Cited by 254Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchMitochondrial Function and Pathology

The DOI matches its Crossref record; 109 of the 111 references it cites were found in a registry or an index.

Reduction in mitochondrial superoxide dismutase modulates Alzheimer’s disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice

Open access

Esposito, Luke, Raber, Jacob, Kekonius, Lisa, Yan, Fengrong, Yu, Giu-Qiu, Bien-Ly, Nga, Puoliväli, Jukka, Scearce-Levie, Kimberly, Masliah, Eliezer, Mucke, Lennart·2006·The Journal of Neuroscience

DOI 10.1523/jneurosci.0482-06.2006PMC PMC6674260

Open this paper in CoChat — free account

Abstract

Alzheimer's disease (AD) is associated with accumulations of amyloid-beta (Abeta) peptides, oxidative damage, mitochondrial dysfunction, neurodegeneration, and dementia. The mitochondrial antioxidant manganese superoxide dismutase-2 (Sod2) might protect against these alterations. To test this hypothesis, we inactivated one Sod2 allele (Sod2(+/-)) in human amyloid precursor protein (hAPP) transgenic mice, reducing Sod2 activity to approximately 50% of that in Sod2 wild-type (Sod2(+/+)) mice. A reduction in Sod2 activity did not obviously impair mice without hAPP/Abeta expression. In hAPP mice, however, it accelerated the onset of behavioral alterations and of deficits in prepulse inhibition of acoustic startle, a measure of sensorimotor gating. In these mice, it also worsened hAPP/Abeta-dependent depletion of microtubule-associated protein 2, a marker of neuronal dendrites. Sod2 reduction decreased amyloid plaques in the brain parenchyma but promoted the development of cerebrovascular amyloidosis, gliosis, and plaque-independent neuritic dystrophy. Sod2 reduction also increased the DNA binding activity of the transcription factor nuclear factor kappaB. These results suggest that Sod2 protects the aging brain against hAPP/Abeta-induced impairments. Whereas reductions in Sod2 would be expected to trigger or exacerbate neuronal and vascular pathology in AD, increasing Sod2 activity might be of therapeutic benefit.

Integrity signals

Registry

Crossref · 10.1523/jneurosci.0482-06.2006

Cites

109 of 109 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178
Validation of open:closed arm entries in an elevated plus-maze as a measure of anxiety in the rat
Pellow, S., Chopin, P., File, S. E., & Briley, M. (1985) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(85)90031-7 · Cited by 5,822
Free radicals in biology and medicine
Halliwell, B. B., & Gutteridge, J. M. C. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90140-0 · Cited by 2,938
The use of a plus-maze to measure anxiety in the mouse
Lister, R. G. (1987) · Psychopharmacology · doi:10.1007/bf00177912 · Cited by 2,617
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516
Self-citation
High-Level Neuronal Expression of Aβ1–42in Wild-Type Human Amyloid Protein Precursor Transgenic Mice: Synaptotoxicity without Plaque Formation
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective
Tanzi, R. E., & Bertram, L. (2005) · Cell · doi:10.1016/j.cell.2005.02.008 · Cited by 1,849
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789
Frequency of Stages of Alzheimer-Related Lesions in Different Age Categories
Braak, H., & Braak, E. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00056-0 · Cited by 1,656
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

Flagged first, then by citations

Show all 111 references

2 of the 111 references couldn’t be matched to a known paper.

Research works printed but not linked: 10

10.1172/JCI200523269 · DOI · Paper page
(1995), Mol Pharmacol, 48, 825
(2003), Behav Pharmacol, 14, 419
(1987), Psychopharmacology, 92, 180
(1993), Am J Pathol, 142, 871
(2000), CMAJ, 162, 65
(1989), Prog Clin Biol Res, 317, 781
(2000), Nature, 404, 352
(1994), Mol Cell Biol, 14, 7377
(1999), Ann NY Acad Sci, 903, 317

