Causes of oxidative stress in Alzheimer disease

Inflammation and Alzheimer’s disease

Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514

The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction

Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,304

Plasma Homocysteine as a Risk Factor for Dementia and Alzheimer's Disease

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Copper, iron and zinc in Alzheimer's disease senile plaques

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Hydrogen peroxide mediates amyloid β protein toxicity

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Metabolic reduction in the posterior cingulate cortex in very early Alzheimer's disease

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Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids

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APP Processing and Synaptic Function

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Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study

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

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Design, Synthesis, and Evaluation of Chalcone Derivatives as Multifunctional Agents against Alzheimer's Disease

Wang, X., Zhou, L., Tan, R., Liang, G., Fang, S., Li, W., Xie, M., Wen, Y., Wu, J., & Chen, Y. (2021) · Chemistry & Biodiversity · doi:10.1002/cbdv.202100341 · Cited by 27

Intermittent theta burst stimulation attenuates oxidative stress and reactive astrogliosis in the streptozotocin-induced model of Alzheimer’s disease-like pathology

Stanojevic, J., Zeljković, M., Dragić, M., Stojanović, I. R., Ilic, T. V., Stevanović, I. D., & Ninković, M. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1161678 · Cited by 27

Function and Redox State of Peritoneal Leukocytes as Preclinical and Prodromic Markers in a Longitudinal Study of Triple-Transgenic Mice for Alzheimer's Disease

Maté, I., Cruces, J., Giménez‐Llort, L., & la Fuente, M. D. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140861 · Cited by 28

Preventing H2O2-induced apoptosis in cerebellar granule neurons by regulating the VEGFR-2/Akt signaling pathway using a novel dimeric antiacetylcholinesterase bis(12)-hupyridone

Cui, W., Li, W., Zhao, Y., Mak, S., Gao, Y., Luo, J., Zhang, H., Liu, Y., Carlier, P. R., Rong, J., et al. (2011) · Brain Research · doi:10.1016/j.brainres.2011.02.006 · Cited by 26

Design, synthesis and evaluation of 2-arylethenyl- N -methylquinolinium derivatives as effective multifunctional agents for Alzheimer's disease treatment

Xia, C., Wang, N., Guo, Q.-L., Liu, Z.-Q., Wu, J., Huang, S., Ou, T., Tan, J., Wang, H., Li, D., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.02.042 · Cited by 26

Synthesis, in vitro and structural aspects of benzothiazole analogs as anti-oxidants and potential neuroprotective agents

Ramaiah, M. J., Karthikeyan, D., Mathavan, S., Yamajala, R. B. R. D., Ramachandran, S., Vasavi, P. J., & Chandana, N. V. (2020) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2020.103415 · Cited by 25

Chemical and functional changes of human insulin by in vitro incubation with blood from diabetic patients in oxidative stress

Montes-Cortes, D. H., Hicks, J. J., Ceballos, G. M., García-Sánchez, J. R., Medina-Navarro, R., & Olivares-Corichi, I. M. (2009) · Metabolism · doi:10.1016/j.metabol.2009.10.013 · Cited by 25

Highly Efficient Synthesis of 1,3-Dihydroxy-2-carboxycarbazole and Its Neuroprotective Effects

Liu, K., & Zhang, S. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00158 · Cited by 24

Discovery of novel hybrid tryptamine-rivastigmine molecules as potent AChE and BChE inhibitors exhibiting multifunctional properties for the management of Alzheimer's disease

Shankar, G., Kumar, P., Rai, S., Ghosh, A., Varma, T., Wani, M. A., Kumar, S., Mandloi, U., Singh, G. K., Garg, P., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117066 · Cited by 23

Copper Ion Uptake by Chitosan in the Presence of Amyloid-β and Histidine

Mahl, C. R. A., Taketa, T. B., Neto, J. B. M. R., Almeida, W. P., & Beppu, M. M. (2019) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-019-03120-z · Cited by 23

A modified preparation (LMK03) of the oriental medicine Jangwonhwan reduces Aβ1–42 level in the brain of Tg-APPswe/PS1dE9 mouse model of Alzheimer disease

Seo, J., Jung, E.-Y., Kim, J., Lyu, Y.-S., Han, P., & Kang, H.-W. (2010) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2010.05.055 · Cited by 24

Neuroimmunomodulatory steroids in Alzheimer dementia

Hampl, R., & Bičı́ková, M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.02.007 · Cited by 23

