.2009.09.024
A DFT study on the radical scavenging activity of juglone and its derivatives
resolves10.1016/j.freeradbiomed.2004.04.021
Isolation of long-lived mutants in Caenorhabditis elegans using selection for resistance to juglone
resolves10.1155/2016/8636409
Structural and Antioxidant Properties of Compounds Obtained from Fe<sup>2+</sup>Chelation by Juglone and Two of Its Derivatives: DFT, QTAIM, and NBO Studies
resolves10.1146/annurev-food-041715-033206
Food Antioxidants: Chemical Insights at the Molecular Level
resolves10.1016/j.foodchem.2010.08.012
The molecular basis of working mechanism of natural polyphenolic antioxidants
resolves10.3390/molecules16021749
Structure of Dihydrochalcones and Related Derivatives and Their Scavenging and Antioxidant Activity against Oxygen and Nitrogen Radical Species
resolves10.1021/jp037247d
Antioxidant Properties of Phenolic Compounds: H-Atom versus Electron Transfer Mechanism
resolves10.1074/jbc.M601849200
The Peptidylprolyl cis/trans-Isomerase Pin1 Modulates Stress-induced Dephosphorylation of Tau in Neurons
resolves10.3233/JAD-180361
Walnut Supplementation in the Diet Reduces Oxidative Damage and Improves Antioxidant Status in Transgenic Mouse Model of Alzheimer’s Disease
resolves10.1021/bi973162p
Selective Inactivation of Parvulin-Like Peptidyl-Prolyl <i>cis/trans</i> Isomerases by Juglone
resolves10.1074/jbc.M507760200
The Protein Phosphatase 2A Phosphatase Activator Is a Novel Peptidyl-Prolyl cis/trans-Isomerase
resolves10.1002/bab.1870
The antioxidant 2,3‐dichloro,5,8‐dihydroxy,1,4‐naphthoquinone inhibits acetyl‐cholinesterase activity and amyloid β<sub>42</sub>aggregation: A dual target therapeutic candidate compound for the treatment of Alzheimer's disease
resolves10.1016/j.foodchem.2005.05.019
Antioxidative and mutagenic properties of Zanthoxylum ailanthoides Sieb & zucc.
resolves10.1007/BF02977668
Monoamine oxidase inhibitory naphthoquinones from the roots ofLithospermum erythrorhizon
resolves10.1111/cbdd.12708
Evaluation of Natural and Synthetic 1,4‐naphthoquinones as Inhibitors of Monoamine Oxidase
resolves10.3892/mmr.2014.2040
Monoamine oxidase inhibitors: Promising therapeutic agents for Alzheimer’s disease (Review)
resolves10.1007/s11064-008-9775-9
Cellular Stress Response: A Novel Target for Chemoprevention and Nutritional Neuroprotection in Aging, Neurodegenerative Disorders and Longevity
resolves10.1021/acschemneuro.9b00093
Fluorescent 1,4-Naphthoquinones To Visualize Diffuse and Dense-Core Amyloid Plaques in APP/PS1 Transgenic Mouse Brains
resolves10.1021/jm200691d
Synthesis of Monomeric Derivatives To Probe Memoquin’s Bivalent Interactions
resolves10.1016/j.bmcl.2010.12.093
Multitargeted drugs discovery: Balancing anti-amyloid and anticholinesterase capacity in a single chemical entity
resolves10.1021/jm070559a
Novel Class of Quinone-Bearing Polyamines as Multi-Target-Directed Ligands To Combat Alzheimer's Disease
resolves10.1016/S0006-2952(02)01514-9
β-Amyloid aggregation induced by human acetylcholinesterase: inhibition studies
resolves10.1016/S0896-6273(00)80108-7
Acetylcholinesterase Accelerates Assembly of Amyloid-β-Peptides into Alzheimer's Fibrils: Possible Role of the Peripheral Site of the Enzyme
resolves10.1007/s12031-010-9416-z
