Cited by 777Alzheimer's disease research and treatmentsAntioxidant Activity and Oxidative StressDementia and Cognitive Impairment Research

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

Increased Lipid Peroxidation Precedes Amyloid Plaque Formation in an Animal Model of Alzheimer Amyloidosis

Open access

Praticò, Domenico, Uryu, Kunihiro, Leight, Susan, Trojanoswki, John Q., Lee, Virginia M.-Y.·2001·The Journal of Neuroscience

DOI 10.1523/jneurosci.21-12-04183.2001PMC PMC6762743

Open this paper in CoChat — free account Open PDF

Abstract

Oxidative stress is a key feature in the Alzheimer's disease (AD) brain and manifests as lipid peroxidation (LPO). Isoprostanes (iPs) are specific and sensitive markers of in vivo LPO. To determine whether amyloid beta (Abeta) deposition in vivo is associated with increased LPO, we examined iP levels in a transgenic mouse model (Tg2576) of AD amyloidosis. Urine, plasma, and brain tissues were collected from Tg2576 and littermate wild-type (WT) animals at different time points starting at 4 months of age and continuing until 18 months of age. Levels of urinary 8,12-iso-iPF(2alpha)-VI were higher in Tg2576 than in WT animals as early as 8 months of age and remained this high for the rest of the study. A similar pattern was observed for plasma levels of 8,12-iso-iPF(2alpha)-VI. Homogenates from the cerebral cortex and hippocampus of Tg2576 mice had higher levels of 8,12-iso-iPF(2alpha)-VI than those from WT mice starting at 8 months of age. In contrast, a surge of Abeta 1-40 and 1-42 levels as well as Abeta deposits in Tg2576 mouse brains occurred later, at 12 months of age. A direct correlation was observed between brain 8,12-iso-iPF(2alpha)-VI and Abeta 1-40 and 1-42. Because LPO precedes amyloid plaque formation in Tg2576 mice, this suggests that brain oxidative damage contributes to AD pathogenesis before Abeta accumulation in the AD brain.

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

Crossref · 10.1523/jneurosci.21-12-04183.2001

Cites

24 of 24 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
The measurement and mechanism of lipid peroxidation in biological systems
Gutteridge, J. M. C., & Halliwell, B. B. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90206-q · Cited by 1,297
Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease
Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · cited 4×
“Indeed, the recent demonstration of rare Ab plaques as well as scant amounts of formic acid-extractable Ab in 8-month-old Tg2576 mouse brains prompts cautious interpretation of our data with respect to whether LPO precedes or is linked to the initial stages of AD-like amyloidosis in Tg2576 mice ( Kawarabayashi et al.,…”
BackgroundInfluential
Antioxidants, Oxidative Stress, and Degenerative Neurological Disorders
Floyd, R. A. (1999) · Proceedings of The Society for Experimental Biology and Medicine · doi:10.1046/j.1525-1373.1999.d01-140.x · Cited by 828
Oxidative Alterations in Alzheimer's Disease
Markesbery, W. R., & Carney, J. M. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00215.x · Cited by 789
Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain
Gravina, S. A., Ho, L., Eckman, C. B., Long, K. E., Otvos, L., Younkin, L. H., Suzuki, N., & Younkin, S. G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7013 · Cited by 676
APPSW Transgenic Mice Develop Age-related Aβ Deposits and Neuropil Abnormalities, but no Neuronal Loss in CA1
IRIZARRY, M. C., MCNAMARA, M., FEDORCHAK, K., HSIAO, K., & HYMAN, B. T. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199709000-00002 · Cited by 649
Amyloid‐β Deposition in Alzheimer Transgenic Mice Is Associated with Oxidative Stress
Smith, M. A., Hirai, K., Hsiao, K., Pappolla, M. A., Harris, P. L. R., Siedlak, S. L., Tabaton, M., & Perry, G. L. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70052212.x · Cited by 547
Age-related CNS disorder and early death in transgenic FVB/N mice overexpressing Alzheimer amyloid precursor proteins
Hsiao, K., Borchelt, D., Olson, K., Johannsdottir, R., Kitt, C. A., Yunis, W. S., Xu, S., Eckman, C., Younkin, S. G., Price, D., et al. (1995) · Neuron · doi:10.1016/0896-6273(95)90107-8 · Cited by 527
Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid β-peptide
Yan, S. D., Yan, S. F., Chen, X., Fu, J., Chen, M., Kuppusamy, P., Smith, M. A., Perry, G., Godman, G. C., Nawroth, P., et al. (1995) · Nature Medicine · doi:10.1038/nm0795-693 · Cited by 406