A New Chiral Pyrrolyl α-Nitronyl Nitroxide Radical Attenuates β-Amyloid Deposition and Rescues Memory Deficits in a Mouse Model of Alzheimer Disease

Shi, T., Zhao, D., Wang, H., Feng, S., Liu, S., Xing, J.-H., Qu, Y., Gao, P., Sun, X., & Zhao, M. (2012) · Neurotherapeutics · doi:10.1007/s13311-012-0168-z · Cited by 22

Conformational Transitions of the Amyloid‐β Peptide Upon Copper(II) Binding and pH Changes

Liao, Q., Owen, M. C., Olubiyi, O. O., Barz, B., & Strodel, B. (2017) · Israel Journal of Chemistry · doi:10.1002/ijch.201600108 · Cited by 22

Regulation of amyloid-β production by the prion protein

Jarosz-Griffiths, H., Whitehouse, I. J., & Hooper, N. M. (2012) · Prion · doi:10.4161/pri.18988 · Cited by 23

Key roles of Arg5, Tyr10 and His residues in Aβ–heme peroxidase: Relevance to Alzheimer’s disease

Lu, N., Li, J., Tian, R., & Peng, Y. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.08.130 · Cited by 22

Bivalent Ligands Targeting Multiple Pathological Factors Involved in Alzheimer's Disease

Liu, K., Gandhi, R., Chen, J., & Zhang, S. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml300229y · Cited by 21

Multitarget Activities of Kleeb Bua Daeng, a Thai Traditional Herbal Formula, Against Alzheimer’s Disease

Chheng, C., Waiwut, P., Plekratoke, K., Chulikhit, Y., Daodee, S., Monthakantirat, O., Pitiporn, S., Musigavong, N., Kwankhao, P., & Boonyarat, C. (2020) · Pharmaceuticals · doi:10.3390/ph13050079 · Cited by 21

Neuroprotective effects of SB‐415286 on hydrogen peroxide‐induced cell death in B65 rat neuroblastoma cells and neurons

Pizarro, J. G., Yeste‐Velasco, M., Rimbau, V., Casadesús, G., Smith, M. A., Pallàs, M., Folch, J., & Camins, A. (2008) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2008.02.002 · Cited by 21

Human Induced Pluripotent Stem Cell-Derived Neural Cells from Alzheimer's Disease Patients Exhibited Different Susceptibility to Oxidative Stress

Zhang, L., Xu, M., Ren, Q., Liu, G., Meng, S., Xiahou, K., Zhang, Y., Jiang, N., & Zhou, W. (2020) · Stem Cells and Development · doi:10.1089/scd.2020.0103 · Cited by 20

Is Brain Copper Deficiency in Alzheimer's, Lewy Body, and Creutzfeldt Jakob Diseases the Common Key for a Free Radical Mechanism and Oxidative Stress-Induced Damage?

Deloncle, R., & Guillard, O. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140765 · Cited by 20

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

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

Neuroprotective Activity of Polyphenol-Rich Ribes diacanthum Pall against Oxidative Stress in Glutamate-Stimulated HT-22 Cells and a Scopolamine-Induced Amnesia Animal Model

Kim, H. J., Baek, S. Y., Sok, D., Lee, K. J., Kim, Y., & Kim, M. R. (2020) · Antioxidants · doi:10.3390/antiox9090895 · Cited by 19

ATM-Mediated Mitochondrial Radiation Responses of Human Fibroblasts

Shimura, T. (2021) · Genes · doi:10.3390/genes12071015 · Cited by 19

HNK-1 Carrier Glycoproteins Are Decreased in the Alzheimer’s Disease Brain

García‐Ayllón, M., Botella-López, A., Cuchillo‐Ibáñez, I., Rábano, A., Andreasen, N., Blennow, K., Ávila, J., & Sáez‐Valero, J. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9644-x · Cited by 19

Metabolic inhibitors accentuate the anti-tumoral effect of HDAC5 inhibition

Hendrick, E., Peixoto, P., Blomme, A., Polese, C., Matheus, N., Cimino, J., Frère, A., Mouithys-Mickalad, A., Serteyn, D., Bettendorff, L., et al. (2017) · Oncogene · doi:10.1038/onc.2017.103 · Cited by 18

Effects of an Armillaria mellea Polysaccharide on Learning and Memory of D-Galactose-Induced Aging Mice

Li, H., Xu, G., & Yuan, G. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.919920 · Cited by 18

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

Modulating Metals As A Therapeutic Strategy For Alzheimer’s Disease

Hung, L. W., & Barnham, K. J. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.32 · Cited by 18

Potentiation of amyloid-β peptide neurotoxicity in human dental-pulp neuron-like cells by the membrane lipid peroxidation product 4-hydroxynonenal

Testa, G., Gamba, P., Scipio, F. D., Sprio, A. E., Salamone, P., Gargiulo, S., Sottero, B., Biasi, F., Berta, G. N., Poli, G., et al. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.581 · Cited by 18

Spontaneous and Induced Nontransgenic Animal Models of AD

Kaushal, A., Wani, W. Y., Anand, R., & Gill, K. D. (2013) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/1533317513488914 · Cited by 18

Association of the C47T Polymorphism in SOD2 with Amnestic Mild Cognitive Impairment and Alzheimer’s Disease in Carriers of the APOEε4 Allele

Gamarra, D., Elcoroaristizabal, X., Martínez, M. F., & de Pancorbo, M. M. (2015) · Disease Markers · doi:10.1155/2015/746329 · Cited by 18

Inhibition of copper-mediated aggregation of human γD-crystallin by Schiff bases

Chauhan, P., Muralidharan, S., Velappan, A. B., Datta, D., Pratihar, S., Debnath, J., & Ghosh, K. S. (2017) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-016-1433-0 · Cited by 18

Insights into the Impact of a Membrane-Anchoring Moiety on the Biological Activities of Bivalent Compounds As Potential Neuroprotectants for Alzheimer’s Disease

Liu, H., Jiang, Y., Liu, K., Gómez‐Murcia, V., Ma, X., Torrecillas, A., Chen, Q., Zhu, X., Lesnefsky, E. J., Gómez-Fernández, J. C., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01284 · Cited by 18

Bivalent Compound 17MN Exerts Neuroprotection through Interaction at Multiple Sites in a Cellular Model of Alzheimer’s Disease

Liu, K., Chojnacki, J. E., Wade, E. E., Saathoff, J. M., Lesnefsky, E. J., Chen, Q., & Zhang, S. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150242 · Cited by 18

Unravelling of molecular biomarkers in synaptic plasticity of Alzheimer’s disease: Critical role of the restoration of neuronal circuits

Pinky, P., Neha, N., Ali, M., Tiwari, P., Alam, M. M., Hattiwale, H. M., Jamal, A., & Parvez, S. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102069 · Cited by 17

In silico and in vitro studies to elucidate the role of Cu 2+ and galanthamine as the limiting step in the amyloid beta (1–42) fibrillation process

Rodríguez, M. H., Correa‐Basurto, J., Benítez‐Cardoza, C. G., Reséndiz‐Albor, A. A., & Rosales‐Hernández, M. C. (2013) · Protein Science · doi:10.1002/pro.2319 · Cited by 17

Quantification of copper binding to amyloid precursor protein domain 2 and its Caenorhabditis elegans ortholog. Implications for biological function

Leong, S. L., Young, T. R., Barnham, K. J., Wedd, A. G., Hinds, M. G., Xiao, Z., & Cappai, R. (2013) · Metallomics · doi:10.1039/c3mt00258f · Cited by 17

Toxicity of 6-hydroxydopamine: live cell imaging of cytoplasmic redox flux

Dooley, C. T., Li, L., Misler, J. A., & Thompson, J. H. (2012) · Cell Biology and Toxicology · doi:10.1007/s10565-011-9209-3 · Cited by 18

Neuroinflammation and demyelination from the point of nitrosative stress as a new target for neuroprotection

Ljubisavljević, S., & Stojanović, I. R. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2014-0060 · Cited by 19

Molecular imaging of neurodegeneration by a novel cross-disease biomarker

Shirvan, A., Reshef, A., Yogev‐Falach, M., & Ziv, I. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.05.032 · Cited by 17

Inhibition of myeloperoxidase-mediated oxidative damage by nitrite in SH-SY5Y cells: Relevance to neuroprotection in neurodegenerative diseases

Lu, N., Ding, Y., Tian, R., & Peng, Y. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.03.042 · Cited by 16

Design, synthesis and in-vitro evaluation of fluorinated triazoles as multi-target directed ligands for Alzheimer disease

Dalvi, T., Dewangan, B., Agarwal, G., Suchita, D. S., Jain, A. K., Srivastava, A., & Sahu, B. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.127999 · Cited by 15

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

Effect of Normobaric Hyperoxia on Behavioral Deficits and Neuropathology in Alzheimer's Disease Mouse Model

