A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease.

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619

The molecular pathology of Alzheimer's disease

Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708

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

Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state

Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417

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

Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.

Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014

Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia/reperfusion-induced injury to gerbil brain.

Oliver, C., Starke-Reed, P. E., Stadtman, E. R., Liu, G. J., Carney, J. M., & Floyd, R. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5144 · Cited by 771

Reversal of age-related increase in brain protein oxidation, decrease in enzyme activity, and loss in temporal and spatial memory by chronic administration of the spin-trapping compound N-tert-butyl-alpha-phenylnitrone.

Carney, J. M., Starke-Reed, P. E., Oliver, C., Landum, R. W., Cheng, M. S., Wu, J., & Floyd, R. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.9.3633 · Cited by 724

Free radical damage to protein and DNA: Mechanisms involved and relevant observations on brain undergoing oxidative stress

Floyd, R. A., & Carney, J. M. (1992) · Annals of Neurology · doi:10.1002/ana.410320706 · Cited by 539

β-Amyloid precursor protein metabolites and loss of neuronal Ca2+ homeostasis in Alzheimer's disease

Mattson, M. P., Barger, S. W., Cheng, B., Lieberburg, I. M., Smith‐Swintosky, V. L., & Rydel, R. E. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90009-b · Cited by 518

Abnormal amyloid precursor protein processing in periodontal tissue in a murine model of periodontitis induced by Porphyromonas gingivalis

Shen, H., Jiang, Y., Qiu, C., Xie, X., Zhang, H., He, Z., Song, Z., & Zhou, W. (2024) · Journal of Periodontal Research · doi:10.1111/jre.13224 · Cited by 14

Design of Multi-Target drugs of HDACs and other Anti-Alzheimer related Targets: Current strategies and future prospects in Alzheimer’s diseases therapy

Soltan, O. M., Abdelrahman, K. S., Bass, A. K. A., Takizawa, K., Narumi, A., & Konno, H. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107651 · Cited by 14

Nose-to-brain delivery of DHA-loaded nanoemulsions: A promising approach against Alzheimer’s disease

Otaegui, L., Urgin, T., Zaiter, T., Zussy, C., Vitalis, M., Pellequer, Y., Acar, N., Vigor, C., Galano, J., Durand, T., et al. (2025) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2024.125125 · Cited by 14

Human Serum Albumin-Inspired Glycopeptide-Based Multifunctional Inhibitor of Amyloid-β Toxicity

Roy, R., Pradhan, K., Khan, J., Das, G., Mukherjee, N., Das, D., & Ghosh, S. (2020) · ACS Omega · doi:10.1021/acsomega.0c01028 · Cited by 14

Absence of Pannexin 1 Stabilizes Hippocampal Excitability After Intracerebral Treatment With Aβ (1-42) and Prevents LTP Deficits in Middle-Aged Mice

Südkamp, N., Shchyglo, O., & Manahan‐Vaughan, D. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.591735 · Cited by 14

Royal jelly improves learning and memory deficits in an amyloid β-induced model of Alzheimer's disease in male rats: Involvement of oxidative stress

Raoufi, S., Salavati, Z., Komaki‬, A., Shahidi, ‬., & Zarei, M. (2023) · Metabolic Brain Disease · doi:10.1007/s11011-023-01168-9 · Cited by 14

Natural Compounds (Small Molecules) as Potential and Real Drugs of Alzheimer's Disease

Cahlíková, L., Macáková, K., Benešová, N., Chlebek, J., Hošťálková, A., & Opletal, L. (2014) · Studies in natural products chemistry · doi:10.1016/b978-0-444-63281-4.00006-9 · Cited by 14

Anti-Inflammatory Properties of Acetylcholinesterase Inhibitors Administred in Alzheimers Disease

Kamal, M. A., Greig, N. H., & Reale, M. (2009) · Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry · doi:10.2174/187152309787580810 · Cited by 14

Role of amyloid β peptides in the regulation of central cholinergic function and its relevance to Alzheimer's disease pathology

Kar, S. (2002) · Drug Development Research · doi:10.1002/ddr.10080 · Cited by 14

Neprilysin protects human neuronal progenitor cells against impaired development caused by amyloid-β peptide

Mazur‐Kolecka, B., & Frackowiak, J. (2006) · Brain Research · doi:10.1016/j.brainres.2006.09.064 · Cited by 14

