Oxidative stress in Alzheimer’s disease

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

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Role of Oxidative Stress in Development of Complications in Diabetes

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Hydrogen peroxide mediates amyloid β protein toxicity

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

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

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

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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.

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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

Cross-talk between redox signalling and protein aggregation

van Dam, L., & Dansen, T. B. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190054 · Cited by 56

Effect of low-intensity motor balance and coordination exercise on cognitive functions, hippocampal Aβ deposition, neuronal loss, neuroinflammation, and oxidative stress in a mouse model of Alzheimer's disease

Nakanishi, K., Sakakima, H., Norimatsu, K., Otsuka, S., Takada, S., Tani, A., & Kikuchi, K. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113590 · Cited by 53

Molecular mechanisms of the neuroprotective neurorescue action of multi-target green tea polyphenols

Mandel, S. A. (2012) · Frontiers in Bioscience-Scholar · doi:10.2741/s286 · Cited by 54

Development of a neuroprotective potential algorithm for medicinal plants

Liu, W., Ma, H., DaSilva, N. A., Rose, K. N., Johnson, S. L., Zhang, L., Wan, C. C., Dain, J. A., & Seeram, N. P. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2016.09.014 · Cited by 56

Role of Component Herbs in Antioxidant Activity of Shengmai San — A Traditional Chinese Medicine Formula Preventing Cerebral Oxidative Damage in Rat

Ichikawa, H., Wang, X., & Konishi, T. (2003) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x03001193 · Cited by 53

Differential expression of phosphorylated translation initiation factor 2 alpha in Alzheimer’s disease and Creutzfeldt-Jakob’s disease

Ferrer, I. (2002) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2002.t01-1-00410.x · Cited by 52

Multi-Target-Directed Ligands as an Effective Strategy for the Treatment of Alzheimer’s Disease

Kumar, R., Kumar, V., Kumar, B., Thakur, A., & Dwivedi, A. R. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666210512005508 · Cited by 55

Type-Dependent Oxidative Damage in Frontotemporal Lobar Degeneration: Cortical Astrocytes Are Targets of Oxidative Damage

Martínez, A., Carmona, M., Portero‐Otín, M., Naudí, A., Pamplona, R., & Ferrer, I. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31818e06f3 · Cited by 53

Central role of PKCδ in glycoxidation-dependent apoptosis of human neurons

Nitti, M., d'Abramo, C., Traverso, N., Verzola, D., Garibotto, G., Poggi, A., Odetti, P., Cottalasso, D., Marinari, U., Pronzato, M., et al. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.12.002 · Cited by 53

Iron-chelating backbone coupled with monoamine oxidase inhibitory moiety as novel pluripotential therapeutic agents for Alzheimer’s disease: a tribute to Moussa Youdim

Weinreb, O., Mandel, S. A., Bar‐Am, O., & Amit, T. (2011) · Journal of Neural Transmission · doi:10.1007/s00702-011-0597-6 · Cited by 51

A novel anti-Alzheimer's disease drug, ladostigil

Weinreb, O., Amit, T., Bar‐Am, O., & Youdim, M. B. H. (2011) · International review of neurobiology · doi:10.1016/b978-0-12-386467-3.00010-8 · Cited by 54

Stress kinases involved inTau phosphorylation in alzheimer’s disease, tauopathies and APP transgenic mice

Ferrer, I. (2004) · Neurotoxicity Research · doi:10.1007/bf03033283 · Cited by 53

Expression and Polymorphisms of Gene 8-Oxoguanine Glycosylase 1 and the Level of Oxidative DNA Damage in Peripheral Blood Lymphocytes of Patients with Alzheimer's Disease

Dorszewska, J., Kempisty, B., Jaroszewska-Kolecka, J., Różycka, A., Florczak, J., Lianeri, M., Jagodziński, P. P., & Kozubski, W. P. (2009) · DNA and Cell Biology · doi:10.1089/dna.2009.0926 · Cited by 52