Show all 24 references

Research works printed but not linked: 1

Pappolla, 1998, Evidence of oxidative stress and in vivo neurotoxicity of β-amyloid in a transgenic mouse model of Alzheimer's disease., Am J Pathol, 152, 871

Sorted by citations

Items 401–500 of 776

Assessment of diets containing curcumin, epigallocatechin-3-gallate, docosahexaenoic acid and α-lipoic acid on amyloid load and inflammation in a male transgenic mouse model of Alzheimer's disease: Are combinations more effective?
Sharman, M. J., Gyengési, E., Liang, H., Chatterjee, P., Karl, T., Li, Q.-X., Wenk, M. R., Halliwell, B. B., Martins, R. N., & Münch, G. W. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.11.026 · Cited by 46
Mitochondrial DNA variants in a Japanese population of patients with Alzheimer’s disease
Tanaka, N., Goto, Y., Akanuma, J., Kato, M., Kinoshita, T., Yamashita, F., Tanaka, M., & Asada, T. (2009) · Mitochondrion · doi:10.1016/j.mito.2009.08.008 · Cited by 46
Generation of reactive oxygen species by beta amyloid fibrils and oligomers involves different intra/extracellular pathways
Cenini, G., Cecchi, C., Pensalfini, A., Bonini, S. A., Ferrari‐Toninelli, G., Liguri, G., Memo, M., & Uberti, D. L. (2009) · Amino Acids · doi:10.1007/s00726-009-0319-7 · Cited by 45
Synaptoproteomics of learned helpless rats involve energy metabolism and cellular remodeling pathways in depressive-like behavior and antidepressant response
Mallei, A., Giambelli, R., Gass, P., Racagni, G., Mathé, A. A., Vollmayr, B., & Popoli, M. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.12.012 · Cited by 44
Soluble semicarbazide-sensitive amine oxidase (SSAO) activity is related to oxidative stress and subchronic inflammation in streptozotocin-induced diabetic rats
Somfai, G. M., Knippel, B., Ruzicska, É., Stadler, K., Tóth, M., Salacz, G., Magyar, K., & Somogyi, A. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2005.12.009 · Cited by 44
Misfolded protein oligomers induce an increase of intracellular Ca2+ causing an escalation of reactive oxidative species
Fani, G., Torre, C. E. L., Cascella, R., Cecchi, C., Vendruscolo, M., & Chiti, F. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04513-w · Cited by 44
Combining an Antioxidant‐Fortified Diet with Behavioral Enrichment Leads to Cognitive Improvement and Reduced Brain Pathology in Aging Canines
Head, E. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1396.004 · Cited by 44
Nootropic effect of neferine on aluminium chloride–induced Alzheimer's disease in experimental models
Shuaizeng, Y., Ran, Q., Yang, J., Zhao, Y., & Li, C. (2019) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22429 · Cited by 43
Atorvastatin and pitavastatin reduce oxidative stress and improve IR/LDL-R signals in Alzheimer’s disease
Kurata, T., Miyazaki, K., Morimoto, N., Kawai, H., Ohta, Y., Ikeda, Y., & Abe, K. (2013) · Neurological Research · doi:10.1179/1743132812y.0000000127 · Cited by 44
Pro-oxidant diet enhances β/γ secretase-mediated APP processing in APP/PS1 transgenic mice
Choudhry, F., Howlett, D. R., Richardson, J. C., Francis, P. T., & Williams, R. J. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.07.008 · Cited by 43
Sex Differences in Susceptibility to Oxidative Injury and Sleepiness From Intermittent Hypoxia
Sanfilippo-Cohn, B., Lai, S., Zhan, G., Fenik, P., Praticò, D., Mazza, E., & Veasey, S. C. (2006) · SLEEP · doi:10.1093/sleep/29.2.152 · Cited by 43
Self-citation
Gout and dementia in the elderly: a cohort study of Medicare claims
Singh, J. A., & Cleveland, J. D. (2018) · BMC Geriatrics · doi:10.1186/s12877-018-0975-0 · Cited by 42
Diseases Related to Types of Free Radicals
Maddu, N. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.82879 · Cited by 42
Dehydroepiandrosterone reduces expression and activity of BACE in NT2 neurons exposed to oxidative stress
Tamagno, E., Guglielmotto, M., Bardini, P., Santoro, G., Davit, A., Simone, D. D., Danni, O., & Tabaton, M. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00131-1 · Cited by 42
Absence of 12/15 Lipoxygenase Reduces Brain Oxidative Stress in Apolipoprotein E-Deficient Mice
Chinnici, C. M., Yao, Y., Ding, T., Funk, C. D., & Praticò, D. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61224-2 · Cited by 42