Comparison of Pharmacological Modulation of APP Metabolism in Primary Chicken Telencephalic Neurons and in a Human Neuroglioma Cell Line
resolves10.1002/cmdc.201500104
Multitarget Therapeutic Leads for Alzheimer’s Disease: Quinolizidinyl Derivatives of Bi‐ and Tricyclic Systems as Dual Inhibitors of Cholinesterases and β‐Amyloid (Aβ) Aggregation
resolves10.1074/jbc.M804901200
Two Endoplasmic Reticulum (ER)/ER Golgi Intermediate Compartment-based Lysine Acetyltransferases Post-translationally Regulate BACE1 Levels
resolves10.1074/jbc.M111.310136
Biochemical Inhibition of the Acetyltransferases ATase1 and ATase2 Reduces β-Secretase (BACE1) Levels and Aβ Generation
resolves10.1001/jama.1994.03510370044030
Hepatotoxic Effects of Tacrine Administration in Patients With Alzheimer's Disease
resolves10.1016/j.bmcl.2013.02.017
Novel tacrine-related drugs as potential candidates for the treatment of Alzheimer’s disease
resolves10.1002/slct.201702781
Synthesis, Biological Assessment and Molecular Modeling of Racemic
<i>QuinoPyranoTacrines</i>
for Alzheimer's Disease Therapy
resolves10.1021/jm5010804
Multitarget Drug Design Strategy:
Quinone–Tacrine
Hybrids Designed To Block Amyloid‑β Aggregation and To
Exert Anticholinesterase and Antioxidant Effects
resolves10.1021/jm200840c
Huprine–Tacrine Heterodimers as Anti-Amyloidogenic Compounds of Potential Interest against Alzheimer’s and Prion Diseases
resolves10.1016/j.jmb.2005.04.016
Prediction of “Aggregation-prone” and “Aggregation-susceptible” Regions in Proteins Associated with Neurodegenerative Diseases
resolves10.1021/cn400197x
Atomic and Dynamic Insights into the Beneficial Effect of the 1,4-Naphthoquinon-2-yl-
<scp>l</scp>
-tryptophan Inhibitor on Alzheimer’s Aβ1–42 Dimer in Terms of Aggregation and Toxicity
resolves10.1016/j.nbd.2012.03.005
Naphthoquinone-tyrptophan reduces neurotoxic Aβ*56 levels and improves cognition in Alzheimer's disease animal model
resolves10.1002/prot.24080
Generic inhibition of amyloidogenic proteins by two naphthoquinone–tryptophan hybrid molecules
resolves10.1159/000448518
Cl-NQTrp Alleviates Tauopathy Symptoms in a Model Organism through the Inhibition of Tau Aggregation-Engendered Toxicity
resolves10.3233/JAD-150927
Naphthoquinone-Tryptophan Hybrid Inhibits Aggregation of the Tau-Derived Peptide PHF6 and Reduces Neurotoxicity
resolves10.1371/journal.pone.0167432
Selection and Characterization of Tau Binding ᴅ-Enantiomeric Peptides with Potential for Therapy of Alzheimer Disease
resolves10.1016/S0925-4439(00)00038-7
Structure of tau protein and assembly into paired helical filaments
resolves10.1021/jp309066p
Methylations of Tryptophan-Modified Naphthoquinone Affect Its Inhibitory Potential toward Aβ Aggregation
resolves10.1021/acschemneuro.9b00123
Antagonistic Activity of Naphthoquinone-Based Hybrids toward Amyloids Associated with Alzheimer’s Disease and Type-2 Diabetes
resolves10.1016/j.tips.2013.12.005
Chemical kinetics for drug discovery to combat protein aggregation diseases
resolves10.1038/s41598-017-18443-2
Mechanistic insights into remodeled Tau-derived PHF6 peptide fibrils by Naphthoquinone-Tryptophan hybrids
resolves10.1002/pro.87
9,10‐Anthraquinone hinders β‐aggregation: How does a small molecule interfere with Aβ‐peptide amyloid fibrillation?
resolves10.1016/j.bmcl.2014.05.008
Naturally occurring polyphenolic inhibitors of amyloid beta aggregation
resolves10.1371/journal.pone.0136528
Unraveling Comparative Anti-Amyloidogenic Behavior of Pyrazinamide and D-Cycloserine: A Mechanistic Biophysical Insight
resolves10.1039/C8FO01569D
Health functions and structure–activity relationships of natural anthraquinones from plants
resolves10.1016/j.jep.2016.06.037
Inhibitory activities of major anthraquinones and other constituents from Cassia obtusifolia against β-secretase and cholinesterases
resolves10.1515/znc-2008-5-610
Coumarin, Anthroquinone and Stilbene Derivatives with Anticholinesterase Activity
resolves10.1016/j.jep.2017.10.028
Morinda officinalis How. – A comprehensive review of traditional uses, phytochemistry and pharmacology
resolves10.3390/molecules22101638
Bioassay-Guided Isolated Compounds from Morinda officinalis Inhibit Alzheimer’s Disease Pathologies
resolves10.1074/jbc.M410984200
Anthraquinones Inhibit Tau Aggregation and Dissolve Alzheimer's Paired Helical Filaments in Vitro and in Cells
resolves10.1055/s-0033-1360180
Inhibition of Tau Aggregation by Three Aspergillus nidulans Secondary Metabolites: 2,ω-Dihydroxyemodin, Asperthecin, and Asperbenzaldehyde
resolves10.1007/s00018-019-03312-0
Purpurin modulates Tau-derived VQIVYK fibrillization and ameliorates Alzheimer’s disease-like symptoms in animal model
resolves10.1006/bbrc.2001.5116
Role of Cysteine-291 and Cysteine-322 in the Polymerization of Human Tau into Alzheimer-like Filaments
resolves10.1002/open.201800222
Anthraquinone Derivative Reduces Tau Oligomer Progression by Inhibiting Cysteine‐Cysteine Interaction
resolves10.2174/0929867304666220313105818
Inhibitors of Aβ Peptide Aggregation as Potential Anti-Aizheimer Agents
resolves10.1002/elps.200800377
CE can identify small molecules that selectively target soluble oligomers of amyloid β protein and display antifibrillogenic activity
resolves10.1021/jm9013407
Mitoxantrone Analogues as Ligands for a Stem−Loop Structure of Tau Pre-mRNA
resolves10.1016/j.bmc.2014.03.045
Novel aromatic–polyamine conjugates as cholinesterase inhibitors with notable selectivity toward butyrylcholinesterase
resolves10.1016/j.bioorg.2018.10.073
Assessment of novel azaanthraquinone derivatives as potent multi-target inhibitors of inflammation and amyloid-β aggregation in Alzheimer’s disease
resolves10.1016/j.bbrc.2007.03.056
High throughput screening for small molecule inhibitors of heparin-induced tau fibril formation
resolves10.1021/jm401824w
Synthesis and Multitarget Biological Profiling of a Novel Family of Rhein Derivatives As Disease-Modifying Anti-Alzheimer Agents
resolves10.4155/fmc-2017-0049
Design, Synthesis and Multitarget Biological Profiling of Second-Generation Anti-Alzheimer Rhein–Huprine Hybrids
resolves10.1039/C3OB42010H
Design, synthesis and evaluation of novel tacrine–rhein hybrids as multifunctional agents for the treatment of Alzheimer's disease
resolves10.3389/fnmol.2011.00019
Interactions of AChE with A? Aggregates in Alzheimer?s Brain: Therapeutic Relevance of IDN 5706
resolves10.2165/11539810-000000000-00000
Managing Cognitive Dysfunction through the Continuum of Alzheimerʼs Disease
resolves10.3390/molecules21040466
Navigating the Chemical Space of Multitarget-Directed Ligands: From Hybrids to Fragments in Alzheimer’s Disease
The 12 references without a DOI — listed, not checked
no DOI — not checkedAdelina, C. (2019). The costs of dementia: Advocacy, media and stigma. World Alzheimer Report 2019: Attitudes to Dementia, Alzheimer’s Disease International. Available online: https://www.alzint.org/u/WorldAlzheimerReport2019.pdf.
no DOI — not checkedUltrastructural studies in Alzheimer’s presenile dementia
no DOI — not checkedReview of the advances in treatment for Alzheimer disease: Strategies for combating β-amyloid protein
no DOI — not checkedAcetylcholinesterase: Mechanism of catalysis and inhibition
no DOI — not checkedAntibacterial and cytotoxic activities of naphthoquinone pigments from onosma Visianii clem
no DOI — not checkedOrganocatalytic asymmetric vinylogous addition to quinones—Formation of optically active α-aryl ketones
no DOI — not checkedAn evaluation of the extent and threat of bark harvesting of medicinal plant species in the venda region, limpopo province, south africa
no DOI — not checkedThe Chemistry of the Quinonoid Compounds
no DOI — not checkedNF-κB-regulated, proinflammatory miRNAs in Alzheimer’s disease
no DOI — not checkedJuglone suppresses epithelial-mesenchymal transition in prostate cancer cells via the protein kinase b/glycogen synthase kinase-3β/snail signaling pathway
no DOI — not checkedHuprine X is a novel high-affinity inhibitor of acetylcholinesterase that is of interest for treatment of Alzheimer’s disease
no DOI — not checkedTolerance and adverse events of treatment with acetylcholinesterase inhibitors in a clinical sample of patients with very slight and mild Alzheimer’s disease over a six-month period
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