Gao, B.-B., Long, Z., Zhao, L., & He, G. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110308 · Cited by 15

Degeneration Modulates Retinal Response to Transient Exogenous Oxidative Injury

Lederman, M., Hagbi-Levi, S., Grunin, M. A., Obolensky, A., Berenshtein, E., Banin, E., Chevion, M., & Chowers, I. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087751 · Cited by 15

Involvement of molecular chaperones and the transcription factor Nrf2 in neuroprotection mediated by para-substituted-4,5-diaryl-3-thiomethyl-1,2,4-triazines

Khodagholi, F., Ansari, N., Amini, M., & Tusi, S. K. (2012) · Cell Stress and Chaperones · doi:10.1007/s12192-011-0316-0 · Cited by 15

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

Salvianic borneol ester reduces β-amyloid oligomers and prevents cytotoxicity

Han, M., Liu, Y. M., Zhang, B., Qiao, J., Lu, W., Zhu, Y., Wang, Y., & Zhao, C. (2011) · Pharmaceutical Biology · doi:10.3109/13880209.2011.559585 · Cited by 14

Therapeutic potential of blackberry extract in the preventing memory deficits and neurochemical alterations in the cerebral cortex, hippocampus and cerebellum of a rat model with amnesia

de Mello, J. E., Luduvico, K. P., dos Santos, A., Teixeira, F. C., Cardoso, J. D. S., Soares, M. S. P., Cunico, W. J., Vizzotto, M., Stefanello, F. M., & Spanevello, R. M. (2023) · Metabolic Brain Disease · doi:10.1007/s11011-023-01175-w · Cited by 14

DNA low-density array analysis of colchicine neurotoxicity in rat cerebellar granular neurons

Yeste‐Velasco, M. (2008) · NeuroToxicology · doi:10.1016/j.neuro.2007.11.007 · Cited by 14

Reactive Oxygen Species in the Induction of Toxicity

Lenaz, G., & Strocchi, P. (2009) · Wiley eBooks · doi:10.1002/9780470744307.gat024 · Cited by 15

A Unified View of Assessing the Pro‐oxidant versus Antioxidant Nature of Amyloid Beta Conformers

Mitra, S., Prasad, P., & Chakraborty, S. (2018) · ChemBioChem · doi:10.1002/cbic.201800446 · Cited by 13

Protective effects of clioquinol on human neuronal-like cells: a new formulation of clioquinol-loaded PLGA microspheres for Alzheimer’s disease

Barcia, E., Salama, A., Fernández-Carballido, A. M., & Negro, S. (2010) · Journal of drug targeting · doi:10.3109/1061186x.2010.523789 · Cited by 13

Inhibitory effect of human serum albumin on Cu-induced Aβ40 aggregation and toxicity

Lu, N., Yang, Q., Li, J., Tian, R., & Peng, Y. (2015) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2015.10.020 · Cited by 13

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

Under Pressure: The Effect of Antioxidants on Health Consequences Related to Oxidative Stress

Patel, P. C., & Wolfe, M. T. (2020) · Entrepreneurship Theory and Practice · doi:10.1177/1042258720964184 · Cited by 12

Key roles of Tyr 10 in Cu bound Aβ complexes and its relevance to Alzheimer's disease

Lu, N., Li, J., & Gao, Z. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.07.009 · Cited by 12

Key Roles for Tyrosine 10 in Aβ–Heme Complexes and Its Relevance to Oxidative Stress

Lu, N., Li, J., Tian, R., & Peng, Y. (2014) · Chemical Research in Toxicology · doi:10.1021/tx5003035 · Cited by 12

Apolipoprotein E Highly Correlates with AβPP- and Tau-Related Markers in Human Cerebrospinal Fluid

Vuletic, S., Li, G., Peskind, E. R., Kennedy, H., Marcovina, S. M., Leverenz, J. B., Petrie, E. C., Lee, V. M.-Y., Galasko, D., Schellenberg, G. D., et al. (2008) · Journal of Alzheimer's Disease · doi:10.3233/jad-2008-15307 · Cited by 12

17β‐Oestradiol Stimulation of G‐Proteins in Aged and Alzheimer’s Human Brain: Comparison with Phytoestrogens

Jefremov, V., Rakitin, A., Mahlapuu, R., Zilmer, K., Bogdanović, N., Zilmer, M., & Karelson, E. (2008) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2008.01696.x · Cited by 12

Dual role of Cu2+ ions on the aggregation and degradation of soluble Aβ oligomers and protofibrils investigated by fluorescence spectroscopy and AFM

García, S. P., Cuscó, C., Brissos, R. F., Torrents, E., Caubet, A., & Gámez, P. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.07.007 · Cited by 12

Dietary interventions in mitigating the impact of environmental pollutants on Alzheimer’s disease – A review

Khandayataray, P., & Murthy, M. K. (2024) · Neuroscience · doi:10.1016/j.neuroscience.2024.11.020 · Cited by 11

Dysregulation of Metabolic Peptides in the Gut–Brain Axis Promotes Hyperinsulinemia, Obesity, and Neurodegeneration

Green, C., Zaman, V., Blumenstock, K., Banik, N. L., & Haque, A. (2025) · Biomedicines · doi:10.3390/biomedicines13010132 · Cited by 12

Effects of Sideritis scardica Extract on Scopolamine-Induced Learning and Memory Impairment in Mice

Lazarova, M. I., Tancheva, L. P., Tasheva, K. N., Denev, P. N., Uzunova, D. N., Stefanova, M. O., Tsvetanova, E. R., Georgieva, A. P., & Kalfin, R. E. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230017 · Cited by 10

Age- and sex-associated alterations in hypothalamic mitochondrial bioenergetics and inflammatory-associated signaling in the 3xTg mouse model of Alzheimer’s disease

Adlimoghaddam, A., Fontaine, K. M., & Albensi, B. C. (2024) · Biology of Sex Differences · doi:10.1186/s13293-024-00671-7 · Cited by 11

Phytocompounds of Senecio candicans as potential acetylcholinesterase inhibitors targeting Alzheimer's disease: A structure-based virtual screening and molecular dynamics simulation study

Periyasamy, T. S., Chandrasekar, A. K., Roy, G., Sekar, N., & Lakshmanan, H. (2025) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2025.108396 · Cited by 9

Mechanistic Insight of Bivalent Compound 21MO as Potential Neuroprotectant for Alzheimer’s Disease

Saathoff, J. M., Liu, K., Chojnacki, J. E., Liu, H., Chen, Q., Lesnefsky, E. J., & Zhang, S. (2016) · Molecules · doi:10.3390/molecules21040412 · Cited by 9

Evaluation of Mitochondrial Oxidative Stress in the Brain of a Transgenic Mouse Model of Alzheimer’s Disease by in vitro Electron Paramagnetic Resonance Spectroscopy

Manabe, T., Matsumura, A., Yokokawa, K., Saito, T., Fujikura, M., Iwahara, N., Matsushita, T., Suzuki, S., Hisahara, S., Kawamata, J., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180985 · Cited by 9

The impact of proteostasis dysfunction secondary to environmental and genetic causes on neurodegenerative diseases progression and potential therapeutic intervention

Elmatboly, A. M., Sherif, A., Deeb, D. A., Benmelouka, A. Y., Bin-Jumah, M. N., Aleya, L., & Abdel‐Daim, M. M. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-020-07914-1 · Cited by 9

Protective effects of Huperzia serrata and its components against oxidative damage and cognitive dysfunction

Ohba, T., Nakamura, S., Shimazawa, M., Hayashi, Y., Kono, H., & Hara, H. (2020) · PharmaNutrition · doi:10.1016/j.phanu.2020.100203 · Cited by 8

The effect of Fenton reaction on protease-resistant prion protein (PrPSc) degradation and scrapie infectivity

Park, S.-J., Kim, N., Jeong, B., Jin, J., Choi, J.-K., Park, Y.-J., Kim, J., Carp, R. I., & Kim, Y. (2008) · Brain Research · doi:10.1016/j.brainres.2008.07.117 · Cited by 8

Cognitive Symptoms and Welding Fume Exposure

Ross, J., Macdiarmid, J. I., Semple, S. E., WATT, S. J., Moir, G., & Henderson, G. (2012) · The Annals of Occupational Hygiene · doi:10.1093/annhyg/mes042 · Cited by 8

Cytotoxicity and antioxidant activities of leaf extracts of Varthemia sericea (Batt. et Trab.) Diels

Dehimat, A., Azizi, I., Barragan‐Montero, V., & Khettal, B. (2021) · European Journal of Integrative Medicine · doi:10.1016/j.eujim.2021.101338 · Cited by 8

Novel Positron Emission Tomography Radiotracers for Imaging Mitochondrial Complex I

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Spectroscopic study on the interaction of Aβ42 with di(picolyl)amine derivatives and the toxicity to SH-S5Y5 cells

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