Sorted by citations

Mitochondria in neuroplasticity and neurological disorders
Mattson, M. P., Gleichmann, M., & Cheng, A. (2008) · Neuron · doi:10.1016/j.neuron.2008.10.010 · Cited by 1,081
Mitochondrial generation of superoxide and hydrogen peroxide as the source of mitochondrial redox signaling
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063
Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease
Du, H., Guo, L., Fang, F., Chen, D., Sosunov, A. A., McKhann, G. M., Yan, Y., Wang, C., Zhang, H., Molkentin, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm.1868 · Cited by 950
Mitophagy and Alzheimer’s Disease: Cellular and Molecular Mechanisms
Kerr, J. S., Adriaanse, B. A., Greig, N. H., Mattson, M. P., Cader, M. Z., Bohr, V. A., & Fang, E. F. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.01.002 · Cited by 870
Oxidative stress mitigation by antioxidants - An overview on their chemistry and influences on health status
Pisoschi, A. M., Pop, A., Iordache, F., Stanca, L., Predoi, G., & Șerban, A. I. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112891 · Cited by 883
Metals in Alzheimer's and Parkinson's Diseases
Barnham, K. J., & Bush, A. I. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.02.019 · Cited by 695
Amyloid-Beta and Phosphorylated Tau Accumulations Cause Abnormalities at Synapses of Alzheimer’s disease Neurons
Rajmohan, R., & Reddy, P. H. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160612 · Cited by 730
Reactive Oxygen Species in the Regulation of Synaptic Plasticity and Memory
Massaad, C. A., & Klann, E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3208 · Cited by 635
Oxidative stress: A major pathogenesis and potential therapeutic target of antioxidative agents in Parkinson’s disease and Alzheimer’s disease
Jiang, T., Sun, Q., & Chen, S. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.07.005 · Cited by 605
Microglial cell dysregulation in brain aging and neurodegeneration
von Bernhardi, R., Eugenín-von Bernhardi, L., & Eugenín, J. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00124 · Cited by 556
Physiologic brain activity causes DNA double-strand breaks in neurons, with exacerbation by amyloid-β
Suberbielle, E., Sanchez, P. E., Kravitz, A. V., Wang, X., Ho, K., Eilertson, K., Devidze, N., Kreitzer, A. C., & Mucke, L. (2013) · Nature Neuroscience · doi:10.1038/nn.3356 · Cited by 487
Oxidative Stress and Neurodegenerative Disorders
Li, J., Wuliji, O., Li, W., Jiang, Z.-G., & Ghanbari, H. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141224438 · Cited by 520
Neuroprotective Effect of Antioxidants in the Brain
Lee, K. H., Cha, M., & Lee, B. H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197152 · Cited by 543
Mechanism of Oxidative Stress and Synapse Dysfunction in the Pathogenesis of Alzheimer’s Disease: Understanding the Therapeutics Strategies
Kamat, P. K., Kalani, A., Rai, S., Swarnkar, S., Tota, S., Nath, C., & Tyagi, N. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-9053-6 · Cited by 511
Alzheimer's Disease (AD)-Like Pathology in Aged Monkeys after Infantile Exposure to Environmental Metal Lead (Pb): Evidence for a Developmental Origin and Environmental Link for AD
Wu, J., Basha, R. M., Brock, B., Cox, D. P., Cardozo‐Pelaez, F., McPherson, C. A., Harry, J., Rice, D. C., Maloney, B., Chen, D., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.4405-07.2008 · Cited by 473
Update on the oxidative stress theory of aging: Does oxidative stress play a role in aging or healthy aging?
Salmon, A. B., Richardson, A. G., & Pérez, V. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.015 · Cited by 451
Alzheimer disease models and human neuropathology: similarities and differences
Duyckaerts, C., Potier, M.-C., & Delatour, B. (2008) · Acta Neuropathologica · doi:10.1007/s00401-007-0312-8 · Cited by 375
The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease
McManus, M. J., Murphy, M. P., & Franklin, J. L. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.0552-11.2011 · Cited by 432