The protective role of dl-α-lipoic acid in biogenic amines catabolism triggered by Aβ amyloid vaccination in mice

Jesudason, E. P., Masilamoni, J. G., Kirubagaran, R., Dicky John Davis, G., & Rajadas, J. (2005) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2005.01.010 · Cited by 14

Amyloid β-peptide alters thrombin-induced calcium responses in cultured human neural cells

Mattson, M. P., & Begley, J. G. (1996) · Amyloid · doi:10.3109/13506129609014352 · Cited by 14

The Role of Aβ-Peptide on Spatial Memory, EEG, Auditory Evoked Potentials And Nicotinic Cholinergic Receptors in A/P Transgenic Mice

Wang, J. (2003) · Cited by 14

Impairment of Tricarboxylic Acid Cycle (TCA) Cycle in Alzheimer's Disease: Mechanisms, Implications, and Potential Therapies

Mohan, G. S., & Kumar, R. (2025) · Aging and Disease · doi:10.14336/ad.2025.0472 · Cited by 14

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

Curcumin and Homotaurine Suppress Amyloid-β25–35 Aggregation in Synthetic Brain Membranes

Zou, X., Himbert, S., Dujardin, A., Juhasz, J., Ros, S., Stöver, H. D. H., & Rheinstadter, M. C. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00057 · Cited by 13

A Revisit to Etiopathogenesis and Therapeutic Strategies in Alzheimer’s Disease

Kumar, M., & Bansal, N. (2021) · Current Drug Targets · doi:10.2174/1389450122666211118125233 · Cited by 14

Effect of Aged Garlic Extract on the Cytotoxicity of Alzheimer β-Amyloid Peptide in Neuronal PC12 Cells

Griffin, B., Selassie, M., & Gwebu, E. T. (2000) · Nutritional Neuroscience · doi:10.1080/1028415x.2000.11747310 · 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

Evidence against increased glycoxidation in patients with Alzheimer's disease

Seidl, R., Schüller, E., Cairns, N. J., & Lübec, G. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00576-4 · Cited by 13

The pyrrolopyrimidine U101033E is a potent free radical scavenger and prevents Fe(II)-induced lipid peroxidation in synaptosomal membranes

Lauderback, C. M., Breier, A. M., Hackett, J. M., Varadarajan, S., Goodlett-Mercer, J., & Butterfield, D. A. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00015-6 · Cited by 13

Aged garlic extract™ attenuates the cytotoxicity of β-amyloid on undifferentiated PC12 cells

Selassie, M., Griffin, B., Gwebu, N. T., & Gwebu, E. T. (1999) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1007/s11626-999-0109-2 · Cited by 13

Membrane-Modulating Drugs can Affect the Size of Amyloid-β25–35 Aggregates in Anionic Membranes

Khondker, A., Alsop, R. J., Himbert, S., Tang, J., Shi, A., Hitchcock, A. P., & Rheinstadter, M. C. (2018) · Scientific Reports · doi:10.1038/s41598-018-30431-8 · Cited by 13

THE ARTERIAL CHEMORECEPTORS

Hayashida, Y., Kondo, H., & González, C. (2006) · Advances in experimental medicine and biology · doi:10.1007/0-387-31311-7 · Cited by 13

Mitochondria-targeting by small molecules against Alzheimer's disease: A mechanistic perspective

Pal, C. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167617 · Cited by 12

Mechanistic and therapeutic implications of EphA‐4 receptor tyrosine kinase in the pathogenesis of Alzheimer's disease

Ganguly, D., Thomas, J. A., Ali, A., & Kumar, R. K. (2022) · European Journal of Neuroscience · doi:10.1111/ejn.15591 · Cited by 12

Oxidative Stress Events and Neuronal Dysfunction in Alzheimer’s Disease: Focus on APE1/Ref-1-Mediated Survival Strategies

Kaur, N., Sarkar, B., Mittal, S., Dhiman, M., Taglialatela, G., Perez‐Polo, R. J., & Mantha, A. K. (2014) · Springer eBooks · doi:10.1007/978-81-322-2035-0_13 · Cited by 12

Hydroxyl radical oxidation of guanosine 5′-triphosphate (GTP): requirement for a GTP–Cu(II) complex

Cerchiaro, G., Bolin, C. M., & Cardozo‐Pelaez, F. (2009) · Redox Report · doi:10.1179/135100009x392520 · Cited by 12