Self-citation
Bax Regulates Production of Superoxide in Both Apoptotic and Nonapoptotic Neurons: Role of Caspases
Kirkland, R. A., Saavedra, G. M., Cummings, B. S., & Franklin, J. L. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.2862-10.2010 · Cited by 42
Protection against inflammatory neurodegeneration and glial cell death by 7β-hydroxy epiandrosterone, a novel neurosteroid
Dudás, B., Hanin, I., Rose, M., & Wülfert, E. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.11.001 · Cited by 42
Oxidative Stress during the Progression ofβ-Amyloid Pathology in the Neocortex of the Tg2576 Mouse Model of Alzheimer’s Disease
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
How do different lipid peroxidation mechanisms contribute to ferroptosis?
Do, Q., & Xu, L. (2023) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2023.101683 · Cited by 45
Progress in the development of new drugs in Alzheimer's disease
Piau, A., Nourhashémi, F., Hein, C., Caillaud, C., & Vellas, B. (2011) · The Journal of nutrition, health and aging · doi:10.1007/s12603-011-0012-x · Cited by 32
Aging, gender and APOE isotype modulate metabolism of Alzheimer's Aβ peptides and F2‐isoprostanes in the absence of detectable amyloid deposits
Yao, J., Petanceska, S. S., Montine, T. J., Holtzman, D. M., Schmidt, S. D., Parker, C. A., Callahan, M. J., Lipinski, W. J., Bisgaier, C. L., Turner, B. A., et al. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02532.x · Cited by 41
Bridging the Gap Between Fluid Biomarkers for Alzheimer’s Disease, Model Systems, and Patients
Bjorkli, C., Sandvig, A., & Sandvig, I. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00272 · Cited by 41
RETRACTED: Nicotinamide Ameliorates Amyloid Beta-Induced Oxidative Stress-Mediated Neuroinflammation and Neurodegeneration in Adult Mouse Brain
Rehman, I., Ahmad, R., Khan, I., Lee, H. J., Park, J., Ullah, R., Choi, M. J., Kang, H. Y., & Kim, M. O. (2021) · Biomedicines · doi:10.3390/biomedicines9040408 · Cited by 47
Retracted
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
A role for 12/15 lipoxygenase in the amyloid β precursor protein metabolism
Succol, F., & Praticò, D. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04742.x · Cited by 41
Self-citation
Dietary Lipids in the Aetiology of Alzheimer???s Disease
Cooper, J. L. (2003) · Drugs & Aging · doi:10.2165/00002512-200320060-00001 · Cited by 40
Role of NRF2 in Pathogenesis of Alzheimer’s Disease
Chu, C., Uruno, A., Katsuoka, F., & Yamamoto, M. (2024) · Antioxidants · doi:10.3390/antiox13121529 · Cited by 43
Calpastatin levels affect calpain activation and calpain proteolytic activity in APP transgenic mouse model of Alzheimer's disease
Vaisid, T., Kosower, N. S., Katzav, A., Chapman, J., & Barnoy, S. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.04.004 · Cited by 40
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
FDG and Amyloid PET in Cognitively Normal Individuals at Risk for Late-Onset Alzheimer’s Disease
Murray, J., Tsui, W. H., Li, Y., McHugh, P. F., Williams, S., Cummings, M., Pirraglia, E., Sólnes, L. B., Osorio, R. S., Glodzik, L., et al. (2014) · Advances in Molecular Imaging · doi:10.4236/ami.2014.42003 · Cited by 39
The plasma membrane redox system is impaired by amyloid β-peptide and in the hippocampus and cerebral cortex of 3xTgAD mice
Hyun, D. H., Mughal, M. R., Yang, H., Lee, J. H., Ko, E. J., Hunt, N. D., de Cabo, R., & Mattson, M. P. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.07.020 · Cited by 39
Aging, lipid modifications and phospholipases—new concepts
Balazy, M., & Nigam, S. (2003) · Ageing Research Reviews · doi:10.1016/s1568-1637(02)00065-x · Cited by 39
CNS Redox Homeostasis and Dysfunction in Neurodegenerative Diseases
Goldsteins, G., Hakosalo, V., Jaronen, M., Keuters, M. H., Lehtonen, Š., & Koıstınaho, J. (2022) · Antioxidants · doi:10.3390/antiox11020405 · Cited by 42
Targeting Mitochondrial Dysfunction in Neurodegenerative Diseases: Expanding the Therapeutic Approaches by Plant-Derived Natural Products
Zhang, X., Wang, L., Li, B., Shi, J., Xu, J. F., & Yuan, M. (2023) · Pharmaceuticals · doi:10.3390/ph16020277 · Cited by 42
Genetic ablation of the p66Shc adaptor protein reverses cognitive deficits and improves mitochondrial function in an APP transgenic mouse model of Alzheimer’s disease