Accelerating Amyloid-β Fibrillization Reduces Oligomer Levels and Functional Deficits in Alzheimer Disease Mouse Models
Cheng, I. H.-J., Scearce-Levie, K. A., Legleiter, J. A., Palop, J. J., Gerstein, H., Bien‐Ly, N., Puolivaöli, J., Lesné, S., Ashe, K. H., Muchowski, P. J., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701078200 · Cited by 418
Neuroprotective strategies involving ROS in Alzheimer disease
Dumont, M., & Beal, M. F. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.026 · Cited by 402
SOD2 in mitochondrial dysfunction and neurodegeneration
Flynn, J. M., & Melov, S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.027 · Cited by 390
Oxidative Stress: Signaling Pathways, Biological Functions, and Disease
Liu, S., Liu, J., Wang, Y., Deng, F., & Deng, Z. (2025) · MedComm · doi:10.1002/mco2.70268 · Cited by 485
Antioxidant Therapies for Alzheimer's Disease
Feng, Y., & Wang, X. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/472932 · Cited by 393
Mitochondrial Oxidative Stress Causes Hyperphosphorylation of Tau
Melov, S., Adlard, P. A., Morten, K., Johnson, F., Golden, T. R., Hinerfeld, D., Schilling, B., Mavros, C., Masters, C. L., Volitakis, I., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000536 · Cited by 363
Manganese in Health and Disease
Ávila, D. S., Puntel, R. L., & Aschner, M. (2013) · Metal ions in life sciences · doi:10.1007/978-94-007-7500-8_7 · Cited by 378
Epigenetics, oxidative stress, and Alzheimer disease
Zawia, N. H., Lahiri, D. K., & Cardozo-Pelaez, F. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.006 · Cited by 337
Nox2-derived radicals contribute to neurovascular and behavioral dysfunction in mice overexpressing the amyloid precursor protein
Park, L., Zhou, P., Pitstick, R., Capone, C., Anrather, J., Norris, E. H., Younkin, L., Younkin, S., Carlson, G., McEwen, B. S., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711568105 · Cited by 332
PINK1 signalling rescues amyloid pathology and mitochondrial dysfunction in Alzheimer’s disease
Du, F., Yu, Q., Yan, S., Hu, G., Lue, L., Walker, D., Wu, L., Yan, S. F., Tieu, K., & Yan, S. S. (2017) · Brain · doi:10.1093/brain/awx258 · Cited by 308
Mitochondrial dysfunction in neurodegenerative diseases and the potential countermeasure
Wang, Y., Xu, E., Musich, P. R., & Lin, F. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13116 · Cited by 298
Alzheimer disease, the two-hit hypothesis: An update
Zhu, X., Lee, H., Perry, G. L., & Smith, M. A. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.10.014 · Cited by 299
Interplay of gut microbiota and oxidative stress: Perspective on neurodegeneration and neuroprotection
Shandilya, S., Kumar, S., Jha, N. K., Kesari, K. K., & Ruokolainen, J. (2021) · Journal of Advanced Research · doi:10.1016/j.jare.2021.09.005 · Cited by 310
Antioxidant Therapy in Oxidative Stress-Induced Neurodegenerative Diseases: Role of Nanoparticle-Based Drug Delivery Systems in Clinical Translation
Ashok, A., Andrabi, S. S., Mansoor, S., Kuang, Y., Kwon, B. K., & Labhasetwar, V. D. (2022) · Antioxidants · doi:10.3390/antiox11020408 · Cited by 270
SOD1 (Copper/Zinc Superoxide Dismutase) Deficiency Drives Amyloid β Protein Oligomerization and Memory Loss in Mouse Model of Alzheimer Disease
Murakami, K., Murata, N., Noda, Y., Tahara, S., Kaneko, T., Kinoshita, N., Hatsuta, H., Murayama, S., Barnham, K. J., Irie, K., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.279208 · Cited by 241
Evolving and Expanding the Roles of Mitophagy as a Homeostatic and Pathogenic Process
Gustafsson, Å. B., & Dorn, G. W. (2018) · Physiological Reviews · doi:10.1152/physrev.00005.2018 · Cited by 235
Overexpression of SOD-2 reduces hippocampal superoxide and prevents memory deficits in a mouse model of Alzheimer's disease
Massaad, C. A., Washington, T. M., Pautler, R. G., & Klann, E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902714106 · Cited by 223
Cerium oxide nanoparticles protect against Aβ-induced mitochondrial fragmentation and neuronal cell death
