The DOI matches its Crossref record; 58 of the 59 references it cites were found in a registry or an index.
Oxidative Damage Is the Earliest Event in Alzheimer Disease
Open accessAbstract
Recently, we demonstrated a significant increase of an oxidized nucleoside derived from RNA, 8-hydroxyguanosine (8OHG), and an oxidized amino acid, nitrotyrosine in vulnerable neurons of patients with Alzheimer disease (AD). To determine whether oxidative damage is an early- or end-stage event in the process of neurodegeneration in AD, we investigated the relationship between neuronal 8OHG and nitrotyrosine and histological and clinical variables, i.e. amyloid-beta (A beta) plaques and neurofibrillary tangles (NFT), as well as duration of dementia and apolipoprotein E (ApoE) genotype. Our findings show that oxidative damage is quantitatively greatest early in the disease and reduces with disease progression. Surprisingly, we found that increases in A beta deposition are associated with decreased oxidative damage. These relationships are more significant in ApoE epsilon4 carriers. Moreover, neurons with NFT show a 40%-56% decrease in relative 8OHG levels compared with neurons free of NFT. Our observations indicate that increased oxidative damage is an early event in AD that decreases with disease progression and lesion formation. These findings suggest that AD is associated with compensatory changes that reduce damage from reactive oxygen.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Past and recent studies have demonstrated that oxidative damage is not only an early event in the pathogenesis of AD, occurring before the onset of clinical symptoms but also a factor contributing to the disease progression [17,18,19,20,21].”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [19]
In the citing paper
“In the brains of individuals with AD and preclinical AD (i.e., evidence of Aβ and tau deposition in the brain without any clinical manifestation of the disease), as well as patients with MCI (a mild clinical impairment with no proof of underlying pathology with biomarkers), many oxidative damage products are measured, and numerous investigations have pointed to OS as a key and early player in the”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [19]
In the citing paper
“In the AD brain, mitochondria can be sources of ROS and also the target of OS, especially mitochondrial DNA (mtDNA) is susceptible to oxidative damage [19,53,63].”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [19]
In the citing paper
“Oxidative damage to RNA in EC, hippocampus, subiculum, and temporal neocortex of subjects with AD has been described. The levels of 8-OHdG increase early before pathological changes occur, and this can explain that the selective vulnerability of neurons in the EC during AD may be related to the vulnerability of these particular neurons to oxidative damage [19].”
From Role of Oxidative Damage in Alzheimer’s Disease and Neurodegeneration: From Pathogenic Mechanisms to Biomarker Discovery (2021) · cites this paper as [19]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Theory and Practice of Histological Techniques
Bancroft, J. D., & Gamble, M. (1990) · Cited by 6,948
Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961
Restriction isotyping of human apolipoprotein E by gene amplification and cleavage with HhaI.