Derungs, R., Camici, G. G., Spescha, R. D., Welt, T., Tackenberg, C., Späni, C. B., Wirth, F., Grimm, A., Eckert, A., Nitsch, R. M., et al. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.112 · Cited by 39
SuHeXiang Wan Essential Oil Alleviates Amyloid Beta Induced Memory Impairment Through Inhibition of Tau Protein Phosphorylation in Mice
Jeon, S., Hur, J., Jeong, H. J., Koo, B., & Pak, S. C. (2011) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x11009305 · Cited by 38
New techniques to detect oxidative stress markers: Mass spectrometry‐based methods to detect isoprostanes as the gold standard for oxidative stress in vivo
Yin, H. (2008) · BioFactors · doi:10.1002/biof.5520340203 · Cited by 38
Age-related changes of neuron numbers in the frontal cortex of a transgenic mouse model of Alzheimer’s disease
Lemmens, M. A. M., Sierksma, A. S. R., Rutten, B. P. F., Dennissen, F., Steinbusch, H. W. M., Lucassen, P. J., & Schmitz, C. (2011) · Brain Structure and Function · doi:10.1007/s00429-011-0305-1 · Cited by 37
Alzheimer's Disease and NQO1: Is there a Link?
Chhetri, J., King, A. E., & Gueven, N. (2017) · Current Alzheimer Research · doi:10.2174/1567205014666170203095802 · Cited by 38
In vivo imaging of prodromal hippocampus CA1 subfield oxidative stress in models of Alzheimer disease and Angelman syndrome
Berkowitz, B. A., Lenning, J. C., Khetarpal, N., Tran, C., Wu, J. Y., Berri, A. M., Dernay, K., Haacke, E. M., Khorassani, F. S., Podolsky, R. H., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700229r · Cited by 37
Cell-derived soluble oligomers of human amyloid-β peptides disturb cellular homeostasis and induce apoptosis in primary hippocampal neurons
Yang, T.-T., Hsu, C.-T., & Kuo, Y. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0311-0 · Cited by 38
The role of oxidative stress in the pathogenesis of Alzheimer's disease
Filipčík, P., Cente, M., Ferencĭk, M., Hulín, I., & Novak, M. (2006) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.1007/bf03656857 · Cited by 37
Do 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
Melatonin prevents amyloid protofibrillar induced oxidative imbalance and biogenic amine catabolism
Masilamoni, J. G., Philip, J. E., Ashok, B. S., Kirubagaran, R., Walter, C. E. J., Dicky John Davis, G., Vignesh, S., Dhandayuthapani, S., & Rajadas, J. (2008) · Life Sciences · doi:10.1016/j.lfs.2008.05.011 · Cited by 36
RETRACTED: Transcriptional regulation of βsecretase‐1 by 12/15‐lipoxygenase results in enhanced amyloidogenesis and cognitive impairments
Chu, J., Zhuo, J., & Praticò, D. (2011) · Annals of Neurology · doi:10.1002/ana.22625 · Cited by 36
Self-citation
Retracted
Evidence of early involvement of apoptosis inducing factor-induced neuronal death in Alzheimer brain
Lee, J.-H., Cheon, Y. H., Woo, R., Song, D., Moon, C., & Baik, T. (2012) · Anatomy & Cell Biology · doi:10.5115/acb.2012.45.1.26 · Cited by 36
A multifunctional therapeutic approach to disease modification in multiple familial mouse models and a novel sporadic model of Alzheimer’s disease
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
The Efficacy and Pharmacological Mechanism of Zn7MT3 to Protect against Alzheimer’s Disease
Xu, W., Xu, Q., Cheng, H., & Tan, X. (2017) · Scientific Reports · doi:10.1038/s41598-017-12800-x · Cited by 36
Increased oxidative stress and astrogliosis responses in conditional double-knockout mice of Alzheimer-like presenilin-1 and presenilin-2
Zhu, M., Gu, F., Shi, J., Hu, J., Hu, Y., & Zhao, Z. Y. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.027 · Cited by 35
Involvement of 5-lipoxygenase activating protein in the amyloidotic phenotype of an Alzheimer’s disease mouse model
Chu, J., & Praticò, D. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-127 · Cited by 35
Self-citation
Review of Amyotrophic Lateral Sclerosis, Parkinson’s and Alzheimer’s diseases helps further define pathology of the novel paradigm for Alzheimer’s with heavy metals as primary disease cause
Cavaleri, F. (2015) · Medical Hypotheses · doi:10.1016/j.mehy.2015.10.009 · Cited by 36
Atorvastatin and pitavastatin protect cerebellar Purkinje cells in AD model mice and preserve the cytokines MCP-1 and TNF-α
