The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction in Alzheimer's disease: Implications for early intervention and therapeutics
Open accessAbstract
Alzheimer's disease (AD) is an age-related progressive neurodegenerative disease affecting thousands of people in the world and effective treatment is still not available. Over two decades of intense research using AD postmortem brains, transgenic mouse and cell models of amyloid precursor protein and tau revealed that amyloid beta (Aβ) and hyperphosphorylated tau are synergistically involved in triggering disease progression. Accumulating evidence also revealed that aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction initiates and contributes to the development and progression of the disease. The purpose of this article is to summarize the latest progress in aging and AD, with a special emphasis on the mitochondria, oxidative DNA damage including methods of its measurement. It also discusses the therapeutic potential of oxidative DNA damage and treatment strategies in AD.
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
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
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Structure and function of telomeres
Blackburn, E. H. (1991) · Nature · doi:10.1038/350569a0 · Cited by 3,596
Pathways towards and Away from Alzheimer’s Disease
Mattson, M. P. (2004) · Nature · doi:10.1038/nature02621 · Cited by 3,052
A DNA damage checkpoint response in telomere-initiated senescence
Fagagna, F. D. D., Reaper, P. M., Clay-Farrace, L., Fiegler, H., Carr, P., von Zglinicki, T., Saretzki, G., Carter, N. P., & Jackson, S. P. (2003) · Nature · doi:10.1038/nature02118 · Cited by 2,917 · cited 1×
“The shelterin protein complex then binds the 3' single-stranded end of telomeric DNA, protecting it from DNA damage responses [22,23].”
Oxidative stress and neurodegeneration: where are we now?
Halliwell, B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03907.x · Cited by 2,614
Hydrogen peroxide mediates amyloid β protein toxicity
Behl, C. (1994) · Cell · doi:10.1016/0092-8674(94)90131-7 · Cited by 2,074
Intracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942
Cited by
Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future
Zhang, Y., Chen, H., Li, R., Sterling, K., & Song, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01484-7 · Cited by 988
Dominguez, L. J., Veronese, N., Vernuccio, L., Catanese, G., Inzerillo, F., Salemi, G., & Barbagallo, M. (2021) · Nutrients · doi:10.3390/nu13114080 · Cited by 433
Defective mitophagy in Alzheimer’s disease
Pradeepkiran, J. A., & Reddy, P. H. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101191 · Cited by 367
Self-citationProtective Effects of Indian Spice Curcumin Against Amyloid-β in Alzheimer’s Disease
Reddy, P. H., Manczak, M., Yin, X., Grady, M. C., Mitchell, A., Tonk, S., Kuruva, C. S., Bhatti, J. S., Kandimalla, R., Vijayan, M., et al. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170512 · Cited by 354
Self-citationVenkateshappa, C., Harish, G., Mahadevan, A., Srinivas Bharath, M. M., & Shankar, S. K. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0755-8 · Cited by 232
Harris, S. S., Wolf, F., De Strooper, B., & Busche, M. A. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.005 · Cited by 161
Genetic reduction of Nrf2 exacerbates cognitive deficits in a mouse model of Alzheimer’s disease
Branca, C., Ferreira, E., Nguyen, T.-V., Doyle, K., Caccamo, A., & Oddo, S. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx361 · Cited by 139
Bhatti, G. K., Reddy, A. P., Reddy, P. H., & Bhatti, J. S. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00369 · Cited by 145
Self-citationA critical evaluation of neuroprotective and neurodegenerative MicroRNAs in Alzheimer's disease
Reddy, P. H., Tonk, S., Kumar, S., Vijayan, M., Kandimalla, R., Kuruva, C. S., & Reddy, A. P. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.08.067 · Cited by 143
Self-citationLinking mitochondrial dysfunction, metabolic syndrome and stress signaling in Neurodegeneration
Jha, S. K., Jha, N. K., Kumar, D., Ambasta, R. K., & Kumar, P. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.06.015 · Cited by 122
Molecular Basis of Alzheimer’s Disease: Focus on Mitochondria
Oliver, D. M. A., & Reddy, P. H. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190048 · Cited by 120
Self-citationReddy, P. H., Manczak, M., & Yin, X. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170051 · Cited by 116
Self-citationEpigenetic memory: The Lamarckian brain
Fischer, A. (2014) · The EMBO Journal · doi:10.1002/embj.201387637 · Cited by 107
Oxidative challenge in Alzheimer's disease: state of knowledge and future needs
Cervellati, C., Wood, P. L., Romani, A., Valacchi, G., Squerzanti, M., Sanz, J. M., Ortolani, B., & Zuliani, G. (2016) · Journal of Investigative Medicine · doi:10.1136/jim-2015-000017 · Cited by 75
Papadaniil, C. D., Kosmidou, V. E., Tsolaki, A., Tsolaki, M., Kompatsiaris, I. (., & Hadjileontiadis, L. J. (2016) · Brain Research · doi:10.1016/j.brainres.2016.07.043 · Cited by 71
Siddik, M. A. B., Mullins, C. A., Kramer, A., Shah, H., Gannaban, R. B., Zabet-Moghaddam, M., Huebinger, R. M., Hegde, V. K., MohanKumar, S. M. J., MohanKumar, P. S., et al. (2022) · Cells · doi:10.3390/cells11213523 · Cited by 68
Pathophysiology of Alzheimer’s Disease
Yarns, B. C., Holiday, K. A., Carlson, D. M., Cosgrove, C. K., & Melrose, R. J. (2022) · Psychiatric Clinics of North America · doi:10.1016/j.psc.2022.07.003 · Cited by 68
Nuclear and mitochondrial DNA oxidation in Alzheimer's disease
Santos, R. X., Correia, S. C., Zhu, X., Lee, H.-G., Petersen, R. B., Nunomura, A., Smith, M. A., Perry, G., & Moreira, P. I. (2012) · Free Radical Research · doi:10.3109/10715762.2011.648188 · Cited by 57
Barone, E., Head, E., Butterfield, D. A., & Perluigi, M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.508 · Cited by 53
Calcium-Sensing Receptors of Human Neural Cells Play Crucial Roles in Alzheimer's Disease
Chiarini, A., Armato, U., Liu, D., & Dal Prà, I. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00134 · Cited by 51
Mitochondria and Cellular Redox State on the Route from Ageing to Alzheimer's Disease
Abate, G., Vezzoli, M., Sandri, M., Rungratanawanich, W., Memo, M., & Uberti, D. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111385 · Cited by 41
Perluigi, M., Tramutola, A., Pagnotta, S., Barone, E., & Butterfield, D. A. (2020) · Antioxidants · doi:10.3390/antiox9090779 · Cited by 39
Islam, M. A., Sultana, O. F., Bandari, M., Kshirsagar, S., Manna, P. R., & Reddy, P. H. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102459 · Cited by 28
Self-citation
Metadata
- Authors
- Mao, P., & Reddy, P. H.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
- Publisher
- Elsevier BV
- Published
- 2011-11
- Volume
- 1812
- Issue
- 11
- Pages
- 1359-1370
- ISSN
- 0925-4439 (ISSN-L)
- OpenAlex
- W2116485041
- Cited by
- 313
- References
- 49
- FWCI
- 12.90
- Type
- journal article
- Language
- en
- Open access
- bronze
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