Hixson, J., & Vernier, D. (1990) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)43176-1 · Cited by 2,933
Consortium to Establish a Registry for Alzheimer's Disease (CERAD)
Fillenbaum, G., & Heyman, A. (2002) · doi:10.1002/0470846410.ch42(iii · Cited by 2,859
Diagnosis of Alzheimer's Disease
Khachaturian, Z. S. (1985) · Archives of Neurology · doi:10.1001/archneur.1985.04060100083029 · Cited by 2,499
Hydrogen peroxide mediates amyloid β protein toxicity
Behl, C. (1994) · Cell · doi:10.1016/0092-8674(94)90131-7 · Cited by 2,074
Mitochondrial abnormalities in Alzheimer's disease
Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367
Self-citationReiman, E. M., Caselli, R. J., Yun, L. S., Chen, K., Bandy, D., Minoshima, S., Thibodeau, S. N., & Osborne, D. (1996) · New England Journal of Medicine · doi:10.1056/nejm199603213341202 · Cited by 1,366
Strittmatter, W. J., Weisgraber, K. H., Huang, D. Y., Dong, L. M., Salvesen, G. S., Pericak-Vance, M., Schmechel, D., Saunders, A. M., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8098 · Cited by 1,363
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
Research works printed but not linked: 2
- Smith, 1998, ApoE: Isoform specific antioxidant activity [abstract], Neurobiol Aging, 19, S222
- Nunomura, 2000, Increasing amyloid ß 42 deposition is associated with decreasing neuronal RNA oxidation in Down's syndrome and familial Alzheimer's disease [abstract], Brain pathol, 10, 783
Cited by
Sorted by citations
Items 901–1,000 of 1,005
The Role of Oxidative Stress in Alzheimer ’ s Disease
Madeo, J. (2013) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.1000116 · Cited by 44
Persson, T., Lattanzio, F., Calvo‐Garrido, J., Rimondini, R., Rubio-Rodrigo, M., Sundström, E., Maioli, S., Matton, A., & Cedazo-Mı́nguez, Á. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150738 · Cited by 44
Shin, C. M., Chung, Y. H., Kim, M. J., Lee, E. Y., Kim, E., & Ik, C. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03391-1 · Cited by 44
Balogiannis, S., Mavroudis, I. A., Manolides, S. L., & Manolides, L. S. (2009) · Acta Oto-Laryngologica · doi:10.1080/00016480802579074 · Cited by 44
Amyloid-β: a (life) preserver for the brain
Obrenovich, M. E., Joseph, J. A., Atwood, C., Perry, G. L., & Smith, M. A. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00038-6 · Cited by 44
Self-citationOxidative stress and iron imbalance in Alzheimer disease: How rust became the fuss!
Smith, M. A. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s334 · Cited by 44
Self-citationEstrogen Bows to a New Master: The Role of Gonadotropins in Alzheimer Pathogenesis
Webber, K. M., Casadesús, G., Marlatt, M. W., Perry, G. L., Hamlin, C. R., Atwood, C., Bowen, R. L., & Smith, M. A. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1347.020 · Cited by 44
Self-citationPolis, B., & Samson, A. O. (2024) · Journal of Alzheimer's Disease · doi:10.3233/jad-240058 · Cited by 43
Strazielle, C., Jazi, R., Verdier, Y., Qian, S., & Lalonde, R. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.08.005 · Cited by 43
Ceruloplasmin and iron in Alzheimer’s disease and Parkinson’s disease: a synopsis of recent studies
Snædal, J., Kristinsson, J. R., Johannesson, & Tórsdóttir, G. (2012) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s34729 · Cited by 43
Villeneuve, L. M., Purnell, P. R., Stauch, K. L., Callen, S. E., Buch, S. J., & Fox, H. S. (2016) · Journal of NeuroVirology · doi:10.1007/s13365-016-0424-9 · Cited by 43
Role of σ1 Receptors in Learning and Memory and Alzheimer’s Disease-Type Dementia
Maurice, T., & Goguadze, N. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-50174-1_15 · Cited by 43