Glutathione S-Transferase P1 *C Allelic Variant Increases Susceptibility for Late-Onset Alzheimer Disease: Association Study and Relationship with Apolipoprotein E ε4 Allele

Bernardini, S., Bellincampi, L., Ballerini, S., et al. (2005) · Clinical Chemistry · doi:10.1373/clinchem.2004.045955 · Cited by 52

Extra-Virgin Olive Oil in Alzheimer’s Disease: A Comprehensive Review of Cellular, Animal, and Clinical Studies

Alkhalifa, A. E., Al-Ghraiybah, N. F., & Kaddoumi, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031914 · Cited by 52

Healthy Aging – Insights from Drosophila

Iliadi, K. G., Knight, D., & Boulianne, G. L. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00106 · Cited by 51

Oxidative Stress Induced Mitochondrial DNA Deletion as a Hallmark forthe Drug Development in the Context of the Cerebrovascular Diseases

Aliev, G., Li, Y., Palacios, H. H., & Obrenovich, M. E. (2011) · Recent Advances in Cardiovascular Drug Discovery (Formerly Recent Patents on Cardiovascular Drug Discovery) · doi:10.2174/157489011797376942 · Cited by 51

Targeted proteomics in Alzheimer’s disease: focus on amyloid-β

Portelius, E., Zetterberg, H., Gobom, J., Andréasson, U., & Blennow, K. (2008) · Expert Review of Proteomics · doi:10.1586/14789450.5.2.225 · Cited by 52

Coordination of copper(II) ions by the 11–20 and 11–28 fragments of human and mouse β-amyloid peptide

Kowalik‐Jankowska, T., Ruta-Dolejsz, M., Wiśniewska, K., & Łankiewicz, L. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00495-6 · Cited by 51

Red blood cell copper, zinc superoxide dismutase activity is higher in Alzheimer's disease and is decreased by d-penicillamine

Rossi, L. C., Squitti, R., Pasqualetti, P., Marchese, E., Cassetta, E., Forastiere, E., Rotilio, G., Rossini, P. M., & Finazzi‐Agrò, A. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00599-2 · Cited by 51

Metabolomic investigation of systemic manifestations associated with Alzheimer's disease in the APP/PS1 transgenic mouse model

González‐Domínguez, R., García‐Barrera, T., Vitórica, J., & Gómez‐Ariza, J. L. (2015) · Molecular BioSystems · doi:10.1039/c4mb00747f · Cited by 50

DNA repair and neurological disease: From molecular understanding to the development of diagnostics and model organisms

Abugable, A. A., Morris, J. L. M., Palminha, N. M., Zaksauskaite, R., Ray, S., & El‐Khamisy, S. F. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.102669 · Cited by 53

Pro‐apoptotic signaling in neuronal cells following iron and amyloid beta peptide neurotoxicity

Kuperstein, F., & Yavin, E. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01831.x · Cited by 50

Enhanced ROS-Generation in Lymphocytes from Alzheimer’s Patients

Leutner, S., Schindowski, K., Frölich, L., Maurer, K., Kratzsch, T., Eckert, A., & Müller, W. E. G. (2005) · Pharmacopsychiatry · doi:10.1055/s-2005-916186 · Cited by 50

Protective effects of Glycyrrhiza uralensis Fisch. on the cognitive deficits caused by β-amyloid peptide 25–35 in young mice

Ahn, J., Um, M. Y., Choi, W., Kim, S., & Ha, T. Y. (2006) · Biogerontology · doi:10.1007/s10522-006-9023-0 · Cited by 50

Alzheimer's β-amyloid peptide as a source of neurotoxic free radicals: the role of structural effects

Pogocki, D. (2003) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2003-1463 · Cited by 50

Enhanced ROS Generation Mediated by Alzheimer's Disease Presenilin Regulation of InsP 3 R Ca 2+ Signaling

Müller, M., Cheung, K., & Foskett, J. K. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3421 · Cited by 50

Nonpeptide neurotrophic agents useful in the treatment of neurodegenerative diseases such as Alzheimer's disease

Akagi, M., Matsui, N., Akae, H., Hirashima, N., Fukuishi, N., Fukuyama, Y., & Akagi, R. (2015) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2014.12.015 · Cited by 50

Cu II Binding to Various Forms of Amyloid‐β Peptides: Are They Friends or Foes?

Borghesani, V., Aliès, B., & Hureau, C. (2017) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201700776 · Cited by 50

Olive (Olea europaea L.) Biophenols: A Nutriceutical against Oxidative Stress in SH-SY5Y Cells

Omar, S. H., Kerr, P. G., Scott, C., Hamlin, A. S., & Obied, H. K. (2017) · Molecules · doi:10.3390/molecules22111858 · Cited by 50

Design, synthesis, and evaluation of N-benzylpyrrolidine and 1,3,4-oxadiazole as multitargeted hybrids for the treatment of Alzheimer’s disease

Choubey, P. K., Tripathi, A., Tripathi, M. K., Seth, A., & Shrivastava, S. K. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104922 · Cited by 53

Activity of Selected Group of Monoterpenes in Alzheimer’s Disease Symptoms in Experimental Model Studies—A Non-Systematic Review

Wojtunik‐Kulesza, K. A., Rudkowska, M., Kasprzak‐Drozd, K., Oniszczuk, A., & Borowicz, K. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147366 · Cited by 51

Up-regulation of Glycohydrolases in Alzheimer's Disease Fibroblasts Correlates with Ras Activation

Emiliani, C., Urbanelli, L., Racanicchi, L., Orlacchio, A., Pelicci, G., Sorbi, S., Bernardi, G., & Orlacchio, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303030200 · Cited by 49

Oxidative stress increases internal calcium stores and reduces a key mitochondrial enzyme

Gibson, G. E., Zhang, H., Xu, H., Park, L. C. H., & Jeitner, T. M. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(01)00091-6 · Cited by 49

Stimulation of SIRT1 Attenuates the Level of Oxidative Stress in the Brains of APP/PS1 Double Transgenic Mice and in Primary Neurons Exposed to Oligomers of the Amyloid-β Peptide

Dong, Y., Cao, K., Tan, L.-C., Wang, X., Qi, X., Xiao, Y. C., & Guan, Z.-Z. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171020 · Cited by 48

Glutathione S-Transferase P1 and T1 Gene Polymorphisms Predict Longitudinal Course and Age at Onset of Alzheimer Disease

Spalletta, G., Bernardini, S., Bellincampi, L., Federici, G., Trequattrini, A., Ciappi, F., Bria, P., Caltagirone, C., & Bossù, P. (2007) · American Journal of Geriatric Psychiatry · doi:10.1097/jgp.0b013e3180547076 · Cited by 47

An endogenous metabolite of dopamine, 3,4-dihydroxyphenylethanol, acts as a unique cytoprotective agent against oxidative stress-induced injury

Hashimoto, T., Ibi, M., Matsuno, K., Nakashima, S., Tanigawa, T., Yoshikawa, T., & Yabe‐Nishimura, C. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.12.003 · Cited by 48

Neurofibrillary tangles and deposition of oxidative products in the brain in cases of myotonic dystrophy

Oyamada, R., Hayashi, M., Katoh, Y., Tsuchiya, K., Mizutani, T., Tominaga, I., & Kashima, H. (2006) · Neuropathology · doi:10.1111/j.1440-1789.2006.00662.x · Cited by 50

Oxidative Stress in Alzheimer’s Disease: Molecular Hallmarks of Underlying Vulnerability

Uddin, M. S., & Kabir, M. T. (2019) · Springer eBooks · doi:10.1007/978-981-13-9636-6_5 · Cited by 50

Neuroprotective effects of multifaceted hybrid agents targeting MAO, cholinesterase, iron and β‐amyloid in ageing and Alzheimer's disease