Dowding, J. M., Song, W., Bossy, K., Karakoti, A., Kumar, A., Kim, A., Bossy, B., Seal, S., Ellisman, M. H., Perkins, G., et al. (2014) · Cell Death & Differentiation · doi:10.1038/cdd.2014.72 · Cited by 221
Reduction of oxidative stress, amyloid deposition, and memory deficit by manganese superoxide dismutase overexpression in a transgenic mouse model of Alzheimer's disease
Dumont, M., Wille, E., Stack, C., Calingasan, N. Y., Beal, M. F., & Lin, M. T. (2009) · The FASEB Journal · doi:10.1096/fj.09-132928 · Cited by 221
Neuroprotection Against Oxidative Stress: Phytochemicals Targeting TrkB Signaling and the Nrf2-ARE Antioxidant System
Hannan, M. A., Dash, R., Sohag, A. A. M., Haque, M. N., & Moon, I. S. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00116 · Cited by 215
Role of reactive oxygen species in the progression of Alzheimer’s disease
Bhatt, S., Puli, L., & Patil, C. R. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.12.004 · Cited by 217
Pharmacological targeting of MCL-1 promotes mitophagy and improves disease pathologies in an Alzheimer’s disease mouse model
Cen, X., Chen, Y., Xu, X., Wu, R., He, F., Zhao, Q. D., Sun, Q., Yi, C., Wu, J., Najafov, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19547-6 · Cited by 203
Deletion of the 7 Nicotinic Acetylcholine Receptor Gene Improves Cognitive Deficits and Synaptic Pathology in a Mouse Model of Alzheimer's Disease
Dziewczapolski, G., Głogowski, M., Masliah, E., & Heinemann, S. F. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.6159-08.2009 · Cited by 199
Role of mitochondrial dysfunction and altered autophagy in cardiovascular aging and disease: from mechanisms to therapeutics
Marzetti, E., Csiszár, A., Dutta, D., Balagopal, G., Calvani, R., & Leeuwenburgh, C. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00936.2012 · Cited by 198
Alzheimer's Disease: Redox Dysregulation As a Common Denominator for Diverse Pathogenic Mechanisms
Rommy von Bernhardi, M., & Eugenín, J. L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4082 · Cited by 193
Current Concepts of Neurodegenerative Mechanisms in Alzheimer’s Disease
Magalingam, K. B., Radhakrishnan, A., Ping, N. S., & Haleagrahara, N. (2018) · BioMed Research International · doi:10.1155/2018/3740461 · Cited by 178
Antioxidant gene therapy against neuronal cell death
Navarro-Yepes, J., Zavala-Flores, L. M., Anandhan, A., Wang, F., Skotak, M., Chandra, N., Li, M., Pappa, A., Martínez‐Fong, D., Razo, L. M. D., et al. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.12.007 · Cited by 182
Mitochondrial Glutathione: Recent Insights and Role in Disease
Marı́, M., de Gregorio, E., de Dios, C., Agujetas, V. R., Cucarull, B., Tutusaus, A., Morales, A., & Colell, A. (2020) · Antioxidants · doi:10.3390/antiox9100909 · Cited by 183
A role for human brain pericytes in neuroinflammation
Jansson, D., Rustenhoven, J., Feng, S. X., Hurley, D., Oldfield, R. L., Bergin, P., Mee, E. W., Faull, R. L. M., & Dragunow, M. (2014) · Journal of Neuroinflammation · doi:10.1186/1742-2094-11-104 · Cited by 174
Wine Polyphenols: Potential Agents in Neuroprotection
Basli, A., Soulet, S., Chaher, N., Mérillon, J., Chibane, M., Monti, J., & Richard, T. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/805762 · Cited by 162
Increased Oxidative Stress Exacerbates α-Synuclein Aggregation In Vivo
Scudamore, O., & Ciossek, T. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nly024 · Cited by 163
Mitochondrial biology, targets, and drug delivery
Milane, L. S., Trivedi, M. S., Singh, A., Talekar, M., & Amiji, M. M. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.03.036 · Cited by 163
Oxidative stress, cellular senescence and ageing
Pole, A., Dimri, M., & Dimri, G. P. (2016) · AIMS molecular science · doi:10.3934/molsci.2016.3.300 · Cited by 168
Mitochondrial abnormalities in spinal and bulbar muscular atrophy
Ranganathan, S., Harmison, G. G., Meyertholen, K., Pennuto, M., Burnett, B. G., & Fischbeck, K. H. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn310 · Cited by 154
Mitochondrial superoxide dismutase SOD2, but not cytosolic SOD1, plays a critical role in protection against glutamate-induced oxidative stress and cell death in HT22 neuronal cells