Amburana cearensis: Pharmacological and Neuroprotective Effects of Its Compounds
Silva, J. H. C. E., Ferreira, R. S., Pereira, É. P. L., Braga‐de‐Souza, S., de Almeida, M. M. A., dos Santos, C. C., Butt, A. M., Caiazzo, E., Capasso, R., da Silva, V. D. A., et al. (2020) · Molecules · doi:10.3390/molecules25153394 · Cited by 43
Nerve Growth Factor-Based Therapy in Alzheimer’s Disease and Age-Related Macular Degeneration
Amadoro, G., Latina, V., Balzamino, B. O., Squitti, R., Varano, M., Calissano, P., & Micera, A. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.735928 · Cited by 44
Casadesús, G., Shukitt‐Hale, B., Stellwagen, H. M., Smith, M. E., Rabin, B. S., & JOSEPH, J. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.09.007 · Cited by 43
Self-citationProlonged coenzyme Q10 treatment in Down syndrome patients, effect on DNA oxidation
Tiano, L., Padella, L., Santoro, L., Carnevali, P., Principi, F., Brugè, F., Gabrielli, O., & Littarru, G. P. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.03.025 · Cited by 43
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
Self-citationProtective roles of quinone reductase and tamoxifen against estrogen-induced mammary tumorigenesis
Montano, M. M., Chaplin, L. J., Deng, H., Mesía-Vela, S., Gaikwad, N. W., Zahid, M., & Rogan, E. G. (2006) · Oncogene · doi:10.1038/sj.onc.1210144 · Cited by 43
Sublethal RNA Oxidation as a Mechanism for Neurodegenerative Disease
Castellani, R. J., Nunomura, A., Rolston, R. K., Moreira, P. I., Takeda, A., Perry, G. L., & Smith, M. A. (2008) · International Journal of Molecular Sciences · doi:10.3390/ijms9050789 · Cited by 43
Self-citationHuman Aβ1–42 reduces iron‐induced toxicity in rat cerebral cortex
Bishop, G. M., & Robinson, S. R. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10661 · Cited by 43
Ma, Q., Ruan, Y., Xu, H. Y., Shi, X., Wang, Z., & Hu, Y. (2015) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2015.10.004 · Cited by 43
Implication of the transcription factor E2F-1 in the modulation of neuronal apoptosis
Verdaguer, E., Susana, G. D. A., Allgaier, C., Pallàs, M., & Camins, A. (2006) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2006.11.001 · Cited by 43
HARTZLER, A., ZHU, X., SIEDLAK, S., CASTELLANI, R., AVILA, J., PERRY, G., & SMITH, M. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00029-5 · Cited by 43
Self-citationNeuroprotective Roles of the Reverse Transsulfuration Pathway in Alzheimer’s Disease
Paul, B. D. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.659402 · Cited by 42
Varas, N. A., Abate, G., Prandelli, C., Martínez, C., Cuetos, F., Menéndez‐González, M., Marziano, M., Cabrera-García, D., Fernández‐Sánchez, M. T., Novelli, A., et al. (2016) · Current Alzheimer Research · doi:10.2174/1567205013666161010125413 · Cited by 42
Waller, R., Murphy, M., Garwood, C. J., Jennings, L. R., Heath, P. R., Chambers, A., Matthews, F. E., Brayne, C., Ince, P. G., Wharton, S. B., et al. (2018) · Glia · doi:10.1002/glia.23465 · Cited by 42
Review Paper: Tau Pathology of Alzheimer Disease: Possible Role of Sleep Deprivation
Ahmadian, N., Hejazi, S., Mahmoudi, J., & Talebi, M. (2018) · Basic and Clinical Neuroscience Journal · doi:10.32598/bcn.9.5.307 · Cited by 42
Role of RNA Oxidation in Neurodegenerative Diseases
Liu, Z., Chen, X., Li, Z., Ye, W., Ding, H., Li, P., & Aung, L. H. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145022 · Cited by 42
Mišković, J., Karaman, M. A., Rašeta, M., Krsmanović, N., Berežni, S., Jakovljević, D. M., Piattoni, F., Zambonelli, A., Gargano, M. L., & Venturella, G. (2021) · Journal of Fungi · doi:10.3390/jof7020115 · Cited by 42
Mizuno, Y., Abolhassani, N., Mazzei, G., Sakumi, K., Saito, T., Saido, T. C., Ninomiya, T., Iwaki, T., Yamasaki, R., Kira, J., et al. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8635088 · Cited by 42
Therapeutic Potential of Ferulic Acid in Alzheimer's Disease
Türkez, H., Arslan, M. E., Barboza, J. N., Kahraman, Ç. Y., de Sousa, D. P., & Mardinoğlu, A. (2021) · Current Drug Delivery · doi:10.2174/1567201819666211228153801 · Cited by 42
Dudás, B., Hanin, I., Rose, M., & Wülfert, E. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.11.001 · Cited by 42
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
Self-citationAging Brain: Prevention of Oxidative Stress by Vitamin E and Exercise
Devi, S. A. (2009) · The Scientific World JOURNAL · doi:10.1100/tsw.2009.46 · Cited by 42
Uranga, R. M., Giusto, N. M., & Salvador, G. A. (2009) · Toxicological Sciences · doi:10.1093/toxsci/kfp152 · Cited by 42
Reactive Oxygen Species in Diabetes-induced Vascular Damage, Stroke, and Alzheimer's Disease
Muhammad, S., Bierhaus, A., & Schwaninger, M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0982 · Cited by 42
Recuero, M., Vicente, M. C., Martı́nez-Garcı́a, A., Ramos, M. C., Carmona‐Sáez, P., Sastre, I., Aldudo, J., Vilella, E., Frank, A., Bullido, M. J., et al. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00457.x · Cited by 42
Andersen, J. M., Myhre, O., & Fonnum, F. (2003) · Neurochemical Research · doi:10.1023/a:1022389503105 · Cited by 42
Sultana, R., Robinson, R. A. S., Di Domenico, F., Abdul, H. M., Clair, D. K. S., Markesbery, W. R., Cai, J., Pierce, W. M., & Butterfield, D. A. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.015 · Cited by 41
Retinoic acid isomers protect hippocampal neurons from amyloid-β induced neurodegeneration
Sahin, M., Karaüzüm, S. B., Perry, G., Smith, M. A., & Alicigüzel, Y. (2005) · Neurotoxicity Research · doi:10.1007/bf03036453 · Cited by 41
Self-citationThe Latest Advances in the Diagnosis and Treatment of Dementia
Hafiz, R., Alajlani, L., Ali, A., Algarni, G. A., Aljurfi, H., Alammar, O. A. M., Ashqan, M. Y., & Alkhashan, A. Y. (2023) · Cureus · doi:10.7759/cureus.50522 · Cited by 41
Li, Y.-P., Yang, G., Jin, L., Yang, H., Chen, J., Chai, G., & Wang, L. (2015) · Brain Research · doi:10.1016/j.brainres.2015.05.031 · Cited by 41
Hunter, S., Arendt, T., & Brayne, C. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8445-3 · Cited by 41
Anderson, G., & Maes, M. H. J. (2017) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527315666161122144659 · Cited by 41
Tian, X., Xie, B., Zou, Z., Jiao, Y., Lin, L., Chen, C., Hsu, C., Peng, J., & Yang, Z. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b02792 · Cited by 41
Liu, S., Li, Y., Yi, F., Liu, Q., Chen, N., He, X., He, C., & Xiao, P. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.112983 · Cited by 41
Akter, R., Chowdhury, M. A. R., & Rahman, M. H. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666201102102810 · Cited by 41
A review on α-mangostin as a potential multi-target-directed ligand for Alzheimer's disease
Yang, A., Liu, C., Wu, J., Kou, X., & Shen, R. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173950 · Cited by 41
Association of vitamin E intake in diet and supplements with risk of dementia: A meta-analysis
Zhao, R., Han, X., Zhang, H., Liu, J., Zhang, M., Zhao, W., Jiang, S., Li, R., Cai, H., & You, H. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.955878 · Cited by 41
Hernández‐Damián, J., Andérica‐Romero, A. C., & Pedraza‐Chaverrí, J. (2014) · Archiv der Pharmazie · doi:10.1002/ardp.201400159 · Cited by 41
Novel therapeutics for Alzheimer's disease: an update.
Bonda, D., Lee, H. P., Lee, H., Friedlich, A. L., Perry, G. L., Zhu, X., & Smith, M. A. (2010) · PubMed · Cited by 41
Self-citationMurakami, Y., Ikeda, Y., Yoshida, N., Notomi, S., Hisatomi, T., Oka, S., Luca, G. D., Yonemitsu, Y., Bignami, M., Nakabeppu, Y., et al. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.06.026 · Cited by 41
Porcellotti, S., Fanelli, F., Fracassi, A., Sepe, S., Cecconi, F., Bernardi, C., Cimini, A., Cerù, M. P., & Moreno, S. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/967203 · Cited by 41
Oxidative stress action in cellular aging
de Oliveira, M. C., & Schoffen, J. P. F. (2010) · Brazilian Archives of Biology and Technology · doi:10.1590/s1516-89132010000600009 · Cited by 41
Santa‐María, I., Smith, M. A., Perry, G. L., Hernández, F., Ávila, J., & Moreno, F. J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.11.024 · Cited by 41
Self-citationMetallostasis and amyloid β-degrading enzymes
Grasso, G., Giuffrida, M. L., & Rizzarelli, E. (2012) · Metallomics · doi:10.1039/c2mt20105d · Cited by 41
Alzheimer?s disease: the impact of age-related changes in reproductive hormones
Casadesús, G., Atwood, C., Zhu, X., Hartzler, A., Webber, K. M., Perry, G. L., Bowen, R. L., & Smith, M. A. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4384-0 · Cited by 41
Self-citationMartínez de Toda, I., Miguélez, L., Vida, C., Carro, E., & De la Fuente, M. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190198 · Cited by 40
Ulusu, N. N. (2015) · Medical Hypotheses · doi:10.1016/j.mehy.2015.05.006 · Cited by 40
Lou, G., ZHANG, Q.-H., Xiao, F., Xiang, Q., Su, Z., Zhang, L., Yang, P., Yang, Y. F., Zheng, Q., & Huang, Y. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.08.003 · Cited by 40
Kalandar, A. (2016) · Advances in neurobiology · doi:10.1007/978-3-319-28383-8_18 · Cited by 40
Nagata, Y., Hirayama, A., Ikeda, S., Shirahata, A., Shoji, F., Maruyama, M., Kayano, M., Bundo, M., Hattori, K., Yoshida, S., et al. (2018) · Biomarker Research · doi:10.1186/s40364-018-0119-x · Cited by 42
The human brainome: network analysis identifies HSPA2 as a novel Alzheimer’s disease target
Petyuk, V., Chang, R. R., Ramirez‐Restrepo, M., Beckmann, N. D., Henrion, M., Piehowski, P., Zhu, K., Wang, S., Clarke, J., Huentelman, M. J., et al. (2018) · Brain · doi:10.1093/brain/awy215 · Cited by 40
Traumatic Brain Injury and Suicidal Behavior: A Review
Wadhawan, A., Stiller, J. W., Potocki, E., Okusaga, O. O., Dagdag, A., Lowry, C. A., Benros, M. E., & Postolache, T. T. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181055 · Cited by 40
Upregulation of Cisd2 attenuates Alzheimer's‐related neuronal loss in mice
Chen, Y., Chou, T., Lin, I., Chen, C., Kao, C., Huang, G., Chen, L., Wang, P., Lin, C., & Tsai, T. (2019) · The Journal of Pathology · doi:10.1002/path.5374 · Cited by 40
Hin, N., Newman, M., Kaslin, J., Douek, A. M., Lumsden, A. L., Nik, S. H. M., Dong, Y., Zhou, X., Manucat-Tan, N. B., Ludington, A. J., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0227258 · Cited by 40
Alterations in oxidative stress biomarkers associated with mild hyperlipidemia and smoking
Miri, R., Saadati, H., Ardi, P., & Firuzi, O. (2011) · Food and Chemical Toxicology · doi:10.1016/j.fct.2011.12.031 · Cited by 40
Moskovitz, J., Du, F., Bowmann, C. F., & Yan, S. S. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00453.2015 · Cited by 40
Hicks, J., Lai, Y., Sheng, W., Yang, X., Zhu, D., Sun, G. Y., & Lee, J. C. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.07.027 · Cited by 40
Dietary Lipids in the Aetiology of Alzheimer???s Disease
Cooper, J. L. (2003) · Drugs & Aging · doi:10.2165/00002512-200320060-00001 · Cited by 40
Luteolin: Nature's promising warrior against Alzheimer's and Parkinson's disease
Goyal, A., Solanki, K., & Verma, A. (2023) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23619 · Cited by 39
Three Postulates to Help Identify the Cause of Alzheimer's Disease
de la Torre, J. C. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101884 · Cited by 39
Oxidative damage is present in the fatal brain edema of diabetic ketoacidosis
Hoffman, W. H., Siedlak, S. L., Wang, Y., Castellani, R. J., & Smith, M. A. (2010) · Brain Research · doi:10.1016/j.brainres.2010.10.085 · Cited by 39
Self-citationLipiński, B., & Pretorius, E. (2013) · Frontiers in Human Neuroscience · doi:10.3389/fnhum.2013.00735 · Cited by 39
Isorhynchophylline alleviates learning and memory impairments induced by aluminum chloride in mice
Li, H., Ip, S., Zheng, G., Xian, Y., & Lin, Z. (2018) · Chinese Medicine · doi:10.1186/s13020-018-0187-8 · Cited by 39
Current Therapeutic Targets for Alzheimer's Disease
Chaudhary, A., Maurya, P. K., Yadav, B. S., Singh, S., & Mani, A. (2018) · Journal of Biomedicine · doi:10.7150/jbm.26783 · Cited by 39
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
Relation of Plasma Selenium and Lipid Peroxidation End Products in Patients With Alzheimer’s Disease
Chmátalová, Z., Vyhnálek, M., Laczó, J., Hort, J., POSPISILOVA, R., Pechová, M., & Skoumalová, A. (2017) · Physiological Research · doi:10.33549/physiolres.933601 · Cited by 39
Xiong, Y., Ruan, Y.-T., Zhao, J., Yang, Y., Chen, L., Mai, Y., Yu, Q., Cao, Z., Liu, F., Liao, W., et al. (2022) · World Journal of Psychiatry · doi:10.5498/wjp.v12.i3.410 · Cited by 39
Staging anti-inflammatory therapy in Alzheimer’s disease
Lichtenstein, M. P. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00142 · Cited by 39
Cerebral Arachidonate Cascade in Dementia: Alzheimers Disease and Vascular Dementia
Yagami, T. (2005) · Current Neuropharmacology · doi:10.2174/157015906775203011 · Cited by 39
Effects of HNE‐modification induced by Aβ on neprilysin expression and activity in SH‐SY5Y cells
Wang, R., Wang, S., Malter, J. S., & Wang, D. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05855.x · Cited by 39
Krüger, J., Hinttala, R., Majamaa, K., & Remes, A. M. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-8 · Cited by 39
Bonda, D., Liu, G., Men, P., Perry, G. L., Smith, M. A., & Zhu, X. (2012) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152712799960709 · Cited by 39
Self-citationPhenylpropanoids and Alzheimer's disease: A potential therapeutic platform
Kolaj, I., Liyanage, S. I., & Weaver, D. F. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2018.08.001 · Cited by 39
The common marmoset as a model of neurodegeneration
Perez‐Cruz, C., & Rodríguez-Callejas, J. D. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.02.002 · Cited by 39
Krstic, D., & Knuesel, I. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-62 · Cited by 38
Mitoproteomics: Tackling Mitochondrial Dysfunction in Human Disease
Gómez‐Serrano, M., Camafeita, E., Loureiro, M., & Peral, B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1435934 · Cited by 38
Oyeleke, M. B., & Owoyele, B. V. (2022) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2022.114997 · Cited by 38
Atwood, C., & Bowen, R. L. (2015) · Hormones and Behavior · doi:10.1016/j.yhbeh.2015.06.021 · Cited by 38
Self-citationObrenovich, M. E., Palacios, H. H., Gasimov, E. K., Leszek, J., & Aliev, G. (2009) · Cardiovascular Psychiatry and Neurology · doi:10.1155/2009/327360 · Cited by 38
Self-citationMitigation of ROS Insults by Streptomyces Secondary Metabolites in Primary Cortical Neurons
Leirós, M., Alonso, E., Sánchez, J. A., Rateb, M. E., Ebel, R., Houssen, W. E., Jaspars, M., Alfonso, A., & Botana, L. M. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn4001878 · Cited by 38
Yang, T.-T., Hsu, C.-T., & Kuo, Y. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0311-0 · Cited by 38
Reactive oxygen: its sources and significance in Alzheimer disease
Perry, G. L., Nunomura, A., Cash, A., Taddeo, M. A., Hirai, K., Aliev, G., Ávila, J., Wataya, T., Shimohama, S., Atwood, C., et al. (2002) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-7091-6139-5_7 · Cited by 38
Self-citationMultimodal drugs and their future for Alzheimer's and Parkinson's disease
der Schyf, C. J. V., & Geldenhuys, W. J. (2011) · International review of neurobiology · doi:10.1016/b978-0-12-386467-3.00006-6 · Cited by 38
Tau phosphorylation and assembly
Gómez‐Ramos, A., Smith, M. A., Perry, G. L., & Ávila, J. (2004) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2004-1489 · Cited by 38
Self-citationDo glutathione and copper interact to modify Alzheimer's disease pathogenesis?
Ho, T., Ahmadi, S., & Kerman, K. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.01.025 · Cited by 37
Aldred, S., Bennett, S. J., & Mecocci, P. (2009) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2009.08.021 · Cited by 37
Luo, J., Lee, S., VandeVrede, L. A., Qin, Z., Aissa, M. B., Larson, J., Teich, A. F., Arancio, O., D’Souza, Y., Elharram, A., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0103-6 · Cited by 37
Cerium Oxide Nanoparticles for the Treatment of Neurological Oxidative Stress Diseases
Estevez, A. Y., & Erlichman, J. S. (2011) · ACS symposium series · doi:10.1021/bk-2011-1083.ch009 · Cited by 37
Metadata
- Authors
- Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., Chiba, S., Atwood, C. S., Petersen, R. B., & Smith, M. A.
- Affiliations
- Asahikawa Medical University (JP)
- Case Western Reserve University (US)
- Takeda (Japan) (JP)
- Sensei Biotherapeutics (United States) (US)
- Kyoto University (JP)
- Corresponding author
- Nunomura, Akihiko
- ORCID
- Venue
- Journal of Neuropathology & Experimental Neurology
- Publisher
- Oxford University Press (OUP)
- Published
- 2001-08
- Volume
- 60
- Issue
- 8
- Pages
- 759-767
- ISSN
- 0022-3069 (ISSN-L)
- 1554-6578
- OpenAlex
- W1542215809
- Cited by
- 1,885
- References
- 59
- Citations by year
- 2026: 46 · 2025: 31 · 2024: 52 · 2023: 61 · 2022: 80 · 2021: 98 · 2020: 86 · 2019: 82 · 2018: 69 · 2017: 73 · 2016: 70 · 2015: 83 · 2014: 86 · 2013: 86 · 2012: 104
- FWCI
- 33.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuropathology & Experimental Neurology (publishedVersion)
- PubMed (publishedVersion)
- Asahikawa Medical University Collection and Research (Asahikawa Medical University) (submittedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Funders
- Alzheimer's Association
- National Institutes of Health (5r01ag009287-08, AG09287)
- Japan Society for the Promotion of Science (12670918)
- National Institute on Aging (AG-14249, R01AG014249, AG 09287)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, oxidative damage, 8-hydroxyguanosine, nitrotyrosine, amyloid plaques, neurofibrillary tangles, APOE ε4, disease progression, neurodegeneration, reactive oxygen species, RNA oxidation
- MeSH terms
- Aged, Alzheimer Disease, Apolipoproteins E, Brain, Female, Genotype, Guanosine, Heterozygote, Humans, Male, Middle Aged, Neurons, Tyrosine, Amyloid beta-Peptides, Neurofibrillary Tangles, Oxidative Stress, Disease Progression, Plaque, Amyloid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