Kozuki, M., Kurata, T., Miyazaki, K., Morimoto, N., Ohta, Y., Ikeda, Y., & Abe, K. (2011) · Brain Research · doi:10.1016/j.brainres.2011.03.024 · Cited by 34
Uridine Prodrug Improves Memory in Tg2576 and TAPP Mice and Reduces Pathological Factors associated with Alzheimer's Disease in Related Models
Saydoff, J. A., Olariu, A., Sheng, J. G., Hu, Z., Li, Q., Garcia, R. A. G., Pei, J., Sun, G. Y., & von Borstel, R. W. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130059 · Cited by 36
Metal Binding of Flavonoids and Their Distinct Inhibition Mechanisms Toward the Oxidation Activity of Cu2+–β-Amyloid: Not Just Serving as Suicide Antioxidants!
Tay, W. M., da Silva, G. F. Z., & Ming, L. (2013) · Inorganic Chemistry · doi:10.1021/ic301832p · Cited by 35
Dihydroxy‐Metabolites of Dihomo‐γ‐linolenic acid drive ferroptosis‐mediated neurodegeneration
Sarparast, M., Pourmand, E., Hinman, J., Vonarx, D., Reason, T., Zhang, F., Paithankar, S., Chen, B., Borhan, B., Watts, J. L., et al. (2023) · ACS Central Science · doi:10.1021/acscentsci.3c00052 · Cited by 33
Ginkgo biloba extract inhibits hippocampal neuronal injury caused by mitochondrial oxidative stress in a rat model of Alzheimer’s disease
Xia, C., Zhou, M., Dong, X., Zhao, Y., Jiang, M., Zhu, G., & Zhang, Z. (2024) · PLoS ONE · doi:10.1371/journal.pone.0307735 · Cited by 33
Elevated amyloid-β plaque deposition in dietary selenium-deficient Tg2576 transgenic mice
Haratake, M., Yoshida, S., Mandai, M., Fuchigami, T., & Nakayama, M. (2013) · Metallomics · doi:10.1039/c3mt00035d · Cited by 33
Genetic Variants and Oxidative Stress in Alzheimer’s Disease
Kowalska, M., Wize, K., Prendecki, M., Lianeri, M., Kozubski, W. P., & Dorszewska, J. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200224121447 · Cited by 34
The in vivo Down syndrome genomic library in mouse
Hérault, Y., Duchon, A., Velot, É., Maréchal, D., & Brault, V. (2012) · Progress in brain research · doi:10.1016/b978-0-444-54299-1.00009-1 · Cited by 36
Emerging evidence for the neuroprotective role of α-synuclein
Lee, H., Zhu, X., Takeda, A., Perry, G. L., & Smith, M. A. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.04.024 · Cited by 37
Thromboxane Receptor Activation Mediates Isoprostane-Induced Increases in Amyloid Pathology in Tg2576 Mice
Shineman, D. W., Zhang, B., Leight, S. N., Praticò, D., & Lee, V. M. ‐. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0684-08.2008 · Cited by 33
Self-citation
DP‐155, a Lecithin Derivative of Indomethacin, is a Novel Nonsteroidal Antiinflammatory Drug for Analgesia and Alzheimer's Disease Therapy
Dvir, E., Elman, A., Simmons, D. A., Shapiro, I., Duvdevani, R., Dahan, A., Hoffman, A., & Friedman, J. E. (2007) · CNS Drug Reviews · doi:10.1111/j.1527-3458.2007.00014.x · Cited by 33
Extracellular Superoxide Dismutase Overexpression Protects Against Aging-Induced Cognitive Impairment in Mice
Levin, E. D., Christopher, N. C., Lateef, S., Elamir, B. M., Patel, M., Liang, L., & Crapo, J. D. (2002) · Behavior Genetics · doi:10.1023/a:1015201823417 · Cited by 33
Up-regulation of Bcl-2 in APP transgenic mice is associated with neuroprotection
Karlnoski, R., Wilcock, D. M., Dickey, C. A., Ronan, V., Gordon, M. N., Zhang, W., Morgan, D., & Taglialatela, G. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.09.007 · Cited by 33
Mechanisms of Neural and Behavioral Dysfunction in Alzheimer’s Disease
Wesson, D. W., Nixon, R. A., Levy, E., & Wilson, D. A. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8177-1 · Cited by 34
The pathophysiology of triose phosphate isomerase dysfunction in Alzheimer's disease.
Tajes, M., Guivernau, B., Ramos‐Fernández, E., Bosch-Morató, M., Palomer, E., Guix, F. X., & Muñoz, F. J. (2013) · PubMed · doi:10.14670/hh-28.43 · Cited by 32
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
Oxidative stress, the immune response, synaptic plasticity, and cognition in transgenic models of Alzheimer disease
Bello-Medina, P. C., González-Franco, D. A., Vargas-Rodríguez, I., & Díaz-Cintra, S. Y. (2021) · Neurología (English Edition) · doi:10.1016/j.nrleng.2019.06.008 · Cited by 35
Serum copper in Alzheimer’s disease and vascular dementia
Agarwal, R., Kushwaha, S. S., Tripathi, C. B., Singh, N. K., & Chhillar, N. (2008) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-008-0081-8 · Cited by 32
Oxidative Stress and Alzheimer’s Disease
Singh, S. K., Castellani, R. J., & Perry, G. L. (2016) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-319-33486-8_10 · Cited by 33
Effects of rosmarinic acid on cognitive and biochemical alterations in ovariectomized rats treated with D-galactose
Kantar, D., Öztürk, N., Er, H., Aslan, M., Demır, N., Derin, N., Ağar, A., & Yargıçoğlu, P. (2015) · Folia Histochemica et Cytobiologica · doi:10.5603/fhc.a2015.0034 · Cited by 32
Analysis of calcium homeostasis in fresh lymphocytes from patients with sporadic Alzheimer's disease or mild cognitive impairment
Jaworska, A. M., Dzbek, J., Styczyńska, M., & Kuźnicki, J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.01.012 · Cited by 33
Transient OGG1, APE1, PARP1 and Polβ expression in an Alzheimer's disease mouse model
Lillenes, M. S., Støen, M., Gómez-Muñoz, M., Torp, R., Günther, C., Nilsson, L. N. G., & Tønjum, T. (2013) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2013.09.002 · Cited by 29
Normalization of hyperhomocysteinemia improves cognitive deficits and ameliorates brain amyloidosis of a transgenic mouse model of Alzheimer's disease
Zhuo, J., & Praticò, D. (2010) · The FASEB Journal · doi:10.1096/fj.10-161828 · Cited by 31
Self-citation
Decay in Retinoic Acid Signaling in Varied Models of Alzheimer’s Disease and In-Vitro Test of Novel Retinoic Acid Receptor Ligands (RAR-Ms) to Regulate Protective Genes
Khatib, T., Chisholm, D. R., Whiting, A., Platt, B., & McCaffery, P. J. A. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190931 · Cited by 31
Paraoxonase 1 decline and lipid peroxidation rise reflect a degree of brain atrophy and vascular impairment in dementia
Bednarz-Misa, I. S., Berdowska, I., Zboch, M., Misiak, B., Zieliński, B., Płaczkowska, S., Fleszar, M. G., Wiśniewski, J. Ł., Gamian, A., & Krzystek‐Korpacka, M. (2020) · Advances in Clinical and Experimental Medicine · doi:10.17219/acem/111377 · Cited by 30
Possible mechanisms of APP-mediated oxidative stress in Alzheimer’s disease1,2 1Guest Editors: Mark A. Smith and George Perry 2This article is part of a series of reviews on “Causes and Consequences of Oxidative Stress in Alzheimer’s Disease.” The full list of papers may be found on the homepage of the journal.
Multhaup, G., Scheuermann, S., Schlicksupp, A., Simons, A., Strauss, M., Kemmling, A., Oehler, C., Cappai, R., Pipkorn, R., & Bayer, T. A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00806-7 · Cited by 30
Blood-Based Protein Biomarkers for Diagnosis and Classification of Neurodegenerative Diseases
Noelker, C., Hampel, H. J., & Dodel, R. C. (2011) · Molecular Diagnosis & Therapy · doi:10.1007/bf03256398 · Cited by 29
Characterization of tau pathologies in gray and white matter of Guam parkinsonism-dementia complex
Winton, M. J., Joyce, S. C., Zhukareva, V. A., Practico, D., Perl, D. P., Galasko, D. R., Craig, U.-K., Trojanowski, J. Q., & Lee, V. M. ‐. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0053-0 · Cited by 31
Self-citation
Abnormal amyloid β 42 expression and increased oxidative stress in plasma of CKD patients with cognitive dysfunction: A small scale case control study comparison with Alzheimer's disease
Vinothkumar, G., Kedharnath, C., Krishnakumar, S., Sreedhar, S., Preethikrishnan, K., Dinesh, S., Sundaram, A., Balakrishnan, D., Shivashekar, G., Sureshkumar, et al. (2017) · BBA Clinical · doi:10.1016/j.bbacli.2017.06.001 · Cited by 29
Amyloid beta deposition related retinal pigment epithelium cell impairment and subretinal microglia activation in aged APPswePS1 transgenic mice
Dong, Z., Li, J., Gan, Y., Sun, X., Leng, Y., & Ge, J. (2018) · International Journal of Ophthalmology · doi:10.18240/ijo.2018.05.06 · Cited by 27
Machine Learning Profiling of Alzheimer's Disease Patients Based on Current Cerebrospinal Fluid Markers and Iron Content in Biofluids
Ficiarà, E., Boschi, S., Ansari, S. A., D’Agata, F., Abollino, O., Caroppo, P., Fede, G. D., Indaco, A., Rainero, I., & Guiot, C. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.607858 · Cited by 29
Sex and menopause impact 31P-Magnetic Resonance Spectroscopy brain mitochondrial function in association with 11C-PiB PET amyloid-beta load
Jett, S., Dyke, J. P., Andy, C., Schelbaum, E., Jang, G., Boneu, C., Pahlajani, S. S., Diaz, I., Brinton, R. D., & Mosconi, L. (2022) · Scientific Reports · doi:10.1038/s41598-022-26573-5 · Cited by 29
Systematic review of 31P-magnetic resonance spectroscopy studies of brain high energy phosphates and membrane phospholipids in aging and Alzheimer's disease
Jett, S., Boneu, C., Zarate, C., Carlton, C., Kodancha, V., Nerattini, M., Battista, M., Pahlajani, S. S., Williams, S., Dyke, J. P., et al. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1183228 · Cited by 30
Advances in Blood Biomarkers for Alzheimer’s Disease: Ultra-Sensitive Detection Technologies and Impact on Clinical Diagnosis
Zhang, Y., Bi, K., Zhou, L., Wang, J., Huang, L., Sun, Y., Peng, G., & Wu, W. (2024) · Degenerative Neurological and Neuromuscular Disease · doi:10.2147/dnnd.s471174 · Cited by 30
Effects of Reactive Oxygen and Nitrogen Species on TrkA Expression and Signalling: Implications for proNGF in Aging and Alzheimer’s Disease
Kropf, E., & Fahnestock, M. L. (2021) · Cells · doi:10.3390/cells10081983 · Cited by 28
Oxidative Stress in Brain in Amnestic Mild Cognitive Impairment
Butterfield, D. A. (2023) · Antioxidants · doi:10.3390/antiox12020462 · Cited by 29
Brain-Penetrant Tetrahydronaphthalene Thromboxane A2-Prostanoid (TP) Receptor Antagonists as Prototype Therapeutics for Alzheimer’s Disease
Soper, J. H., Sugiyama, S., Herbst, K. J., James, M. J., Wang, X., Trojanowski, J. Q., Smith, A. B., Lee, V. M. ‐., Ballatore, C., & Brunden, K. R. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn3000795 · Cited by 28
Self-citation
Nutritional management of brain aging in dogs
Roudebush, P., Zicker, S. C., Cotman, C. W., Milgram, N. W., Muggenburg, B. A., & Head, E. (2005) · Journal of the American Veterinary Medical Association · doi:10.2460/javma.2005.227.722 · Cited by 28
Comparative effectiveness of allopurinol versus febuxostat for preventing incident dementia in older adults: a propensity-matched analysis
Singh, J. A., & Cleveland, J. D. (2018) · Arthritis Research & Therapy · doi:10.1186/s13075-018-1663-3 · Cited by 28
Evaluation of the neuroprotective effect of donepezil in type 2 diabetic rats
Gomaa, A. A., Makboul, R. M., El‐Mokhtar, M. A., Abdel‐Rahman, E. A., Ahmed, E. A., & Nicola, M. A. (2020) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12585 · Cited by 26
Alzheimer's disease biomarkers: correspondence between human studies and animal models
Sabbagh, J. J., Kinney, J. W., & Cummings, J. L. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2013.04.010 · Cited by 27
Copper Perturbation in 2 Monozygotic Twins Discordant for Degree of Cognitive Impairment
Squitti, R., Cassetta, E., Forno, G. D., Lupoi, D., Lippolis, G., Pauri, F., Vernieri, F., Cappa, A., & Rossini, P. M. (2004) · Archives of Neurology · doi:10.1001/archneur.61.5.738 · Cited by 27
Vulnerability of neurons with mitochondrial dysfunction to oxidative stress is associated with down-regulation of thioredoxin
Gao, J., Zhu, Z., Ding, H., Qian, Z., Zhu, L., & Ke, Y. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2006.09.007 · Cited by 27
Mitochondria as a target for neuroprotection: implications for Alzheimer´s disease
Cardoso, S., Seiça, R. M. F., & Moreira, P. I. (2016) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2016.1205488 · Cited by 27
Amyloid plaque-associated oxidative degradation of uniformly radiolabeled arachidonic acid
Furman, R., Murray, I. V. J., Schall, H. E., Liu, Q., Ghiwot, Y., & Axelsen, P. H. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00316 · Cited by 26
Risk of dementia in gout and hyperuricaemia: a meta-analysis of cohort studies
Pan, S.-Y., Cheng, R., Xia, Z., Zhang, Q., & Liu, Y. (2021) · BMJ Open · doi:10.1136/bmjopen-2020-041680 · Cited by 24
Recent insights into the role of glia and oxidative stress in Alzheimer's disease gained from Drosophila
Goodman, L. D., & Bellen, H. J. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.07.012 · Cited by 29
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
Current Therapies and New Strategies for the Management of Alzheimer’s Disease
Aderinwale, O. G., Ernst, H. W., & Mousa, S. A. (2010) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/1533317510372372 · Cited by 27

Authors: Praticò, D., Uryu, K., Leight, S., Trojanoswki, J. Q., & Lee, V. M.-Y.
Affiliations: University of Pennsylvania (US)
ORCID: Praticò, Domenico
Uryu, Kunihiro
Lee, Virginia M.-Y.
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2001-06-15
Volume: 21
Issue: 12
Pages: 4183-4187
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.21-12-04183.2001
PMC: PMC6762743
OpenAlex: W1954454186
Cited by: 777
References: 24
Citations by year: 2026: 4 · 2025: 15 · 2024: 17 · 2023: 29 · 2022: 19 · 2021: 32 · 2020: 23 · 2019: 27 · 2018: 16 · 2017: 24 · 2016: 24 · 2015: 28 · 2014: 32 · 2013: 37 · 2012: 48
FWCI: 22.76
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 183 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: American Heart Association
National Institutes of Health (AG-11542)
National Institute on Aging (P01AG011542, AG 11542)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: lipid peroxidation, isoprostanes, amyloid-beta, amyloid plaques, Alzheimer's disease, Tg2576 mice, oxidative stress, Aβ40, amyloid-beta 42, brain oxidative damage, pathogenesis
MeSH terms: Aging, Alzheimer Disease, Amyloidosis, Animals, Brain, Cerebellum, Cerebral Cortex, Disease Models, Animal, Enzyme-Linked Immunosorbent Assay, Female, Hippocampus, Male, Mice, Transgenic, Peptide Fragments, Lipid Peroxidation, Dinoprost, Amyloid beta-Peptides, Mice, 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

Increased Lipid Peroxidation Precedes Amyloid Plaque Formation in an Animal Model of Alzheimer Amyloidosis

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks