Oxidative stress in Alzheimer’s disease

Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051

Role of Oxidative Stress in Development of Complications in Diabetes

Baynes, J. (1991) · Diabetes · doi:10.2337/diab.40.4.405 · Cited by 3,791

Hydrogen peroxide mediates amyloid β protein toxicity

Behl, C. (1994) · Cell · doi:10.1016/0092-8674(94)90131-7 · Cited by 2,074

RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease

Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012

Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975

beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity

Mattson, M. P., Cheng, B., Davis, D. G., Bryant, K., Lieberburg, I. M., & Rydel, R. E. (1992) · Journal of Neuroscience · doi:10.1523/jneurosci.12-02-00376.1992 · Cited by 1,633

Iron accumulation in Alzheimer disease is a source of redox-generated free radicals

Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,365

Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease.

Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., & Markesbery, W. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10540 · Cited by 1,296

Widespread Peroxynitrite-Mediated Damage in Alzheimer’s Disease

Smith, M. A., Richey Harris, P. L., Sayre, L. M., Beckman, J. S., & Perry, G. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-08-02653.1997 · Cited by 1,239

A Review of the Pathogenesis and Chinese Medicine Intervention of Alzheimer's Disease

Zhao, J., Yang, J., Li, D., Wang, F., & Li, L. (2022) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2201002 · Cited by 21

Anti-aggregation effects of thymoquinone against Alzheimers -amyloid in vitro

Ismail, N., Ismail, M., Shahid, I., & Latiff, L. A. (2013) · Journal of Medicinal Plants Research · doi:10.5897/jmpr10.852 · Cited by 21

The antioxidant xanthorrhizol prevents amyloid-β-induced oxidative modification and inactivation of neprilysin

Lim, C. S., & Han, J. (2018) · Bioscience Reports · doi:10.1042/bsr20171611 · Cited by 21

Quantification of antioxidant activity in brain tissue homogenates using the ‘total equivalent antioxidant capacity’

Shea, T. B., Rogers, E. J., Ashline, D. J., et al. (2003) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(03)00028-1 · Cited by 21

Apolipoprotein Aβ: Black Sheep in a Good Family

Kontush, A. (2004) · Brain Pathology · doi:10.1111/j.1750-3639.2004.tb00088.x · Cited by 21

Apple Phenolics Protect in Vitro Oxidative Stress‐induced Neuronal Cell Death

Heo, H. J., Kim, D., Choi, S. J., Shin, D. H., & Lee, C. Y. (2004) · Journal of Food Science · doi:10.1111/j.1365-2621.2004.tb09949.x · Cited by 21

The Oxidant Defense System in Human Neuroblastoma IMR-32 Cells Predifferentiation and Postdifferentiation to Neuronal Phenotypes

Erlejman, A. G., & Oteiza, P. I. (2002) · Neurochemical Research · doi:10.1023/a:1021600522299 · Cited by 21

Chemical composition and in vitro evaluation of antioxidant, antimicrobial, and enzyme inhibitory activities of Erucaria uncata and Thymeleae hirsuta

Djermane, N., Gali, L., Arhab, R., Gherraf, N., Bensouıcı, C., Erenler, R., Gök, M., & Abdessamed, A. (2020) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2020.101834 · Cited by 20

Associations between risk of Alzheimer's disease and obstructive sleep apnea, intermittent hypoxia, and arousal responses: A pilot study

Tsai, C.-Y., Wu, S., Kuan, Y., Lin, Y.-T., Hsu, C.-R., Hsu, W.-H., Liu, Y.-S., Majumdar, A., Stettler, M. E. J., Yang, C., et al. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.1038735 · Cited by 20

Innovative pathological network‐based multitarget approaches for Alzheimer's disease treatment

Mayo, P., Pascual-Guerra, J., Crisman, E., Domínguez, C., López, M. G., & Leon, R. M. (2024) · Medicinal Research Reviews · doi:10.1002/med.22045 · Cited by 19

Reduction of brain lipid peroxidation by CSF drainage in Alzheimer's disease patients

Praticò, D., Yao, Y., Rokach, J., et al. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6405 · Cited by 20

Photo-oxidation of cardiolipin and cytochrome c with bilayer-embedded Pc 4

Kim, J. H., Rodríguez, M. E., Oleinick, N. L., & Anderson, V. E. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.05.014 · Cited by 20

Chemically induced oxidative stress affects ASH neuronal function and behavior in C. elegans

Gourgou, E., & Chronis, N. (2016) · Scientific Reports · doi:10.1038/srep38147 · Cited by 22

Antioxidant and acetylcholinesterase inhibitory activities of ginger root ( Zingiber officinale Roscoe) extract

Tùng, B. T., Thu, D. K., Thu, N. T. K., et al. (2017) · Journal of Complementary and Integrative Medicine · doi:10.1515/jcim-2016-0116 · Cited by 20

Cell-line and culture model specific responses to organic contaminants in house dust: Cell bioenergetics, oxidative stress, and inflammation endpoints

dos Santos, M. M., Fei, M. T. P., Li, C., Jia, S., & Snyder, S. A. (2022) · Environment International · doi:10.1016/j.envint.2022.107403 · Cited by 19

Ginsenosides Rg1 and Rg2 Activate Autophagy and Attenuate Oxidative Stress in Neuroblastoma Cells Overexpressing Aβ(1-42)

Liu, Z., Cecarini, V., Cuccioloni, M., Bonfili, L., Gong, C., Angeletti, M., & Eleuteri, A. M. (2024) · Antioxidants · doi:10.3390/antiox13030310 · Cited by 21

Natural Antioxidants: An Effective Strategy for the Treatment of Alzheimer’s Disease at the Early Stage

Wang, Y., Huang, Y., Ma, A., You, J., Miao, J., & Li, J. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c01323 · Cited by 21

Aluminum and Gene Transcription in the Mammalian Central Nervous System — Implications for Alzheimer's Disease

Lukiw, W. J. (2001) · Elsevier eBooks · doi:10.1016/b978-044450811-9/50032-x · Cited by 19

Peripheral biomarkers of oxidative stress in aging and Alzheimer's disease

Marcourakis, T., Camarini, R., Kawamoto, E. M., Scorsi, L. R., & Scavone, C. (2008) · Dementia & Neuropsychologia · doi:10.1590/s1980-57642009dn20100002 · Cited by 21

Cyclooxygenase I and II inhibitors distinctly enhance hippocampal- and cortex-dependent cognitive functions in mice

Syed, H., Ikram, M. F., Yaqinuddin, A., & Ahmed, T. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.4351 · Cited by 19

Synthesis, biological evaluation and in silico molecular docking of novel 1-hydroxy-naphthyl substituted heterocycles

El‐Desoky, E. I., Keshk, E. M., El‐Sawi, A. A., et al. (2018) · Saudi Pharmaceutical Journal · doi:10.1016/j.jsps.2018.03.013 · Cited by 19

Role of simvastatin and insulin in memory protection in a rat model of diabetes mellitus and dementia

Fahim, V. F., Wadie, W., Shafik, A. N., & Attallah, M. I. (2018) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2018.10.012 · Cited by 19

Alzheimer’s Disease Markers in Aged ApoE-PON1 Deficient Mice

Narasimhulu, C. A., Mitra, C., Bhardwaj, D., Burge, K. Y., & Parthasarathy, S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180883 · Cited by 19

The ubiquitous role of mitochondria in Parkinson and other neurodegenerative diseases

Theocharopoulou, G. (2020) · AIMS neuroscience · doi:10.3934/neuroscience.2020004 · Cited by 19

Quantitation of the glutathione in human peripheral blood by matrix-assisted laser desorption ionization time-of-flight mass spectrometry coupled with micro-scale derivatization

Feng, C., Huang, H.-Y., & Lu, C. (2011) · Analytica Chimica Acta · doi:10.1016/j.aca.2011.02.015 · Cited by 19

Apolipoprotein E genotype is related to nitric oxide production in platelets

Marcourakis, T., Bahia, V. S., Kawamoto, E. M., Munhoz, C. D., Gorjão, R., Artes, R., Kok, F., Caramelli, P., Nitríni, R., Curi, R., et al. (2008) · Cell Biochemistry and Function · doi:10.1002/cbf.1516 · Cited by 19

Functional and Morphological Olfactory Bulb Modifications in Mice after Vanadium Inhalation

Colín-Barenque, L., Pedraza‐Chaverrí, J., Medina‐Campos, O. N., Jimenez‐Martínez, R., Bizarro‐Nevares, P., González-Villalva, A. E., Lemus, M. R., & van der Goes, T. I. F. (2014) · Toxicologic Pathology · doi:10.1177/0192623314548668 · Cited by 20

Designed Amyloid β Peptide Fibril—A Tool for High‐Throughput Screening of Fibril Inhibitors

Dolphin, G. T., Ouberai, M. M., Dumy, P., & Garcia, J. (2007) · ChemMedChem · doi:10.1002/cmdc.200700103 · Cited by 19

Rapid Characterization of Amyloid-β Side-Chain Oxidation by Tandem Mass Spectrometry and the Scoring Algorithm for Spectral Analysis

Schiewe, A. J., Margol, L., Soreghan, B. A., Thomas, S. N., & Yang, A. J. (2004) · Pharmaceutical Research · doi:10.1023/b:pham.0000032994.36343.02 · Cited by 19

Synthesis, characterization, biological evaluation, BSA binding properties, density functional theory and molecular docking study of Schiff bases

Joksimović, N., Petronijević, J., Ćoćić, D., Janković, N., Milović, E., Kosanić, M., & Petrović, N. (2021) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2021.130952 · Cited by 20

Zinc Ortho Methyl Carbonodithioate Improved Pre and Post-Synapse Memory Impairment via SIRT1/p-JNK Pathway against Scopolamine in Adult Mice

Jahan, R., Yousaf, M., Khan, H., Shah, S. A., Khan, A. A., Bibi, N., Javed, F. T., Ijaz, M., Ali, A., & Wei, D.-Q. (2023) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-023-10067-w · Cited by 18

GUIDED NANOSTRUCTURES USING ANODIZED ALUMINUM OXIDE TEMPLATES

Noh, K., Brammer, K. S., Seong, T., et al. (2011) · NANO · doi:10.1142/s1793292011002883 · Cited by 18

The case for iron chelation and/or antioxidant therapy in Alzheimer's disease

Malecki, E. A., & Connor, J. R. (2002) · Drug Development Research · doi:10.1002/ddr.10105 · Cited by 18

Anti-Inflammatory and Cytoprotective Effects of TMC-256C1 from Marine-Derived Fungus Aspergillus sp. SF-6354 via up-Regulation of Heme Oxygenase-1 in Murine Hippocampal and Microglial Cell Lines

Kim, D., Cho, K. H., Ko, W., Yoon, C., Sohn, J., Yim, J. H., Kim, Y., & Oh, H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17040529 · Cited by 19

Nomenclature and general classification of antioxidant activity/capacity assays

Sun, Y., Yang, C., & Tsao, R. (2017) · Wiley eBooks · doi:10.1002/9781119135388.ch1 · Cited by 18

Influence of crowding and surfaces on protein amyloidogenesis: A thermo-kinetic perspective.

Menon, S., & Sengupta, N. (2019) · Biochimica et Biophysica Acta - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.03.009 · Cited by 13

Vitamin C attenuates memory loss induced by post-traumatic stress like behavior in a rat model

Alzoubi, K. H., Shatnawi, A. F., Alqudah, M. A. Y., & Alfaqih, M. A. (2019) · Behavioural Brain Research · doi:10.1016/j.bbr.2019.112350 · Cited by 18

N-Acetylcysteine Prevents 4-Hydroxynonenal- and Amyloid-β-Induced Modification and Inactivation of Neprilysin in SH-SY5Y Cells

Wang, R., Malter, J. S., & Wang, D.-S. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1226 · Cited by 18

A novel single-site manganese(ii) complex of a pyridine derivative as a catalase mimetic for disproportionation of H2O2 in water

Zienkiewicz‐Machnik, M., Szlachetko, J., Lothschütz, C., et al. (2013) · Dalton Transactions · doi:10.1039/c3dt50288k · Cited by 18

A simple isotopic labeling method to study cysteine oxidation in Alzheimer’s disease: oxidized cysteine-selective dimethylation (OxcysDML)

Gu, L., & Robinson, R. A. S. (2016) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-016-9307-4 · Cited by 18

Evaluation of 2-amino-6-nitrobenzothiazole derived hydrazones as acetylcholinesterase inhibitors: in vitro assays, molecular docking and theoretical ADMET prediction

Tripathi, R. K. P., & Ayyannan, S. R. (2017) · Medicinal Chemistry Research · doi:10.1007/s00044-017-2095-3 · Cited by 18

Antioxidant Activity of Daemonorops draco Resin

Purwanti, S., Wahyuni, W. T., & Batubara, I. (2019) · Jurnal Kimia Sains dan Aplikasi · doi:10.14710/jksa.22.5.179-183 · Cited by 18

Isoprostane F2alpha-VI, a new marker of oxidative stress, increases following light damage to the mouse retina.

Dentchev, T., Yao, Y., Praticò, D., & Dunaief, J. L. (2007) · PubMed Central · Cited by 18

20S proteasome mediated degradation of DHFR: implications in neurodegenerative disorders

Amici, M., Sagratini, D., Pettinari, A., et al. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.12.014 · Cited by 18

Efficacy of vitamin E, phosphatidyl choline, and pyruvate on buffering neuronal degeneration and oxidative stress in cultured cortical neurons and in central nervous tissue of apolipoprotein E-deficient mice

Shea, T. B., Ekinci, F. J., Ortiz, D., et al. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00872-9 · Cited by 18

Suppression of tau‐induced phenotypes by vitamin E demonstrates the dissociation of oxidative stress and phosphorylation in mechanisms of tau toxicity

Cowan, C. M., Sealey, M. A., & Mudher, A. K. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15253 · Cited by 17

Enfektif Hastalıklarda Oksidan ve Antioksidan Parametrelerin Rolü: Sistematik Bir Literatür Değerlendirmesi

Çenesiz, S. (2020) · Kafkas Universitesi Veteriner Fakultesi Dergisi · doi:10.9775/kvfd.2020.24618 · Cited by 18

Alleviating the unwanted effects of oxidative stress on Aβ clearance: a review of related concepts and strategies for the development of computational modelling

Somin, S., Kulasiri, D., & Samarasinghe, S. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00344-2 · Cited by 18

Neuroprotective effects of vinpocetine, as a phosphodiesterase 1 inhibitor, on long-term potentiation in a rat model of Alzheimer’s disease

Shekarian, M., Salehi, I., Raoufi, S., Asadbegi, M., Kourosh‐Arami, M., & Komaki‬, A. (2023) · BMC Neuroscience · doi:10.1186/s12868-023-00790-8 · Cited by 18

Plasma and cerebrospinal fluid nonenzymatic protein damage is sustained in Alzheimer's disease

Dakterzada, F., Jové, M., Cantero, J. L., Pamplona, R., & Piñoll‐Ripoll, G. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102772 · Cited by 17

Comparison of scopolamine-induced cognitive impairment responses in three different ICR stocks

Yoon, W. B., Choi, H. J., Kim, J. E., Park, J. W., Kang, M. J., Bae, S. J., Lee, Y. J., Choi, Y. S., Kim, K., Jung, Y.-S., et al. (2018) · Laboratory Animal Research · doi:10.5625/lar.2018.34.4.317 · Cited by 17

Mechanical properties of RBCs under oxidative stress measured by optical tweezers

Liu, J., Zhang, F., Zhu, L., et al. (2019) · Optics Communications · doi:10.1016/j.optcom.2019.02.060 · Cited by 17

Genome instability biomarkers and blood micronutrient risk profiles associated with mild cognitive impairment and Alzheimer's disease

Lee, S. L., Thomas, P., & Fenech, M. F. (2015) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2014.12.012 · Cited by 18

Chronic Exposure to High Levels of Zinc or Copper has Little Effect on Brain Metal Homeostasis or Aβ Accumulation in Transgenic APP-C100 Mice

Maynard, C. J., Cappai, R., Volitakis, I., Laughton, K. M., Masters, C. L., Bush, A. I., & Li, Q. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9401-7 · Cited by 17

The potential of antioxidant activity of methanolic extract of Coscinium fenestratum (Goetgh.) Colebr (Menispermaceae)

Karthika, K., Gangadharan, G., Jamuna, S., Paulsamy, S., Ali, M. A., Al-Hemaid, F. M. A., Elshikh, M. S., & Lee, J. (2018) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2018.08.010 · Cited by 17

Apolipoprotein E isoform‐specific disruption of phosphoinositide hydrolysis: protection by estrogen and glutathione

Cedazo-Mínguez, Á., & Cowburn, R. F. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02761-2 · Cited by 17

pH Effects on the Conformational Preferences of Amyloid β‐Peptide (1–40) in HFIP Aqueous Solution by NMR Spectroscopy

Valerio, M., Porcelli, F., Zbilut, J. P., Giuliani, A., Manetti, C., & Conti, F. (2008) · ChemMedChem · doi:10.1002/cmdc.200700324 · Cited by 18

Role of Metals in Neuronal Apoptosis: Challenges Associated with Neurodegeneration

Ravid, R., & Rao, K. S. J. (2006) · Current Alzheimer Research · doi:10.2174/156720506778249399 · Cited by 18

Synthetic β-hydroxy ketone derivative inhibits cholinesterases, rescues oxidative stress and ameliorates cognitive deficits in 5XFAD mice model of AD

Ahmad, S. I., Ali, G., Muhammad, T., Ullah, R., Umar, M. N., & Hashmi, A. N. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05997-0 · Cited by 16

The impact of chronic stress on intracellular redox balance: A systems level analysis

Geddie, H., Cairns, M., Smith, L., van Wyk, M., Beselaar, L., Truter, N., Rautenbach, F., Marnewick, J. L., Joseph, D. E., & Essop, M. F. (2023) · Physiological Reports · doi:10.14814/phy2.15640 · Cited by 17

Botany, traditional uses, phytochemistry, pharmacological activities, and toxicity of the mangrove plant Avicennia marina: a comprehensive review

Zhou, P., Hu, H., Wu, X., Feng, Z., Li, X., Tavakoli, S., Wu, K., Deng, L.-M., & Luo, H. (2025) · Phytochemistry Reviews · doi:10.1007/s11101-025-10080-2 · Cited by 18

A single-component yet multifunctional tongue-mimicking sensor array for upconversion fluorescence biosensing

Wang, Q., Fang, Z.-Q., Wu, Y., et al. (2020) · The Analyst · doi:10.1039/d0an01641a · Cited by 16

Perspective insights of repurposing the pleiotropic efficacy of statins in neurodegenerative disorders: An expository appraisal

Bhat, A., Dalvi, H., Jain, H., Rangaraj, N., Singh, S. B., & Srivastava, S. (2020) · Current Research in Pharmacology and Drug Discovery · doi:10.1016/j.crphar.2020.100012 · Cited by 17

Effects of 4-Hydroxy-Nonenal and Amyloid-β on Expression and Activity of Endothelin Converting Enzyme and Insulin Degrading Enzyme in SH-SY5Y Cells

Wang, R., Wang, S., Malter, J. S., & Wang, D.-S. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1066 · Cited by 16

Neuroprotective effect of Picholine virgin olive oil and its hydroxycinnamic acids component against β-amyloid-induced toxicity in SH-SY5Y neurotypic cells

Villareal, M. O., Sasaki, K., Margout, D., Savry, C., Almaksour, Z., Larroque, M., & Isoda, H. (2016) · Cytotechnology · doi:10.1007/s10616-016-9980-3 · Cited by 17

Multi-functional neuroprotective activity of neohesperidin dihydrochalcone: a novel scaffold for Alzheimer's disease therapeutics identified via drug repurposing screening

Chakraborty, S., Rakshit, J., Bandyopadhyay, J., et al. (2018) · New Journal of Chemistry · doi:10.1039/c8nj00853a · Cited by 16

Attenuation of hydrogen peroxide-induced oxidative stress in SH-SY5Y cells by three flavonoids from Acer okamotoanum

Kim, J. H., Quilantang, N. G., Kim, H. Y., Lee, S., & Cho, E. J. (2018) · Chemical Papers · doi:10.1007/s11696-018-0664-7 · Cited by 16

A Diet Enriched in Palmitate and Deficient in Linoleate Exacerbates Oxidative Stress and Amyloid-β Burden in the Hippocampus of 3xTg-AD Mouse Model of Alzheimer’s Disease

Marwarha, G., Larson, K., Lund, J., Schommer, J., & Ghribi, O. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180835 · Cited by 16

Serum antioxidant vitamins and malondialdehyde levels in patients with obsessive-compulsive disorder

Shohag, M. H., Ullah, M. A., Azad, M. A. K., et al. (2012) · Cited by 16

α-Glycerylphosphorylethanolamine rescues astrocytes from mitochondrial impairment and oxidative stress induced by amyloid β-peptides

Bisaglia, M. (2003) · Neurochemistry International · doi:10.1016/s0197-0186(03)00131-1 · Cited by 16

The status of ongoing trials for mild cognitive impairment

Sramek, J. J., Veroff, A. E., & Cutler, N. R. (2001) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.10.4.741 · Cited by 16

Unraveling the Molecular Mechanisms Behind the Metabolic Basis of Sporadic Alzheimer's Disease

Erol, A. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2009-1047 · Cited by 30

The Evolution of AChE Inhibitors in Alzheimer's Disease: From Single‐Target to Multi‐Target Ligands

Mehta, N. V., Kapadia, A., Khambete, M., & Abhyankar, A. N. (2025) · ChemBioChem · doi:10.1002/cbic.202500053 · Cited by 20

A comprehensive review on RAGE-facilitated pathological pathways connecting Alzheimer’s disease, diabetes mellitus, and cardiovascular diseases

Chakraborty, A., Sami, S. A., & Marma, K. K. S. (2021) · The Egyptian Journal of Internal Medicine · doi:10.1186/s43162-021-00081-w · Cited by 18

Road to Alzheimer’s Disease: The Pathomechanism Underlying

Anand, R., Kaushal, A., Wani, W. Y., & Gill, K. D. (2011) · Pathobiology · doi:10.1159/000332218 · Cited by 16

Disruption of mitochondrial redox homeostasis by enzymatic activation of a trialkylphosphine probe

Nguyen, J., Tirla, A., & Rivera‐Fuentes, P. (2021) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob02259d · Cited by 14

Epigenetic plasticity and redox regulation of neural stem cell state and fate

Tay, E. X. Y., Chia, K., & Ong, D. S. T. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.030 · Cited by 15

Synthesis and biological evaluation of benzimidazoles/1,3,5-triazine-2,4-diamine hybrid compounds: a new class of multifunctional alzheimer targeting agents

Karimian, S., Shekouhy, M., Pirhadi, S., Iraji, A., Attarroshan, M., Edraki, N., & Khoshneviszadeh, M. (2022) · New Journal of Chemistry · doi:10.1039/d2nj00371f · Cited by 15

Estrés oxidativo, péptido β-amiloide y enfermedad de Alzheimer

Manzano‐León, N., & Mas‐Oliva, J. (2006) · Gaceta Médica de México · Cited by 16

Oxidative damage increased in presenilin1/presenilin2 conditional double knockout mice

Zhang, D.-L., Chen, Y.-Q., Xu, J., Ji, T., & Mei, B. (2009) · Neuroscience Bulletin · doi:10.1007/s12264-009-0114-1 · Cited by 15

Aspergillus flavus as a Model System to Test the Biological Activity of Botanicals: An Example on Citrullus colocynthis L. Schrad. Organic Extracts

Degola, F., Marzouk, B., Gori, A., et al. (2019) · Toxins · doi:10.3390/toxins11050286 · Cited by 15

Immunohistochemical detection of 8-hydroxy-2′-deoxyguanosine in gallbladder epithelium of patients with pancreaticobiliary maljunction

Otani, K., Shimizu, S., Chijiiwa, K., et al. (2001) · European Journal of Gastroenterology & Hepatology · doi:10.1097/00042737-200111000-00016 · Cited by 15

The neuroprotective effects of Liuwei Dihuang medicine in the APP/PS1 mouse model are dependent on the PI3K/Akt signaling pathway

Yuan, Y., Liu, Y., Li, H., Ma, J., Shao, S., Yu, Z., Shi, M. M., Zhang, Z., & Zhang, Z. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1188893 · Cited by 15

Molecular Neuropathogenesis of Alzheimer‘s Disease: An Interaction Model Stressing the Central Role of Oxidative Stress

Rodrigues, R., Smith, M. A., Wang, X., Perry, G. L., Lee, H., Zhu, X., & Petersen, R. B. (2012) · Future Neurology · doi:10.2217/fnl.12.27 · Cited by 14

An Acetate Prodrug of a Pyridinol-Based Vitamin E Analogue

Khdour, O. M., Lu, J., & Hecht, S. M. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0491-9 · Cited by 14

Methyl Jasmonate: Behavioral and Molecular Implications in Neurological Disorders

Aluko, O. M., Iroegbu, J. D., Ijomone, O. M., & Umukoro, S. (2021) · Clinical Psychopharmacology and Neuroscience · doi:10.9758/cpn.2021.19.2.220 · Cited by 14

Comparative Analyses of DHA‐Phosphatidylcholine Forage and Liposomes on Alzheimer's Disease in SAMP8 Mice

Meng, J., Zhou, M., Wang, C., Xue, C., Zhang, T., & Wang, Y. (2019) · European Journal of Lipid Science and Technology · doi:10.1002/ejlt.201800524 · Cited by 14

Distinct mechanisms account for β-amyloid toxicity in PC12 and differentiated PC12 neuronal cells

Sung, Y.-J., Cheng, C.-L., Chen, C.-S., Huang, H.-B., Huang, F.-L., Wu, P.-C., Shiao, M., & Tsay, H.-J. (2003) · Journal of Biomedical Science · doi:10.1007/bf02256429 · Cited by 14

Combined Structure and Ligand-Based Design of Selective Acetylcholinesterase Inhibitors

Pérez‐Sánchez, H., den-Haan, H., Pérez-Garrido, A., Peña-García, J. J., Chakraborty, S., Orhan, İ. E., Şenol, F. S., & Villalgordo, J. M. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00463 · Cited by 14

A laser Raman tweezers study of eryptosis

Barkur, S., Mathur, D., & Chidangil, S. (2018) · Journal of Raman Spectroscopy · doi:10.1002/jrs.5361 · Cited by 13

Potential of Ramalin and Its Derivatives for the Treatment of Alzheimer’s Disease

Kim, T. K., Hong, J., Kim, K., Han, S. J., Kim, I., Oh, H., & Yim, J. H. (2021) · Molecules · doi:10.3390/molecules26216445 · Cited by 13

Superoxide dismutase activity in the mongolian gerbil brain after acute poisoning with aluminum

Mićić, D. V., Petronijević, N., & Vučetić, S. S. (2003) · Journal of Alzheimer s Disease · doi:10.3233/jad-2003-5107 · Cited by 14

Time for a Change in the Research Paradigm for Alzheimer's Disease: The Value of a Chaotic Matrix Modeling Approach

Hunter, S., Friedland, R. P., & Brayne, C. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2009.00117.x · Cited by 13

Causes of Alzheimer’s disease: paracetamol (acetaminophen) today? Amphetamines tomorrow?

Jones, G. R. N. (2001) · Medical Hypotheses · doi:10.1054/mehy.2000.1235 · Cited by 13

MINI-COGNITIVE TESTING IN PATIENTS WITH AGE-RELATED MACULAR DEGENERATION

Al-Salem, K. M., & Schaal, S. (2013) · Retina · doi:10.1097/iae.0000000000000006 · Cited by 13

Adaptative response to enhanced basal oxidative damage in sod mutants from Saccharomyces cerevisiae

Manfredini, V., Martins, V., Peralba, M. D. C. R., & Benfato, M. S. (2005) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-005-4058-0 · Cited by 13

Cordycepin, a bioactive compound from Cordyceps spp ., moderates Alzheimer’s disease-associated pathology via anti-oxidative stress and autophagy activation

Sorraksa, N., Heebkaew, N., Promjantuek, W., Kunhorm, P., Kaokean, P., Chaicharoenaudomung, N., & Noisa, P. (2023) · Journal of Asian Natural Products Research · doi:10.1080/10286020.2023.2258797 · Cited by 13

The Impact of HIV on Early Brain Aging—A Pathophysiological (Re)View

Lazăr, M., Moroti, R., Barbu, E. C., Chițu, C. E., Tilişcan, C., Erculescu, T. M., Rosca, R. R., Frasila, S., Schmilevschi, E. T., Simion, V., et al. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13237031 · Cited by 12

Development of HuperTacrines as Non-Toxic, Cholinesterase Inhibitors for the Potential Treatment of Alzheimer’s Disease

Chioua, M., Pérez, M., Bautista‐Aguilera, Ó. M., Yáñez, M., López, M. G., Romero, A., Cacabelos, R., de la Bellacasa, R. P., Brogi, S., Butini, S., et al. (2015) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557515666150219130156 · Cited by 12

Free Radicals and Oxidative Stress in Neurodegenerative Disorders

Nigam, D. (2014) · Springer eBooks · doi:10.1007/978-81-322-2035-0_11 · Cited by 13

[The role of apolipoprotein E in the pathogenesis of Alzheimer disease].

Okuizumi, K. (1999) · PubMed · Cited by 1

Diagnostic criteria for primary progressive mutiple sclerosis: a position paper.

(2000) · Pure Amsterdam UMC · doi:10.1002/1531-8249(200006)47:6 · Cited by 2

Distribution of apolipoprotein E in senile plaques in brains with Alzheimer's disease: investigation with the confocal laser scan microscope

Nishiyama, E., Iwamoto, N., Ohwada, J., & Arai, H. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01329-7 · Cited by 18

Apolipoprotein E Interaction with the Neurofibrillary Tangles and Senile Plaques in Alzheimer Disease: Implications for Disease Pathogenesis

Richey, P. L., Siedlak, S. L., Smith, M. A., & Perry, G. L. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.1389 · Cited by 72

Presenilin and Amyloidogenesis: A Structure-Function Relationship Study on Presenilin 2

Iwatsubo, T., Tomita, T., Watabiki, T., Takikawa, R., Morohashi, Y., & Takasugi, N. (2002) · Advances in behavioral biology · doi:10.1007/978-0-306-47593-1_11