Cellular Protection and Therapeutic Potential of Tocotrienols

Catalgol, B., Batırel, S., & Özer, N. K. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211796957436 · Cited by 12

Unbiased Proteomic Approach Identifies Pathobiological Profiles in the Brains of Preclinical Models of Repetitive Mild Traumatic Brain Injury, Tauopathy, and Amyloidosis

Ojo, J. O., Crynen, G. C., Algamal, M., Vallabhaneni, P., Leary, P., Mouzon, B., Reed, J. M., MULLAN, M. J., & Crawford, F. (2020) · ASN NEURO · doi:10.1177/1759091420914768 · Cited by 12

Testing the amyloid toxicity hypothesis of alzheimer's disease in transgenic Caenorhabditis elegans model

Gutierrez-Zepeda, A. (2004) · Frontiers in bioscience · doi:10.2741/1485 · Cited by 12

Pharmacokinetics and tolerability of ventricularly administered superoxide dismutase in monkeys and preliminary clinical observations in familial ALS

Smith, R. A., Balis, F. M., Ott, K. H., Elsberry, D. D., Sherman, M. R., & Saifer, M. G. P. (1995) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(95)00051-3 · Cited by 12

Expression of Adult T Cell Leukemia-Derived Factor in Human Brain and Peripheral Nerve Tissues

Asahina, M., Yamada, T., Yoshiyama, Y., & Yodoi, J. (1998) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000017044 · Cited by 12

Managed care: II. some "latent functions"

Bachrach, L. L. (1996) · Psychiatric Services · doi:10.1176/ps.47.3.243 · Cited by 12

The Role of Oxidative Processes and Metal Ions in Aging and Alzheimer’s Disease

Shinobu, L. A., & Beal, M. F. (1997) · Springer eBooks · doi:10.1007/978-1-4899-0197-2_13 · Cited by 12

Are Hippocampal Hypoperfusion and ATP Depletion Prime Movers in the Genesis of Alzheimer’s Disease? A Review of Recent Pertinent Observations from Molecular Biology

Walker, V. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157328 · Cited by 11

Inhibitors of the Maillard Reaction

Colaco, C. A. L. S., & Harrington, C. R. (1996) · CNS Drugs · doi:10.2165/00023210-199606030-00001 · Cited by 11

Salsolinol, a Tetrahydroisoquinoline Catechol Neurotoxin, Induces Human Cu,Zn-superoxidie Dismutase Modificaiton

Kang, J. (2007) · BMB Reports · doi:10.5483/bmbrep.2007.40.5.684 · Cited by 11

Generation and propagation of yeast prion [URE3] are elevated under electromagnetic field

Lian, H., Lin, K., Yang, C., & Cai, P. (2017) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0867-9 · Cited by 11

Prevention and Therapy of Neurodegenerative Disorders: Role of Nutritional Antioxidants

Matteo, V. D., Pierucci, M., Giovanni, G. D., & Esposito, E. (2007) · Elsevier eBooks · doi:10.1016/b978-044452809-4/50168-x · Cited by 11

EPR evidence of hydroxyl radical generation as an initiator of lipid peroxidation in amyloid β-protein-stimulated PC12 cells

Hayashi, Y., Ueda, Y., Nakajima, A., & Mitsuyama, Y. (2004) · Brain Research · doi:10.1016/j.brainres.2004.07.067 · Cited by 11

Different Changes in Concentrations of Monoamines and Their Metabolites and Amino Acids in Various Brain Regions by the Herbal Medicine/Toki-Shakuyaku-San Between Female and Male Senescence-Accelerated Mice (SAMP8)

Komatsu, M., Ueda, Y., & Hiramatsu, M. (1999) · Neurochemical Research · doi:10.1023/a:1020945611673 · Cited by 11

Altered response to mirtazapine on gene expression profile of lymphocytes from Alzheimer's patients

Palotás, A., Puskás, L. G., Kitajka, K., Palotás, M., Molnár, J., Pákáski, M., Janka, Z., Penke, B., & Kalman, J. L. (2004) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2004.06.059 · Cited by 11

Untangling Alzheimer's disease from fibrous lesions of neurofibrillary tangles and senile plaques

Mori, H. (2000) · Neuropathology · doi:10.1046/j.1440-1789.2000.00317.x · Cited by 10

The Unexpected Capability of Melanin to Split the Water Molecule and the Alzheimer’s Disease

Arias-Esparza, M. D. C., Arias, R. I. S., Arias, P. E. S., Arias, M. P. S., & Solís-Herrera, A. (2011) · Neuroscience & Medicine · doi:10.4236/nm.2011.23029 · Cited by 10

Combination of Aβ clearance and neurotrophic factors as a potential treatment for Alzheimer’s disease

Lin, L.-F., Liao, M., Xue, X., Zhang, W., Yan, L., Cai, L., Zhou, X., Zhou, X., & Luo, H. (2012) · Neuroscience Bulletin · doi:10.1007/s12264-012-1287-6 · Cited by 10

Delivery systems for antioxidant nutrients

Takata, J., Matsunaga, K., & Karube, Y. (2002) · Toxicology · doi:10.1016/s0300-483x(02)00390-6 · Cited by 10

Molecular mechanisms of neurodegeneration mediated by dysfunctional subcellular organelles in transmissible spongiform encephalopathies

Song, Z., Zhao, D., & Yang, L. (2013) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmt014 · Cited by 10

Analysis of the antioxidant activity of 4-(5-chloro-2-hydroxyphenylamino)-4-oxobut-2-enoic acid derivatives using quantum-chemistry descriptors and molecular docking

Ardjani, T. E. A., & Mekelleche, S. M. (2016) · Journal of Molecular Modeling · doi:10.1007/s00894-016-3160-4 · Cited by 10

Cheminformatic modelling of β-amyloid aggregation inhibitory activity against Alzheimer's disease

Kumar, V., Ojha, P. K., Saha, A., & Roy, K. (2020) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2020.103658 · Cited by 10

ONO‐Pincer‐Type Coumarin‐Based Copper(II) Metalates: Effect on Alzheimer's Disease Pathologies in Caenorhabditis elegans

Kalaiarasi, G., Mohankumar, A., Dharani, S., Dallemer, F., Sundararaj, P., & Prabhakaran, R. (2021) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202100039 · Cited by 10

Area-Specific Differences in OH8dG and mtDNA4977 Levels in Alzheimer Disease Patients and Aged Controls

Lezza, A. M. S., Mecocci, P., Cormio, A., Beal, M. F., Cherubini, A., Cantatore, P., Senin, U., & Gadaleta, M. N. (1999) · Rejuvenation Research · doi:10.1089/rej.1.1999.2.209 · Cited by 10

β-Amyloid1–40 inhibits electrically stimulated release of [3H]norepinephrine and enhances the internal calcium response to low potassium in rat cortex: Prevention with a free radical scavenger

Li, M., & Smith, C. P. (1996) · Brain Research Bulletin · doi:10.1016/0361-9230(96)00031-7 · Cited by 10

A? peptides and calcium influence secretion of the amyloid protein precursor from chick sympathetic neurons in culture

Mok, S. S., Clippingdale, A. B., Beyreuther, K. T., Masters, C. L., Barrow, C. J., & Small, D. H. (2000) · Journal of Neuroscience Research · doi:10.1002/1097-4547(20000815)61:4 · Cited by 10

Alzheimer's disease: inside, outside, upside down

Yan, S. D., Schmidt, A. M., & Stern, D. M. (2001) · Biochemical Society Symposia · doi:10.1042/bss0670015 · Cited by 10

Oxidative Stress in Alzheimer’s Disease

Ceballos-Picot, I. (1997) · Neuroscience intelligence unit · doi:10.1007/978-3-662-22516-5_5 · Cited by 10

Interactions of growth inhibitory factor with hydroxyl and superoxide radicals

Shi, Y., Wang, W., Mo, J., Du, L., Yao, S., & Tang, W. (2003) · BioMetals · doi:10.1023/a:1022582209196 · Cited by 10

Human platelet calcium mobilisation in response to ß-amyloid (25–35): buffer dependency and unchanged response in Alzheimer’s disease

Hedin, H. L. M., Eriksson, S., & Fowler, C. J. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(00)00068-1 · Cited by 10

Excessive glutamine sensitivity in Alzheimer's disease and Down syndrome lymphocytes

Peeters, M. A., Salabelle, A., Attal, N., Rethoré, M. O., Mircher, C., Laplane, D., & LEJEUNE, J. (1995) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(95)00135-o · Cited by 10

Acetyl-L-Carnitine Arginine Amide Prevents β 25–35-Induced Neurotoxicity in Cerebellar Granule Cells

Scorziello, A., Meucci, O., Calvani, M., & Schettini, G. (1997) · Neurochemical Research · doi:10.1023/a:1022430503520 · Cited by 10

Signalling of galanin and amyloid precursor protein through adenylate cyclase

Mahlapuu, R. (2004) · DSpace repository (University of Tartu) · Cited by 10

Amyloid–ß peptides interaction with curcumin:AFM and electrochemical characterisation

Paquim, A.-M. C., Machini, W. B. S., & Oliveira‐Brett, A. M. (2025) · Electrochimica Acta · doi:10.1016/j.electacta.2025.146160 · Cited by 9

Neuroprotective responses of quercetin in regulation of biochemical, structural, and neurobehavioral effects in 28-day oral exposure of iron in rats

Anuradha, U., Angati, A., Gautam, A. S., Dey, M., Pandey, S. K., & Singh, R. K. (2023) · Toxicology Mechanisms and Methods · doi:10.1080/15376516.2023.2256840 · Cited by 9

Inflammation and the pathophysiology of Alzheimer's disease

Murphy, G. M. (2000) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2000.2.3/mgreer · Cited by 9

In vitro neurotoxicity of amyloid β-peptide cross-linked by transglutaminase

Shinagawa, R., Masuda, S., Sasaki, R., Ikura, K., & Takahata, K. (1997) · Cytotechnology · doi:10.1023/a:1007999114779 · Cited by 9

Amyloid Aβ1−40preconditions non‐apoptotic signalsin vivoand protects fetal rat brain from intrauterine ischemic stress

Kuperstein, F., Brand, A., & Yavin, E. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02778.x · Cited by 9

Asymptomatic neurotoxicity of amyloid β-peptides (Aβ1-42 and Aβ25-35) on mouse embryonic stem cell-derived neural cells

Mansor, N. I., Ntimi, C. M., Abdul-Aziz, N. M., Ling, K., Adam, A., Rosli, R., Hassan, Z., & Nordin, N. (2020) · Bosnian Journal of Basic Medical Sciences · doi:10.17305/bjbms.2020.4639 · Cited by 9

The conformational preference of Cα-centered radicals in proteins

Owen, M. C., Komáromi, I., Murphy, R. F., & Lovas, S. (2006) · Journal of Molecular Structure THEOCHEM · doi:10.1016/j.theochem.2005.10.047 · Cited by 9

On the mechanism of the inhibition of glutamine synthetase and creatine phosphokinase by methionine sulfoxide

Haghighi, A. Z., & Maples, K. R. (1996) · Journal of Neuroscience Research · doi:10.1002/jnr.490430114 · Cited by 9

Transfer of the apoptotic message in sister cultures of cerebellar neurons

Berardinis, M. A. D., Ciotti, M. T., Amadoro, G., Galli, C., & Calissano, P. (2001) · Neuroreport · doi:10.1097/00001756-200107200-00019 · Cited by 9

Transformation of beta-amyloid (Aβ) (1-42) tyrosine to L-Dopa as the result ofin vitrohydroxyl radical attack

Giunta, S., Ronchi, P., Valli, B., Franceschi, C., & Galeazzi, L. (2000) · Amyloid · doi:10.3109/13506120009146833 · Cited by 9

Implication of Novel Biochemical Property of β-Amyloid

Elbaum, D., Brzyska, M., Bacia, A., & Alkon, D. L. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.2024 · Cited by 9

Comparison of medial and lateral septal neuron activity during performance of spatial tasks in rats

Zhou, T. L., Tamura, R., Kuriwaki, J.-I., & Ono, T. (1999) · Hippocampus · doi:10.1002/(sici)1098-1063(1999)9:3 · Cited by 56

Evaluation of isatin-1,3,5-triazine-benzylamine hybrids as multi-target directed ligands against Alzheimer's disease

Tamaddon-Abibigloo, Y., Dastmalchi, S., Razzaghi‐Asl, N., Küçükkılınç, T. T., & Mojarrad, J. S. (2024) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2024.140717 · Cited by 8

Role of proline‐rich tyrosine kinase 2 (Pyk2) in the pathogenesis of Alzheimer's disease

Kumar, R. K., Tiwari, V., & Dey, S. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15569 · Cited by 9

Strategies for measuring concentrations and forms of amyloid-β peptides

Shen, H., Liu, K., Kong, F., Ren, M., Wang, X., & Wang, S. (2024) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2024.116405 · Cited by 9

Enzyme Inhibitors Involved in the Treatment of Alzheimer’s Disease

Revadigar, V., Ghalib, R. M., Murugaiyah, V., Embaby, M. A., Jawad, A. H., Mehdi, S. H., Hashim, R., & Sulaiman, O. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-803959-5.50003-9 · Cited by 9

Inhibition of β-amyloid1-40 Peptide Aggregation and Neurotoxicity by Citrate

Park, Y. H., Kim, Y.-J., Son, I. H., & Yang, H. D. (2009) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2009.13.4.273 · Cited by 8

ORGANIZATION OF EXTRACELLULAR MATRIX COMPONENTS DURING DIFFERENTIATION OF ADIPOCYTES IN LONG-TERM CULTURE

Yasuaki, K. U. B. O., Kaidzu, S., Nakajima, I., Takenouchi, K., & NAKAMURA, F. (2000) · In Vitro Cellular & Developmental Biology - Animal · doi:10.1290/1071-2690(2000)036 · Cited by 133

An insight into application and harmful effects of aluminium, aluminium complexes and aluminium nano-particles

Iqbal, I., Sharma, S., & Radha, A. (2022) · Materials Today Proceedings · doi:10.1016/j.matpr.2022.04.870 · Cited by 7

Cell death induction and protection by activation of ubiquitously expressed anion/cation channels. Part 3: the roles and properties of TRPM2 and TRPM7

Okada, Y., Numata, T., Sabirov, R. Z., Kashio, M., Merzlyak, P. G., & Sato-Numata, K. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1246955 · Cited by 7

Chapter 9 The Role of Mitochondrial Genome Mutations in Neurodegenerative Disease

Glazner, G. W. (1999) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(08)60029-2 · Cited by 7

Oxidative Changes and Possible Effects of Polymorphism of Antioxidant Enzymes in Neurodegenerative Disease

Babušíková, E., Evinová, A., Hatok, J., Dobrota, D., & Jurecekov, J. (2013) · InTech eBooks · doi:10.5772/54619 · Cited by 8

Responses of Cultured Astrocytes, C6 Glioma and 1321NI Astrocytoma Cells to Amyloid β-Peptide Fragments

Pentreath, V. W., & Mead, C. (2004) · Nonlinearity in Biology Toxicology Medicine · doi:10.1080/15401420490426990 · Cited by 7

The search for disease modification in moderate to severe Alzheimer disease

Farlow, M. R. (2005) · Neurology · doi:10.1212/wnl.65.6_suppl_3.s25 · Cited by 7

Advances and prospects of using nanocrystalline ceria in prolongation of lifespan and healthy aging

Shcherbakov, A. B., Nm, Z., Spivak, M. Y., & Ivanov, V. K. (2015) · Russian Journal of Inorganic Chemistry · doi:10.1134/s0036023615130057 · Cited by 7

Structurally Related Edaravone Analogues: Synthesis, Antiradical, Antioxidant, and Copper-Chelating Properties

Leblanc, A., Čuperlović‐Culf, M., Morin, P., & Touaibia, M. (2019) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527318666191114092007 · Cited by 7

Human Serum Albumin Fusion Protein as Therapeutics for Targeting Amyloid Beta in Alzheimer's Diseases.

Bang, S., Song, J. K., Shin, S.-W., & Lee, K. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.136298 · Cited by 7

Superoxo radical scavenging action by common analgesic drug paracetamol: A model kinetic study

Singh, B., Das, R. S., Banerjee, R., & Mukhopadhyay, S. (2013) · Inorganica Chimica Acta · doi:10.1016/j.ica.2013.04.031 · Cited by 7

Gene Expression Profiles of APP and BACE1 in Tg SOD1G93A Cortical Cells

Spadoni, O., Crestini, A., Piscopo, P., Malvezzi‐Campeggi, L., Carunchio, I., Pieri, M., Zona, C., & Confaloni, A. (2009) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-009-9356-8 · Cited by 7

((E)-N-(4-(((2-Amino-5-phenylpyridin-3-yl)imino)methyl)pyridin-2-yl)cyclopropanecarboxamide) Ameliorated Aβ1–42-Induced Alzheimer’s Disease in SD Rats by Inhibiting Oxidative Stress and Apoptosis

Ding, Y., Wang, X., Ji, J., Zhang, X., Chen, M., Li, S., Zhang, Q., & Liu, P. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00655 · Cited by 7

Maintaining the Stability of the Genome

Bürkle, A. (1996) · Springer eBooks · doi:10.1007/978-1-4615-5889-7_3 · Cited by 7

In vitro apolipoprotein E protects human red blood cells against lysis induced by amyloid-beta (Aβ) fragment 25-35

Galeazzi, L., Corder, E. H., Galeazzi, R., Casoli, T., Valli, M. B., & Giunta, S. (2002) · Amyloid · doi:10.3109/13506120208995242 · Cited by 7

Antioxidant and Antiapoptotic Effects of 1,1′-(Biphenyl-4,4′-diyl)-bis(3-(dimethylamino)-propan-1-one) on Protecting PC12 Cells from Aβ-Induced Injury

Zhu, Y., Sun, X., Gong, T., He, Q., & Zhang, Z. (2013) · Molecular Pharmaceutics · doi:10.1021/mp400395g · Cited by 7

Antioxidant and Antibacterial Activities of Dimeric Phenol Compounds

Ogata, M. (2008) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.128.1149 · Cited by 7

The relationship between Aβ-associated free radical generation and Aβ fibril formation revealed by negative stain electron microscopy and thioflavine-T fluorometric assay

Monji, A., Utsumi, H., Yoshida, I., Hashioka, S., Tashiro, K., & Tashiro, N. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01756-6 · Cited by 7

In vitro effect of selected medicinal plants on β-amyloid induced toxicity in neuroblastoma cells

Adewusi, E. A. (2012) · UpSpace Institutional Repository (University of Pretoria) · Cited by 7

Oxytocin Protects PC12 Cells Against β-Amyloid-Induced Cell Injury

Alanazi, M. M., Albaker, A. B., Alzaagi, L. A., Alsabhan, J. F., Alasmari, F. F., Almutairi, ‏. M. S., Alharbi, M., Alasmari, A. F., Alqahtani, F., & Alsanea, S. (2025) · Pharmaceuticals · doi:10.3390/ph18030390 · Cited by 6

The central role of mitochondrial dysfunction in neurodegeneration: implications for therapy

Raafat, M. A., Al-Hasnaawei, S., Mousa, H. M., Hanumanthayya, M., Sahoo, S., Prathiba, S., Singh, G., & Sinha, A. (2026) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-026-05542-w · Cited by 6

Alzheimer’s Disease: Focus on the Neuroprotective Role of Melatonin

Srinivasan (2012) · Journal of Neurology Research · doi:10.4021/jnr93w · Cited by 6

Inhibitors of free radical formation fail to attenuate direct β‐amyloid25–35 peptide‐mediated neurotoxicity in rat hippocampal cultures

Lockhart, B. P., Bénicourt, C., Junien, J., & Privat, A. (1994) · Journal of Neuroscience Research · doi:10.1002/jnr.490390416 · Cited by 92

A model for beta-amyloid aggregation and neurotoxicity based on the free radical generating capacity of the peptide: implications of "molecular shrapnel" for Alzheimer's disease.

Hensley, K., Butterfield, D. A., Mattson, M. P., Aksenova, M. V., Harris‐White, M. E., Wu, J., Floyd, R. A., & Carney, J. M. (1995) · PubMed · Cited by 36

Direct evidence of oxidative injury produced by the Alzheimer's β-Amyloid peptide (1–40) in cultured hippocampal neurons

Harris‐White, M. E., Hensley, K., Butterfield, D. A., Leedle, R. A., & Carney, J. M. (1995) · Experimental Neurology · doi:10.1016/0014-4886(95)90041-1 · Cited by 331

Aβ(25–35) peptide displays H2O2-like reactivity towards aqueous FE2+, nitroxide spin probes, Ant) synaptosomal membrane proteins

Butterfield, D. A., Martin, L., Carney, J. M., & Hensley, K. (1995) · Life Sciences · doi:10.1016/0024-3205(95)02279-1 · Cited by 59

β-Amyloid Peptide Free Radical Fragments Initiate Synaptosomal Lipoperoxidation in a Sequence-Specific Fashion: Implications to Alzheimer′s Disease

Butterfield, D. A., Hensley, K., Harris‐White, M. E., Mattson, M. P., & Carney, J. M. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1508 · Cited by 404