Weinreb, O., Amit, T., Bar‐Am, O., & Youdim, M. B. H. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13318 · Cited by 48

Investigating alkyl nitrates as nitric oxide releasing precursors of multitarget acetylcholinesterase-monoamine oxidase B inhibitors

Pisani, L., Iacobazzi, R. M., Catto, M., Rullo, M., Farina, R., Denora, N., Cellamare, S., & Altomare, C. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.10.016 · Cited by 51

Role of the JNK-interacting protein 1/islet brain 1 in cell degeneration in Alzheimer disease and diabetes

Beeler, N., Riederer, B. M., Waeber, G., & Abderrahmani, A. (2009) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2009.07.006 · Cited by 51

Inhibition of A1 Astrocytes and Activation of A2 Astrocytes for the Treatment of Spinal Cord Injury

Wang, J., Cheng, C., Liu, Z., Lin, Y., Yang, L., Zhang, Z., Sun, X., Zhou, M., Jing, P., & Zhong, Z. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03820-9 · Cited by 48

Aluminum, NO, and nerve growth factor neurotoxicity in cholinergic neurons

Szutowicz, A. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.10040 · Cited by 46

Half-Life Mapping of Nitroxyl Radicals with Three-Dimensional Electron Paramagnetic Resonance Imaging at an Interval of 3.6 Seconds

Sato‐Akaba, H., Kuwahara, Y., Fujii, H. G., et al. (2009) · Analytical Chemistry · doi:10.1021/ac901169g · Cited by 46

Neuroprotective profile of the multitarget drug rasagiline in Parkinson's disease

Weinreb, O., Amit, T., Riederer, P. F., Youdim, M. B. H., & Mandel, S. A. (2011) · International review of neurobiology · doi:10.1016/b978-0-12-386467-3.00007-8 · Cited by 45

Involvement of PPAR-gamma in curcumin-mediated beneficial effects in experimental dementia

Rinwa, P., Kaur, B., Jaggi, A. S., & Singh, N. (2010) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-010-0511-z · Cited by 45

Protective melatonin effect on oxidative stress induced by okadaic acid into rat brain

Túnez, I., Muñoz, M. D. C., Feijóo, M., Muñoz-Castañeda, J. R., Bujalance, I., Valdelvira, M. E., & López, P. M. (2003) · Journal of Pineal Research · doi:10.1034/j.1600-079x.2003.00039.x · Cited by 45

Aging causes partial loss of basal forebrain but no loss of pontine reticular cholinergic neurons

Baskerville, K. A., Kent, C., Nicolle, M. M., Gallagher, M., & McKinney, M. (2006) · NeuroReport · doi:10.1097/wnr.0b013e32800fef5a · Cited by 44

Smoking Increases Risk for Cognitive Decline Among Community-Dwelling Older Mexican Americans

Collins, N., Sachs‐Ericsson, N., Preacher, K. J., Sheffield, K. M., & Markides, K. S. (2009) · American Journal of Geriatric Psychiatry · doi:10.1097/jgp.0b013e3181b0f8df · Cited by 43

Nootropic medicinal plants: Therapeutic alternatives for Alzheimer’s disease

Vyas, S., Kothari, S. L., & Kachhwaha, S. (2019) · Journal of Herbal Medicine · doi:10.1016/j.hermed.2019.100291 · Cited by 48

Metals accelerate production of the aberrant splicing isoform of the presenilin‐2

Matsuzaki, S., Manabe, T., Katayama, T., Nishikawa, A., Yanagita, T., Okuda, H., Yasuda, Y., Miyata, S., Meshitsuka, S., & Tohyama, M. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02290.x · Cited by 44

A Multimeric Quinacrine Conjugate as a Potential Inhibitor of Alzheimer's β‐Amyloid Fibril Formation

Dolphin, G. T., Chierici, S., Ouberai, M. M., Dumy, P., & Garcia, J. (2008) · ChemBioChem · doi:10.1002/cbic.200700602 · Cited by 44

In vitro neuroprotective potential of four medicinal plants against rotenone-induced toxicity in SH-SY5Y neuroblastoma cells

Seoposengwe, K., van Tonder, J. J., & Steenkamp, V. (2013) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-13-353 · Cited by 43

Effects of immature cashew nut-shell liquid (Anacardium occidentale) against oxidative damage in Saccharomyces cerevisiae and inhibition of acetylcholinesterase activity

de Lima, S. G., Feitosa, C. M., Citó, A. M. G. L., Neto, J. M. M., Lopes, J. A. D., Leite, A., Brito, M. C., Dantas, S. M. M. D. M., & Cavalcante, A. A. D. C. M. (2008) · Genetics and Molecular Research · doi:10.4238/vol7-3gmr473 · Cited by 42

Oxidative Stress Induced Mitochondrial Failure and Vascular Hypoperfusion as a Key Initiator for the Development of Alzheimer Disease

Aliev, G., Palacios, H. H., Gasimov, E. K., Obrenovich, M. E., Morales, L., Leszek, J., Bragin, V., Herrera, A. S., & Gokhman, D. (2010) · Pharmaceuticals · doi:10.3390/ph3010158 · Cited by 43

Effect of the oral iron chelator deferiprone in diabetic nephropathy rats

Zou, C., Liu, X., Liu, R., Wang, M., Sui, M., Mu, S.-H., Li, L., Ji, L., & Xie, R. (2016) · Journal of Diabetes · doi:10.1111/1753-0407.12420 · Cited by 42

Sex Differences in Alzheimer’s Disease: Where Do We Stand?

Medeiros, A. D. M., & Silva, R. H. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180213 · Cited by 42

The Role of the Microbiota-Gut-Brain Axis in the Health and Illness Condition: A Focus on Alzheimer’s Disease

la Fuente, M. D. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201587 · Cited by 44

Cefotaxime removal enhancement via bio-nanophotocatalyst α-Fe2O3 using photocatalytic degradation technique and its echo-biomedical applications

Al-Hakkani, M. F., Gouda, G. A., Hassan, S. H. A., Saddik, M. S., El‐Mokhtar, M. A., Ibrahim, M. A., Mohamed, M. M. A., & Nagiub, A. M. (2022) · Scientific Reports · doi:10.1038/s41598-022-14922-3 · Cited by 43

Antioxidant role of amyloid β protein in cell-free and biological systems: implication for the pathogenesis of Alzheimerdisease

Sinha, M. S., Bhowmick, P., Banerjee, A., & Chakrabarti, S. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.036 · Cited by 45

Neuropathology and treatment of Alzheimer disease: did we lose the forest for the trees?

Castellani, R. J., Zhu, X., Lee, H., Moreira, P. I., Perry, G. L., & Smith, M. A. (2007) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.7.5.473 · Cited by 42

Localization of the noncovalent binding site between amyloid-β-peptide and oleuropein using electrospray ionization FT-ICR mass spectrometry

Bazoti, F. N., Bergquist, J., Markides, K. E., & Tsarbopoulos, A. (2008) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2008.03.011 · Cited by 43

Environmental enrichment and social interaction improve cognitive function and decrease reactive oxidative species in normal adult mice

Doulames, V. M., Lee, S., & Shea, T. B. (2013) · International Journal of Neuroscience · doi:10.3109/00207454.2013.848441 · Cited by 48

Prevention approaches in a preclinical canine model of Alzheimer’s disease: benefits and challenges

Davis, P. R., & Head, E. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00047 · Cited by 43

Screening and Evaluation of Antioxidant Activity of Some 1,2,4-triazolo[1,5- a ]quinazoline Derivatives

Al‐Salahi, R. A., Anouar, E. H., Marzouk, M., et al. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0224 · Cited by 41

Serum Total Antioxidant Status, Erythrocyte Superoxide Dismutase and Whole-Blood Glutathione Peroxidase Activities in the Stanislas Cohort: Influencing Factors and Reference Intervals

Habdous, M., Herbeth, B., Vincent‐Viry, M., Lamont, J. V., Fitzgerald, P. S., Visvikis‐Siest, S., & Siest, G. (2003) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2003.034 · Cited by 41

Chemiluminescence methods (present and future)

Jiménez, A. M., & Navas, M. J. (2002) · Grasas y Aceites · doi:10.3989/gya.2002.v53.i1.290 · Cited by 41

Natural antioxidants in prevention and management of Alzheimer s disease

Zhao, B. (2012) · Frontiers in Bioscience-Elite · doi:10.2741/e419 · Cited by 41

Dietary Lipids in the Aetiology of Alzheimer???s Disease

Cooper, J. L. (2003) · Drugs & Aging · doi:10.2165/00002512-200320060-00001 · Cited by 40

Neuronal regulation of lifespan: clues from flies and worms

Boulianne, G.-H. L. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(01)00245-7 · Cited by 41

Correlation of the clinical severity of Alzheimer's disease with an aberration in mitochondrial DNA (mtDNA)

Brown, A. M., Sheu, R. K.-F., Mohs, R., Haroutunian, V., & Blass, J. P. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:16:1:41 · Cited by 40

Oxidative Stress and Protein Quality Control Systems in the Aged Canine Brain as a Model for Human Neurodegenerative Disorders

Romanucci, M., & Salda, L. D. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/940131 · Cited by 43

Ferulic acid prevents LPS-induced up-regulation of PDE4B and stimulates the cAMP/CREB signaling pathway in PC12 cells

Huang, H., Hong, Q., Tan, H.-L., Xiao, C., & Gao, Y. (2016) · Acta Pharmacologica Sinica · doi:10.1038/aps.2016.88 · Cited by 40

Discovery of boron-containing compounds as Aβ aggregation inhibitors and antioxidants for the treatment of Alzheimer's disease

Lu, C., Hu, J., Wang, Z., Xie, S., Pan, T., Huang, L., & Li, X. (2018) · MedChemComm · doi:10.1039/c8md00315g · Cited by 40

Further SAR studies on natural template based neuroprotective molecules for the treatment of Alzheimer’s disease

Singh, Y. P., Shankar, G., Jahan, S., Singh, G., Kumar, N., Barik, A., Upadhyay, P., Singh, L., Kamble, K., Singh, G. K., et al. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116385 · Cited by 42

Generation of reactive oxygen species and activation of NF‐κB by non‐Aβ component of Alzheimer's disease amyloid

Tanaka, S., Takehashi, M., Matoh, N., Iida, S., Suzuki, T. W., Futaki, S., Hamada, H., Masliah, E., Sugiura, Y., & Ueda, K. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00958.x · Cited by 40

Plasma 8-isoPGF2α and serum melatonin levels in patients with minimal cognitive impairment and Alzheimer disease

ŞİRİN, F. B., Doğuç, D. K., Vural, H., Eren, İ., İnanlı, İ., Sütçü, R., & Delibaş, N. (2015) · TURKISH JOURNAL OF MEDICAL SCIENCES · doi:10.3906/sag-1406-134 · Cited by 39

Interactions of Mitochondria/Metabolism and Calcium Regulation in Alzheimer’s Disease: A Calcinist Point of View

Gibson, G. E., & Thakkar, A. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2182-3 · Cited by 39

Loss of ferritin‐positive microglia relates to increased iron, RNA oxidation, and dystrophic microglia in the brains of aged male marmosets

Rodríguez-Callejas, J. D., Cuervo-Zanatta, D., Rosas‐Arellano, A., Fonta, C., Fuchs, E., & Perez‐Cruz, C. (2019) · American Journal of Primatology · doi:10.1002/ajp.22956 · Cited by 39

The degraded polysaccharide from Pyropia haitanensis represses amyloid beta peptide-induced neurotoxicity and memory in vivo

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