Fukui, M., & Zhu, B. T. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.024 · Cited by 158
A reciprocal relationship between reactive oxygen species and mitochondrial dynamics in neurodegeneration
Hung, C. H.-L., Cheng, S. S., Cheung, Y.-T., Wuwongse, S., Zhang, N. Q., Ho, J. Y. S., Lee, S. M., & Chang, R. C. (2017) · Redox Biology · doi:10.1016/j.redox.2017.08.010 · Cited by 147
Liberation of Copper from Amyloid Plaques: Making a Risk Factor Useful for Alzheimer’s Disease Treatment
Geng, J., Li, M. C., Wu, L. J., Ren, J., & Qu, X. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3003813 · Cited by 153
Blocking Early GABA Depolarization with Bumetanide Results in Permanent Alterations in Cortical Circuits and Sensorimotor Gating Deficits
Wang, D. D., & Kriegstein, A. R. (2011) · Cerebral Cortex · doi:10.1093/cercor/bhq124 · Cited by 148
A metabolomic study of the CRND8 transgenic mouse model of Alzheimer's disease
Salek, R. M., Xia, J., Innes, A. E., Sweatman, B. C., Adalbert, R., Randle, S. J., McGowan, E. M., Emson, P. C., & Griffin, J. L. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.04.001 · Cited by 148
Mitochondrial import and degradation of amyloid-β peptide
Pinho, C. M., Teixeira, P. F., & Glaser, E. G. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.02.007 · Cited by 149
Amyloid β-Induced Impairments in Hippocampal Synaptic Plasticity Are Rescued by Decreasing Mitochondrial Superoxide
Ma, T., Hoeffer, C. A., Wong, H., Massaad, C. A., Zhou, P., Iadecola, C., Murphy, M. P., Pautler, R. G., & Klann, E. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6566-10.2011 · Cited by 147
Insights into Manganese Superoxide Dismutase and Human Diseases
Liu, M., Sun, X., Chen, B., Dai, R., Xi, Z., & Xu, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415893 · Cited by 157
Metabolism-Centric Overview of the Pathogenesis of Alzheimer's Disease
Kang, S., Lee, Y., & Lee, J. E. (2017) · Yonsei Medical Journal · doi:10.3349/ymj.2017.58.3.479 · Cited by 148
Vascular amyloidosis impairs the gliovascular unit in a mouse model of Alzheimer’s disease
Kimbrough, I. F., Robel, S., Roberson, E. D., & Sontheimer, H. W. (2015) · Brain · doi:10.1093/brain/awv327 · Cited by 140
A neuronal model of Alzheimer's disease: An insight into the mechanisms of oxidative stress–mediated mitochondrial injury
Sompol, P. M., Ittarat, W., Tangpong, J., Chen, Y., Doubinskaia, I. E., Batinic-Haberle, I., Abdul, H. M., Butterfield, D. A., & Clair, D. K. S. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.01.044 · Cited by 137
Brain Renin–Angiotensin System at the Intersect of Physical and Cognitive Frailty
Cosarderelioglu, C., Nidadavolu, L. S., George, C. J., Oh, E. S., Bennett, D. A., Walston, J. D., & Abadir, P. M. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.586314 · Cited by 134
Amyloid β: linking synaptic plasticity failure to memory disruption in Alzheimer’s disease
Ma, T., & Klann, E. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07506.x · Cited by 140
Contribution of reactive oxygen species to cerebral amyloid angiopathy, vasomotor dysfunction, and microhemorrhage in aged Tg2576 mice
Han, B. H., Zhou, M.-L., Johnson, A. W., Singh, I., Liao, F., Vellimana, A. K., Nelson, J. W., Milner, E., Cirrito, J. R., Basak, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414930112 · Cited by 131
Hippocampal long-term potentiation, memory, and longevity in mice that overexpress mitochondrial superoxide dismutase
Hu, D., Cao, P., Thiels, E., Chu, C. T., Wu, G., Oury, T. D., & Klann, E. (2006) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2006.10.003 · Cited by 127
Riding the tiger – physiological and pathological effects of superoxide and hydrogen peroxide generated in the mitochondrial matrix
Brand, M. D. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828258 · Cited by 123
The mitochondria-targeted antioxidant MitoQ inhibits memory loss, neuropathology, and extends lifespan in aged 3xTg-AD mice
Young, M. L., & Franklin, J. L. (2019) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2019.103409 · Cited by 120
Changes in the mitochondrial antioxidant systems in neurodegenerative diseases and acute brain disorders
Ruszkiewicz, J. A., & Albrecht, J. (2015) · Neurochemistry International · doi:10.1016/j.neuint.2014.12.012 · Cited by 125
Evidence supporting oxidative stress in a moderately affected area of the brain in Alzheimer’s disease
Youssef, P., Chami, B., Lim, J., Middleton, T., Sutherland, G. T., & Witting, P. K. (2018) · Scientific Reports · doi:10.1038/s41598-018-29770-3 · Cited by 114
Abnormal social behaviors in mice lacking Fgf17
Scearce-Levie, K. A., Roberson, E. D., Gerstein, H. C., Cholfin, J. A., Mandiyan, V. S., Shah, N. M., Rubenstein, J. L. R., & Mucke, L. (2007) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2007.00357.x · Cited by 114
Triterpenoid CDDO‐methylamide improves memory and decreases amyloid plaques in a transgenic mouse model of Alzheimer’s disease
Dumont, M., Wille, E. J., Calingasan, N. Y., Tampellini, D., Williams, C. R., Gouras, G. K., Liby, K. T., Sporn, M. B., Beal, M. F., & Lin, M. T. S. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05970.x · Cited by 112
Cofilin-mediated neurodegeneration in alzheimer’s disease and other amyloidopathies
Maloney, M. T., & Bamburg, J. R. (2007) · Molecular Neurobiology · doi:10.1007/bf02700622 · Cited by 115
Therapeutic potential of astaxanthin and superoxide dismutase in Alzheimer's disease
Balendra, V., & Singh, S. K. (2021) · Open Biology · doi:10.1098/rsob.210013 · Cited by 111
IRS2 increases mitochondrial dysfunction and oxidative stress in a mouse model of Huntington disease
Sadagurski, M., Cheng, Z., Rozzo, A., Palazzolo, I., Kelley, G. R., Dong, X., Krainc, D., & White, M. F. (2011) · Journal of Clinical Investigation · doi:10.1172/jci46305 · Cited by 107
Reduced mitochondrial SOD displays mortality characteristics reminiscent of natural aging
Paul, A., Belton, A., Nag, S., Martin, I., Grotewiel, M. S., & Duttaroy, A. (2007) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.10.013 · Cited by 105
Neuronal and Vascular Oxidative Stress in Alzheimers Disease
Massaad, C. A. (2011) · Current Neuropharmacology · doi:10.2174/157015911798376244 · Cited by 102
Cerebral Small Vessel Disease: Targeting Oxidative Stress as a Novel Therapeutic Strategy?
Silva, T. M. D., & Miller, A. A. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00061 · Cited by 105
Amyloid-beta aggregation implicates multiple pathways in Alzheimer’s disease: Understanding the mechanisms
Iliyasu, M. O., Musa, S. A., Oladele, S. B., & Iliya, A. I. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1081938 · Cited by 106
Oxidative Stress and Altered Mitochondrial Function in Neurodegenerative Diseases: Lessons From Mouse Models
Fernández-Checa, J. C., Fernandez, A., Morales, A., Marí, M., García‐Ruiz, C., & Colell, A. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791556113 · Cited by 99
Altered carnitine homeostasis is associated with decreased mitochondrial function and altered nitric oxide signaling in lambs with pulmonary hypertension
Sharma, S., Sud, N., Wiseman, D. A., Carter, A. L., Kumar, S., Hou, Y., Rau, T., Wilham, J. M., Harmon, C., Oishi, P. E., et al. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00247.2007 · Cited by 89
Protective Effects of Positive Lysosomal Modulation in Alzheimer's Disease Transgenic Mouse Models
Butler, D., Hwang, J., Estick, C., Nishiyama, A., Kumar, S. S., Baveghems, C. L., Young-Oxendine, H. B., Wisniewski, M. L., Charalambides, A., & Bahr, B. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020501 · Cited by 92
Benfotiamine treatment activates the Nrf2/ARE pathway and is neuroprotective in a transgenic mouse model of tauopathy
Tapias, V., Jainuddin, S., Ahuja, M., Stack, C., Elipenahli, C., Vignisse, J., Gerges, M., Starkova, N. N., Xu, H., Starkov, A. A., et al. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy201 · Cited by 91
Centella Asiatica Improves Memory and Promotes Antioxidative Signaling in 5XFAD Mice
Matthews, D. G., Caruso, M., Murchison, C. F., Zhu, J. Y., Wright, K. M., Harris, C. J., Gray, N. E., Quinn, J. F., & Soumyanath, A. (2019) · Antioxidants · doi:10.3390/antiox8120630 · Cited by 86
“Elevated SOD expression is indicative of the high levels of oxidative stress associated with Aβ plaques in Alzheimer’s disease brains [21,48,80,104].”
Background
Superoxide dismutases: a physiopharmacological update
Valdivia, A., Perez‐Alvarez, S., Aroca‐Aguilar, J., Ikuta, I., & Jordán, J. (2009) · Journal of Physiology and Biochemistry · doi:10.1007/bf03179070 · Cited by 85
Implications of PI3K/AKT/PTEN Signaling on Superoxide Dismutases Expression and in the Pathogenesis of Alzheimer’s Disease
Matsuda, S., Nakagawa, Y., Tsuji, A., Kitagishi, Y., Nakanishi, A., & Murai, T. (2018) · Diseases · doi:10.3390/diseases6020028 · Cited by 86
Mitochondria and Antioxidant Targeted Therapeutic Strategies for Alzheimer's Disease
Dumont, M., Lin, M. T. S., & Beal, M. F. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100507 · Cited by 85
Oxidative stress in cerebral small vessel disease. Role of reactive species
Grochowski, C., Litak, J., Kamieniak, P., & Maciejewski, R. (2017) · Free Radical Research · doi:10.1080/10715762.2017.1402304 · Cited by 90
Reduction of Cerebral Oxidative Stress Following Environmental Enrichment in Mice with Alzheimer‐Like Pathology
Herring, A., Blome, M., Ambrée, O., Sachser, N., Paulus, W., & Keyvani, K. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00257.x · Cited by 87
Alzheimer's Disease and Amyloid: Culprit or Coincidence?
Skaper, S. D. (2012) · International review of neurobiology · doi:10.1016/b978-0-12-386986-9.00011-9 · Cited by 82
IRS2 integrates insulin/ IGF1 signalling with metabolism, neurodegeneration and longevity
White, M. F. (2014) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12347 · Cited by 82
Selective autophagy as a therapeutic target for neurological diseases
Xu, W., Ocak, U., Gao, L., Tu, S., Lenahan, C., Zhang, J., & Shao, A. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03667-9 · Cited by 84
Citrus flavanones naringenin and hesperetin improve antioxidant status and membrane lipid compositions in the liver of old-aged Wistar rats
Miler, M., Živanović, J., Ajdžanović, V. Z., Oreščanin-Dušić, Z., Milenković, D., Konić‐Ristić, A., Blagojević, D. P., Milošević, V., & Šošić‐Jurjević, B. (2016) · Experimental Gerontology · doi:10.1016/j.exger.2016.08.014 · Cited by 79
Study on the neuroprotective effects of Genistein on Alzheimer’s disease
Duan, X., Li, Y., Xu, F., & Ding, H. (2021) · Brain and Behavior · doi:10.1002/brb3.2100 · Cited by 78
Modification of γ‐secretase by nitrosative stress links neuronal ageing to sporadic Alzheimer's disease
Guix, F. X., Wahle, T., Vennekens, K. M., Snellinx, A., Chávez‐Gutiérrez, L., ILL‐Raga, G., Ramos‐Fernández, E., Guardia‐Laguarta, C., Lleó, A., Arimon, M., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201200243 · Cited by 82
Synaptic Mitochondria: An Early Target of Amyloid-β and Tau in Alzheimer’s Disease
Torres, A. K., Jara, C., Park-Kang, H. S., Polanco, C. M., Tapia, D., Alarcón, F., de la Peña, A., Llanquinao, J., Vargas-Mardones, G., Álvarez‐Indo, J., et al. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215139 · Cited by 80
Dissecting the Crosstalk between Endothelial Mitochondrial Damage, Vascular Inflammation, and Neurodegeneration in Cerebral Amyloid Angiopathy and Alzheimer’s Disease
Parodi‐Rullán, R. M., Javadov, S. A., & Fossati, S. (2021) · Cells · doi:10.3390/cells10112903 · Cited by 75
Mitochondrial dihydrolipoyl succinyltransferase deficiency accelerates amyloid pathology and memory deficit in a transgenic mouse model of amyloid deposition
Dumont, M., Ho, D. J., Calingasan, N. Y., Xu, H., Gibson, G. E., & Beal, M. F. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.008 · Cited by 73
Mitochondrial Superoxide Contributes to Blood Flow and Axonal Transport Deficits in the Tg2576 Mouse Model of Alzheimer's Disease
Massaad, C. A., Amin, S. K., Hu, L., Yuan, M., Klann, E., & Pautler, R. G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010561 · Cited by 72

Authors: Esposito, L., Raber, J., Kekonius, L., Yan, F., Yu, G.-Q., Bien-Ly, N., Puoliväli, J., Scearce-Levie, K., Masliah, E., & Mucke, L.
Affiliations: University of California, San Francisco (US)
University of California San Diego (US)
Gladstone Institutes (US)
ORCID: Esposito, Luke
Raber, Jacob
Scearce-Levie, Kimberly
Masliah, Eliezer
Mucke, Lennart
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 2006-05-10
Volume: 26
Issue: 19
Pages: 5167-5179
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.0482-06.2006
PMC: PMC6674260
OpenAlex: W2109187744
Cited by: 254
References: 111
Citations by year: 2026: 5 · 2025: 6 · 2024: 9 · 2023: 12 · 2022: 14 · 2021: 16 · 2020: 18 · 2019: 8 · 2018: 11 · 2017: 13 · 2016: 13 · 2015: 16 · 2014: 16 · 2013: 10 · 2012: 12
FWCI: 10.60
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 184 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (AG‐022074, AG011385)
National Institute on Aging (AG011385, AG022074, P01AG022074)
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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords: Alzheimer's disease, manganese superoxide dismutase, amyloid precursor protein transgenic mice, amyloid-beta, mitochondrial dysfunction, oxidative stress, prepulse inhibition, sensorimotor gating, MAP2, dendritic degeneration, gliosis, neuritic dystrophy, nuclear factor-kappaB, behavioral deficits, neuroprotection
MeSH terms: Superoxide Dismutase 2, Alzheimer Disease, Animals, Mental Disorders, Enzyme Activation, Humans, Mice, Transgenic, Mitochondria, Receptors, Cell Surface, Superoxide Dismutase, Amyloid beta-Protein Precursor, Mice, Protease Nexins

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

Reduction in mitochondrial superoxide dismutase modulates Alzheimer’s disease-like pathology and accelerates the onset of behavioral changes in human amyloid precursor protein transgenic mice

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks