Mitochondria and Cellular Redox State on the Route from Ageing to Alzheimer's Disease

How mitochondria produce reactive oxygen species

Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works

The amyloid hypothesis of Alzheimer's disease at 25 years

Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164 · see citing works

Calcium signalling: dynamics, homeostasis and remodelling

Berridge, M., Bootman, M., & Roderick, H. (2003) · Nature reviews. Molecular cell biology · doi:10.1038/nrm1155 · Cited by 5,747 · see citing works

Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release

Zorov, D. B., Juhaszova, M., & Sollott, S. J. (2014) · Physiological Reviews · doi:10.1152/physrev.00026.2013 · Cited by 5,383 · see citing works

Reactive oxygen species (ROS) as pleiotropic physiological signalling agents

Sies, H., & Jones, D. P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0230-3 · Cited by 5,335 · see citing works

The unfolded protein response: controlling cell fate decisions under ER stress and beyond

Hetz, C. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3270 · Cited by 4,118 · see citing works

First line defence antioxidants-superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX): Their fundamental role in the entire antioxidant defence grid

Ighodaro, O. M., & Akinloye, O. A. (2017) · Alexandria Journal of Medicine · doi:10.1016/j.ajme.2017.09.001 · Cited by 3,970 · see citing works

Hereditary Early-Onset Parkinson's Disease Caused by Mutations in <i>PINK1</i>

Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481 · see citing works

Neuropathological alterations in Alzheimer disease

Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345 · see citing works

Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases

Phaniendra, A., Jestadi, D. B., & Periyasamy, L. (2015) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-014-0446-0 · Cited by 2,886 · see citing works

Alzheimer's disease

Lane, C. A., Hardy, J., & Schott, J. M. (2018) · European Journal of Neurology · doi:10.1111/ene.13439 · Cited by 2,616 · see citing works

World Alzheimer Report 2015 - The Global Impact of Dementia:An analysis of prevalence, incidence, cost and trends

(2015) · HAL · Cited by 2,238 · see citing works

Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: Oxidative eustress

Sies, H. (2017) · Redox Biology · doi:10.1016/j.redox.2016.12.035 · Cited by 2,148 · see citing works

Regulation of antioxidant enzymes: a significant role for melatonin

Rodrı́guez, C., Mayo, J. C., Sainz, R. M., Antolı́n, I., Herrera, F., Martı́n, V., & Reiter, R. J. (2003) · Journal of Pineal Research · doi:10.1046/j.1600-079x.2003.00092.x · Cited by 1,990 · see citing works

Mitochondria: Dynamic Organelles in Disease, Aging, and Development

Chan, D. C. (2006) · Cell · doi:10.1016/j.cell.2006.06.010 · Cited by 1,987 · see citing works

Ros and ros-mediated cellular signaling

Zhang, J., Wang, X., Vikash, V., Ye, Q., Wu, D., Liu, Y., & Dong, W. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4350965 · Cited by 1,980 · see citing works

Mitochondrial DNA damage is more extensive and persists longer than nuclear DNA damage in human cells following oxidative stress

Yakes, F. M., & Van Houten, B. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.2.514 · Cited by 1,854 · see citing works

Mitophagy inhibits amyloid-β and tau pathology and reverses cognitive deficits in models of Alzheimer’s disease

Fang, E. F., Hou, Y., Palikaras, K., Adriaanse, B. A., Kerr, J. S., Yang, B., Lautrup, S., Hasan-Olive, M. M., Caponio, D., Dan, X., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0332-9 · Cited by 1,740 · see citing works

Transcriptional paradigms in mammalian mitochondrial biogenesis and function

Scarpulla, R. C. (2008) · Physiological Reviews · doi:10.1152/physrev.00025.2007 · Cited by 1,666 · see citing works

Pathology of Neurodegenerative Diseases

Dugger, B. N., & Dickson, D. W. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028035 · Cited by 1,665 · see citing works

Functions and dysfunctions of mitochondrial dynamics

Detmer, S. A., & Chan, D. C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2275 · Cited by 1,369 · see citing works

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 · see citing works

Oxidative stress and mitochondrial dysfunction in Alzheimer’s disease

Wang, X., Wang, W., Li, L., Perry, G., Lee, H.-G., & Zhu, X. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.015 · Cited by 1,357 · see citing works

Mitochondrial metabolism of reactive oxygen species

Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336 · see citing works

Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide: Implications for neurodegenerative diseases

Cleeter, M. W. J., Cooper, J. M., Darley-Usmar, V. M., Moncada, S., & Schapira, A. H. V. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00424-2 · Cited by 1,241 · see citing works

Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission

Losón, O. C., Song, Z., Chen, H., & Chan, D. C. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0721 · Cited by 1,235 · see citing works

Hydrogen Peroxide: A Signaling Messenger

Stone, J. R., & Yang, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.243 · Cited by 1,175 · see citing works

The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore

Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R., & Wallace, D. C. (2004) · Nature · doi:10.1038/nature02229 · Cited by 1,086 · see citing works

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 · see citing works

Positron Emission Tomography in Evaluation of Dementia

Silverman, D. H. S., Small, G. W., Chang, C. Y., Lu, C. S., de Aburto, M. A. K., Chen, W., Czernin, J. G., Rapoport, S. I., Pietrini, P., Alexander, G. E., et al. (2001) · JAMA · doi:10.1001/jama.286.17.2120 · Cited by 939 · see citing works

Recent global trends in the prevalence and incidence of dementia, and survival with dementia

Prince, M., Ali, G.-C., Guerchet, M., Prina, A. M., Albanese, E., & Wu, Y.-T. (2016) · Alzheimer's Research &amp; Therapy · doi:10.1186/s13195-016-0188-8 · Cited by 876 · see citing works

Glutathione: new roles in redox signaling for an old antioxidant

Aquilano, K., Baldelli, S., & Ciriolo, M. R. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00196 · Cited by 869 · see citing works

Hydrogen peroxide sensing, signaling and regulation of transcription factors

Marinho, H. S., Real, C., Cyrne, L., Soares, H., & Antunes, F. (2014) · Redox Biology · doi:10.1016/j.redox.2014.02.006 · Cited by 851 · see citing works

The role of mitochondria in reactive oxygen species metabolism and signaling

Starkov, A. A. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.015 · Cited by 846 · see citing works

How increased oxidative stress promotes longevity and metabolic health: The concept of mitochondrial hormesis (mitohormesis)

Ristow, M., & Zarse, K. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.03.014 · Cited by 789 · see citing works

Biochemistry, Physiology, and Pathophysiology of NADPH Oxidases in the Cardiovascular System

Lassegue, B. P., Martín, A. S., & Griendling, K. K. (2012) · Circulation Research · doi:10.1161/circresaha.111.243972 · Cited by 768 · see citing works

Mitochondrial dysfunction is a trigger of Alzheimer's disease pathophysiology

Moreira, P. I., Carvalho, C., Zhu, X., Smith, M. A., & Perry, G. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.10.006 · Cited by 734 · see citing works

The amyloid β-peptide is imported into mitochondria via the TOM import machinery and localized to mitochondrial cristae

Hansson Petersen, C. A., Alikhani, N., Behbahani, H., Wiehager, B., Pavlov, P. F., Alafuzoff, I., Leinonen, V., Ito, A., Winblad, B., Glaser, E., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806192105 · Cited by 693 · see citing works

Mitochondria-Ros Crosstalk in the Control of Cell Death and Aging

Marchi, S., Giorgi, C., Suski, J. M., Agnoletto, C., Bononi, A., Bonora, M., Marchi, E. D., Missiroli, S., Patergnani, S., Poletti, F., et al. (2011) · Journal of Signal Transduction · doi:10.1155/2012/329635 · Cited by 639 · see citing works

Mitohormesis

Yun, J., & Finkel, T. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.01.011 · Cited by 626 · see citing works

Oxidative stress in the progression of Alzheimer disease in the frontal cortex

Ansari, M. A., & Scheff, S. W. (2010) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/nen.0b013e3181cb5af4 · Cited by 605 · see citing works

Peroxiredoxin-2 and STAT3 form a redox relay for H2O2 signaling

Sobotta, M. C., Liou, W., Stöcker, S., Talwar, D., Oehler, M., Ruppert, T., Scharf, A. N. D., & Dick, T. P. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1695 · Cited by 598 · see citing works

Alzheimer's disease is associated with reduced expression of energy metabolism genes in posterior cingulate neurons

Liang, W. S., Reiman, E. M., Valla, J., Dunckley, T., Beach, T. G., Grover, A., Niedzielko, T. L., Schneider, L. E., Mastroeni, D., Caselli, R., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709259105 · Cited by 585 · see citing works

The Alzheimer’s Disease Mitochondrial Cascade Hypothesis

Swerdlow, R. H., Burns, J. M., & Khan, S. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100339 · Cited by 562 · see citing works

Plasma antioxidants are similarly depleted in mild cognitive impairment and in Alzheimer’s disease

Rinaldi, P., Polidori, M. C., Metastasio, A., Mariani, E., Mattioli, P., Cherubini, A., Catani, M., Cecchetti, R., Senin, U., & Mecocci, P. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(03)00031-9 · Cited by 562 · see citing works

Mitochondrial Dysfunction and Biogenesis in Neurodegenerative diseases: Pathogenesis and Treatment

Golpich, M., Amini, E., Mohamed, Z., Raymond, A. A., Ibrahim, N. M., & Ahmadiani, A. (2016) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12655 · Cited by 540 · see citing works

Impaired Mitochondrial Biogenesis Contributes to Mitochondrial Dysfunction in Alzheimer's Disease

Sheng, B., Wang, X.-L., Su, B., Lee, H.-G., Casadesus, G., Perry, G., & Zhu, X.-W. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07581.x · Cited by 538 · see citing works

The Role of NMDA Receptors in Alzheimer’s Disease

Liu, J., Chang, L., Song, Y., Li, H., & Wu, Y. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00043 · Cited by 535 · see citing works

A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients

Maurer, I. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00112-3 · Cited by 475 · see citing works

Understanding disease progression and improving Alzheimer's disease clinical trials: Recent highlights from the Alzheimer's Disease Neuroimaging Initiative

Veitch, D. P., Weiner, M. W., Aisen, P. S., Beckett, L. A., Cairns, N. J., Green, R. C., Harvey, D., Jack, C. R., Jagust, W., Morris, J. C., et al. (2019) · Alzheimer's &amp; Dementia · doi:10.1016/j.jalz.2018.08.005 · Cited by 454 · see citing works

Mitochondrial DNA damage and reactive oxygen species in neurodegenerative disease

Nissanka, N., & Moraes, C. T. (2017) · FEBS Letters · doi:10.1002/1873-3468.12956 · Cited by 453 · see citing works

Mitochondrial dysfunction in Alzheimer's disease: role in pathogenesis and novel therapeutic opportunities

Perez Ortiz, J. M., & Swerdlow, R. H. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14585 · Cited by 426 · see citing works

Oxidative Stress and Aging

Dröge, W. (2003) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-8997-0_14 · Cited by 415 · see citing works

Antioxidant Therapies for Alzheimer's Disease

Feng, Y., & Wang, X. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/472932 · Cited by 382 · see citing works

Changes of some oxidative stress markers in the serum of patients with mild cognitive impairment and Alzheimer's disease

Padurariu, M., Ciobica, A., Hritcu, L., Stoica, B., Bild, W., & Stefanescu, C. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.033 · Cited by 378 · see citing works

Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore

McSTAY, G. P., CLARKE, S. J., & HALESTRAP, A. P. (2002) · Biochemical Journal · doi:10.1042/bj20011672 · Cited by 367 · see citing works

High aggregate burden of somatic mtDNA point mutations in aging and Alzheimer's disease brain

Lin, M. T. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.2.133 · Cited by 366 · see citing works

Mitochondrial biogenesis and healthy aging

López-Lluch, G., Irusta, P. M., Navas, P., & de Cabo, R. (2008) · Experimental Gerontology · doi:10.1016/j.exger.2008.06.014 · Cited by 364 · see citing works

Mitochondrial VDAC1: A Key Gatekeeper as Potential Therapeutic Target

Camara, A. K. S., Zhou, Y., Wen, P., Tajkhorshid, E., & Kwok, W.-M. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00460 · Cited by 357 · see citing works

Mitochondrion-derived reactive oxygen species lead to enhanced amyloid beta formation

Leuner, K., Schütt, T., Kurz, C., Eckert, S. H., Schiller, C., Occhipinti, A., Mai, S., Jendrach, M., Eckert, G. P., Kruse, S. E., et al. (2012) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2011.4173 · Cited by 354 · see citing works

Cytochrome c Nitration by Peroxynitrite

Cassina, A. M., Hodara, R., Souza, J. M., Thomson, L., Castro, L., Ischiropoulos, H., Freeman, B. A., & Radi, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909978199 · Cited by 354 · see citing works

DNA repair deficiency in neurodegeneration

Jeppesen, D. K., Bohr, V. A., & Stevnsner, T. (2011) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2011.04.013 · Cited by 349 · see citing works

Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols

Brown, G. C., & Borutaite, V. (2004) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2004.03.016 · Cited by 344 · see citing works

Brain oxidative stress in a triple-transgenic mouse model of Alzheimer disease

Resende, R., Moreira, P. I., Proença, T., Deshpande, A., Busciglio, J., Pereira, C., & Oliveira, C. R. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.012 · Cited by 343 · see citing works

Effects of antioxidant supplementation on the aging process.

Fusco, D., Colloca, G. A., Monaco, M. R. L., & Cesari, M. (2007) · PubMed Central · Cited by 340 · see citing works

The role of STAT3 in leading the crosstalk between human cancers and the immune system

Wang, Y., Shen, Y., Wang, S., Shen, Q., & Zhou, X. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.12.003 · Cited by 340 · see citing works

Regulation of ATP production by mitochondrial Ca2+

Tarasov, A. I., Griffiths, E. J., & Rutter, G. A. (2012) · Cell Calcium · doi:10.1016/j.ceca.2012.03.003 · Cited by 319 · see citing works

Aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction in Alzheimer's disease: Implications for early intervention and therapeutics

Mao, P., & Reddy, P. H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.08.005 · Cited by 311 · see citing works

Architectural Role of Mitochondrial Transcription Factor A in Maintenance of Human Mitochondrial DNA

Kanki, T., Ohgaki, K., Gaspari, M., Gustafsson, C. M., Fukuoh, A., Sasaki, N., Hamasaki, N., & Kang, D. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.22.9823-9834.2004 · Cited by 308 · see citing works

Brain aging, Alzheimer's disease, and mitochondria

Swerdlow, R. H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.08.012 · Cited by 306 · see citing works

Oxidative Stress Induces Intracellular Accumulation of Amyloid β-Protein (Aβ) in Human Neuroblastoma Cells

Misonou, H., Morishima-Kawashima, M., & Ihara, Y. (2000) · Biochemistry · doi:10.1021/bi000169p · Cited by 304 · see citing works

Mitochondrial dynamics in cell death and neurodegeneration

Cho, D., Nakamura, T., & Lipton, S. A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0435-2 · Cited by 299 · see citing works

Defective DNA base excision repair in brain from individuals with Alzheimer's disease and amnestic mild cognitive impairment

Weissman, L., Jo, D.-G., Sorensen, M. M., de Souza-Pinto, N. C., Markesbery, W. R., Mattson, M. P., & Bohr, V. A. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm605 · Cited by 299 · see citing works

ROS and RNS signalling: adaptive redox switches through oxidative/nitrosative protein modifications

Moldogazieva, N. T., Mokhosoev, I. M., Feldman, N. B., & Lutsenko, S. V. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1457217 · Cited by 291 · see citing works

Abnormal mitochondrial dynamics and neurodegenerative diseases

Su, B., Wang, X., Zheng, L., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.013 · Cited by 289 · see citing works

VDAC1, mitochondrial dysfunction, and Alzheimer’s disease

Shoshan-Barmatz, V., Nahon-Crystal, E., Shteinfer-Kuzmine, A., & Gupta, R. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.03.010 · Cited by 286 · see citing works

Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis

Costantini, P., Belzacq, A.-S., Vieira, H. L., Larochette, N., de Pablo, M. A., Zamzami, N., Susin, S. A., Brenner, C., & Kroemer, G. (2000) · Oncogene · doi:10.1038/sj.onc.1203299 · Cited by 284 · see citing works

The Free Radical Theory of Aging Is Dead. Long Live the Damage Theory!

Gladyshev, V. N. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5228 · Cited by 281 · see citing works

Diagnosis and treatment of dementia: 1. Risk assessment and primary prevention of Alzheimer disease

Patterson, C., Feightner, J., Garcia, A. C. S., Hsiung, G. R., MacKnight, C., & Sadovnick, A. D. (2008) · Canadian Medical Association Journal · doi:10.1503/cmaj.070796 · Cited by 266 · see citing works

Cause and consequence: Mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases

Gibson, G. E., Starkov, A. A., Blass, J. P., Ratan, R. R., & Beal, M. F. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.08.010 · Cited by 256 · see citing works

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

Esposito, L., Raber, J., Kekonius, L., Yan, F., Yu, G.-Q., Bien-Ly, N., Puoliväli, J., Scearce-Levie, K., Masliah, E., & Mucke, L. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.0482-06.2006 · Cited by 254 · see citing works

Superresolution Fluorescence Imaging of Mitochondrial Nucleoids Reveals Their Spatial Range, Limits, and Membrane Interaction

Brown, T., Tkachuk, A. N., Shtengel, G., Kopek, B. G., Bogenhagen, D., Hess, H., & Clayton, D. A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05694-11 · Cited by 254 · see citing works

Inhibition of mitochondrial permeability transition by deletion of the ANT family and CypD

Karch, J., Bround, M. J., Khalil, H., Sargent, M. A., Latchman, N., Terada, N., Peixoto, P. M., & Molkentin, J. D. (2019) · Science Advances · doi:10.1126/sciadv.aaw4597 · Cited by 250 · see citing works

Redox-Dependent Modulation of Aconitase Activity in Intact Mitochondria

Bulteau, A.-L., Ikeda-Saito, M., & Szweda, L. I. (2003) · Biochemistry · doi:10.1021/bi0353979 · Cited by 241 · see citing works

A key role for MAM in mediating mitochondrial dysfunction in Alzheimer disease

Area-Gomez, E., de Groof, A., Bonilla, E., Montesinos, J., Tanji, K., Boldogh, I., Pon, L., & Schon, E. A. (2018) · Cell Death &amp; Disease · doi:10.1038/s41419-017-0215-0 · Cited by 235 · see citing works

Mitochondria in the signaling pathways that control longevity and health span

Akbari, M., Kirkwood, T. B. L., & Bohr, V. A. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100940 · Cited by 232 · see citing works

Amelioration of cognitive deficits and neurodegeneration by curcumin in rat model of sporadic dementia of Alzheimer’s type (SDAT)

Ishrat, T., Hoda, M. N., Khan, M. B., Yousuf, S., Ahmad, M., Khan, M. M., Ahmad, A., & Islam, F. (2009) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2009.02.002 · Cited by 230 · see citing works

The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal

Forman, H. J., Fukuto, J. M., Miller, T., Zhang, H., Rinna, A., & Levy, S. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.06.011 · Cited by 226 · see citing works

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 · see citing works

Oxidant/Antioxidant Imbalance in Alzheimer’s Disease: Therapeutic and Diagnostic Prospects

Wojsiat, J., Zoltowska, K. M., Laskowska-Kaszub, K., & Wojda, U. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/6435861 · Cited by 221 · see citing works

Oxidatively modified proteins in Alzheimer’s disease (AD), mild cognitive impairment and animal models of AD: role of Abeta in pathogenesis

Sultana, R., Perluigi, M., & Butterfield, D. A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0517-0 · Cited by 215 · see citing works

Peroxisomal Hydrogen Peroxide Metabolism and Signaling in Health and Disease

Lismont, C., Revenco, I., & Fransen, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153673 · Cited by 206 · see citing works

Nitric oxide induces conformational and functional modifications of wild-type p53 tumor suppressor protein.

Calmels, S., Hainaut, P. L., & Ohshima, H. (1997) · PubMed · Cited by 188 · see citing works

Regulation of neuron mitochondrial biogenesis and relevance to brain health

Onyango, I. G., Lu, J., Rodova, M., Lezi, E., Crafter, A. B., & Swerdlow, R. H. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.014 · Cited by 188 · see citing works

Role of p53 in Sensing Oxidative DNA Damage in Response to Reactive Oxygen Species-Generating Agents

Achanta, G., & Huang, P. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0494 · Cited by 184 · see citing works

P53 physically interacts with mitochondrial transcription factor A and differentially regulates binding to damaged DNA.

Yoshida, Y., Izumi, H., Torigoe, T., Ishiguchi, H., Itoh, H., Kang, D., & Kohno, K. (2003) · PubMed · Cited by 177 · see citing works

Mitochondrial pathways for ROS formation and myocardial injury: the relevance of p66Shc and monoamine oxidase

Lisa, F. D., Kaludercic, N., Carpi, A., Menabò, R., & Giorgio, M. (2009) · Basic Research in Cardiology · doi:10.1007/s00395-009-0008-4 · Cited by 175 · see citing works

Redox modulation of mitochondriogenesis in exercise. Does antioxidant supplementation blunt the benefits of exercise training?

Gomez-Cabrera, M. C., Salvador-Pascual, A., Cabo, H., Ferrando, B., & Viña, J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.04.006 · Cited by 172 · see citing works

The Good, the Bad, and the Ugly of ROS: New Insights on Aging and Aging‐Related Diseases from Eukaryotic and Prokaryotic Model Organisms

Santos, A. L., Sinha, S., & Lindner, A. B. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1941285 · Cited by 168 · see citing works

Redox signalling and transition metals in the control of the p53 pathway

Méplan, C., Richard, M., & Hainaut, P. L. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00297-x · Cited by 163 · see citing works

Human Mitochondrial DNA ReplicationPreprint

Holt, I. J., & Reyes, A. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012971 · Cited by 155 · see citing works

Mitochondrial Nucleoid: Shield and Switch of the Mitochondrial Genome

Lee, S. R., & Han, J. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/8060949 · Cited by 151 · see citing works

Aging, lifestyle and dementia

Wahl, D., Solon‐Biet, S. M., Cogger, V. C., Fontana, L., Simpson, S. J., Couteur, D. G. L., & Ribeiro, R. V. (2019) · Neurobiology of Disease · doi:10.1016/j.nbd.2019.104481 · Cited by 151 · see citing works

The mitochondrial transcription factor A functions in mitochondrial base excision repair

Canugovi, C., Maynard, S., Bayne, A.-C. V., Sýkora, P., Tian, J., de Souza-Pinto, N. C., Croteau, D. L., & Bohr, V. A. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.07.009 · Cited by 147 · see citing works

Role of p53 in Neurodegenerative Diseases

Chang, J. R., Ghafouri, M., Mukerjee, R., Bagashev, A., Chabrashvili, T., & Sawaya, B. E. (2011) · Neurodegenerative Diseases · doi:10.1159/000329999 · Cited by 145 · see citing works

The voltage-dependent anion channel 1 mediates amyloid β toxicity and represents a potential target for Alzheimer disease therapy

Smilansky, A., Dangoor, L., Nakdimon, I., Ben-Hail, D., Mizrachi, D., & Shoshan-Barmatz, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691493 · Cited by 143 · see citing works

Acute exercise induces tumour suppressor protein p53 translocation to the mitochondria and promotes a p53–Tfam–mitochondrial DNA complex in skeletal muscle

Saleem, A., & Hood, D. A. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.252791 · Cited by 141 · see citing works

Plasma oxidative stress parameters in men and women with early stage Alzheimer type dementia

Puertas, M. C., Martı́nez-Martos, J. M., Cobo, M., Carrera-González, M. P., Mayas, M. D., & Ramı́rez-Expósito, M. J. (2012) · Experimental Gerontology · doi:10.1016/j.exger.2012.05.019 · Cited by 140 · see citing works

Peripheral Mitochondrial Dysfunction in Alzheimer’s Disease: Focus on Lymphocytes

Leuner, K., Schulz, K. L., Schuett, T., Pantel, J., Prvulovic, D., Rhein, V. F., Savaskan, E., Czech, C., Eckert, A., & Müller, W. E. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8300-y · Cited by 127 · see citing works

Oxidative stress induces DNA demethylation and histone acetylation in SH-SY5Y cells: potential epigenetic mechanisms in gene transcription in Aβ production

Gu, X., Sun, J., Li, S., Wu, X., & Li, L. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.10.013 · Cited by 127 · see citing works

Visual Data Mining : Techniques and Tools for Data Visualization and Mining

Soukup, T., & Davidson, I. A. K. (2002) · Cited by 123 · see citing works

Roles of 3-nitrotyrosine- and 4-hydroxynonenal-modified brain proteins in the progression and pathogenesis of Alzheimer's disease

Butterfield, D. A., Reed, T. T., & Rukhsana Sultana, A. (2010) · Free Radical Research · doi:10.3109/10715762.2010.520014 · Cited by 123 · see citing works

Lipid peroxidation up‐regulates BACE1 expression in vivo : a possible early event of amyloidogenesis in Alzheimer’s disease

Chen, L., Na, R., Gu, M., Richardson, A. G., & Ran, Q. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05603.x · Cited by 119 · see citing works

Oxidative post-translational modifications and their involvement in the pathogenesis of autoimmune diseases

Ryan, B. J., Nissim, A., & Winyard, P. G. (2014) · Redox Biology · doi:10.1016/j.redox.2014.05.004 · Cited by 119 · see citing works

Measurement of Mitochondrial ROS Production

Starkov, A. A. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-756-3_16 · Cited by 117 · see citing works

Protein Levels and Activity of Some Antioxidant Enzymes in Hippocampus of Subjects with Amnestic Mild Cognitive Impairment

Rukhsana Sultana, A., Piroddi, M., Galli, F., & Butterfield, D. A. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9593-0 · Cited by 115 · see citing works

The Cerebrocortical Areas in Normal Brain Aging and in Alzheimer's Disease: Noticeable Differences in the Lipid Peroxidation Level and in Antioxidant Defense

Karelson, E., Bogdanović, N., Garlind, A., Winblad, B. G., Zilmer, K., Kullisaar, T., Vihalemm, T., Kairane, C., & Zilmer, M. (2001) · Neurochemical Research · doi:10.1023/a:1010942929678 · Cited by 114 · see citing works

Biophysical characterizations of human mitochondrial transcription factor A and its binding to tumor suppressor p53

Wong, T. S., Rajagopalan, S., Freund, S. M. V., Rutherford, T. J., Andreeva, A. E., Townsley, F. M., Petrovich, M., & Fersht, A. R. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp750 · Cited by 107 · see citing works

Novel Nox homologues in the vasculature: focusing on Nox4 and Nox5

Montezano, A. C. I., Burger, D. E., Ceravolo, G. S., Yusuf, H., Montero, M. J., & Touyz, R. M. (2010) · Clinical Science · doi:10.1042/cs20100384 · Cited by 106 · see citing works

The Aging Mitochondria

Theurey, P., & Pizzo, P. (2018) · Genes · doi:10.3390/genes9010022 · Cited by 103 · see citing works

Amyloid β Oligomers Increase ER-Mitochondria Ca2+ Cross Talk in Young Hippocampal Neurons and Exacerbate Aging-Induced Intracellular Ca2+ Remodeling

Calvo-Rodríguez, M., Hernando-Pérez, E., Núñez, L., & Villalobos, C. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00022 · Cited by 101 · see citing works

The interactions of p53 with tau and Aß as potential therapeutic targets for Alzheimer’s disease

Jembrek, M. J., Slade, N., Hof, P. R., & Šimić, G. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.05.001 · Cited by 99 · see citing works

Correlation-Based Network Generation, Visualization, and Analysis as a Powerful Tool in Biological Studies: A Case Study in Cancer Cell Metabolism

Batushansky, A., Toubiana, D., & Fait, A. (2016) · BioMed Research International · doi:10.1155/2016/8313272 · Cited by 98 · see citing works

Mechanisms of Mitochondrial DNA Repair in Mammals

Zinovkina, L. A. (2018) · Biochemistry (Moscow) · doi:10.1134/s0006297918030045 · Cited by 97 · see citing works

Modulation of mitochondrial dysfunction in neurodegenerative diseases via activation of nuclear factor erythroid-2-related factor 2 by food-derived compounds

Denzer, I., Münch, G. W., & Friedland, K. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.11.019 · Cited by 90 · see citing works

The Dual Function of Reactive Oxygen/Nitrogen Species in Bioenergetics and Cell Death: The Role of ATP Synthase

Kaludercic, N., & Giorgio, V. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3869610 · Cited by 88 · see citing works

The Roles of p53 in Mitochondrial Dynamics and Cancer Metabolism: The Pendulum between Survival and Death in Breast Cancer?

Moulder, D. E., Hatoum, D., Tay, E. S. E., Lin, Y., & McGowan, E. M. (2018) · Cancers · doi:10.3390/cancers10060189 · Cited by 83 · see citing works

Conformational Altered p53 as an Early Marker of Oxidative Stress in Alzheimer's Disease

Buizza, L., Cenini, G., Lanni, C., Ferrari‐Toninelli, G., Prandelli, C., Govoni, S. M., Buoso, E., Racchi, M., Barcikowska, M., Styczyńska, M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029789 · Cited by 81 · see citing works

Mitochondrial Alterations in Peripheral Mononuclear Blood Cells from Alzheimer’s Disease and Mild Cognitive Impairment Patients

Delbarba, A., Abate, G., Prandelli, C., Marziano, M., Buizza, L., Varas, N. A., Novelli, A., Cuetos, F., Martínez, C., Lanni, C., et al. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/5923938 · Cited by 80 · see citing works

The impact of thiol peroxidases on redox regulation

Flohé, L. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1046858 · Cited by 79 · see citing works

p53 in mitochondria enhances the accuracy of DNA synthesis

Bakhanashvili, M., Grinberg, S., Bonda, E., Simon, A. J., Moshitch-Moshkovitz, S., & Rahav, G. (2008) · Cell Death and Differentiation · doi:10.1038/cdd.2008.122 · Cited by 75 · see citing works

Mitochondrial Liaisons of p53

Galluzzi, L., Morselli, E., Kepp, O., Vitale, I., Pinti, M., & Kroemer, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3504 · Cited by 74 · see citing works

Flavonoids as Putative Inducers of the Transcription Factors Nrf2, FoxO, and PPARγ

Pallauf, K., Duckstein, N., Hasler, M., Klotz, L., & Rimbach, G. H. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/4397340 · Cited by 71 · see citing works

Impaired Transcription in Alzheimer's Disease: Key Role in Mitochondrial Dysfunction and Oxidative Stress

Caldeira, G. L., Ferreira, I. L., & Rego, A. C. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121444 · Cited by 70 · see citing works

Glutathione Adducts on Sarcoplasmic/Endoplasmic Reticulum Ca2+ ATPase Cys-674 Regulate Endothelial Cell Calcium Stores and Angiogenic Function as Well as Promote Ischemic Blood Flow Recovery

Thompson, M. D., Mei, Y., Weisbrod, R. M., Silver, M., Shukla, P. C., Bolotina, V. M., Cohen, R. A., & Tong, X. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.554451 · Cited by 70 · see citing works

Deficits in the mitochondrial enzyme α-ketoglutarate dehydrogenase lead to Alzheimer's disease-like calcium dysregulation

Gibson, G. E., Chen, H., Xu, H., Qiu, L., Xu, Z., Denton, T. T., & Shi, Q. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.003 · Cited by 69 · see citing works

Bcl-2 family in inter-organelle modulation of calcium signaling; roles in bioenergetics and cell survival

Lewis, A., Hayashi, T., Su, T.-P., & Betenbaugh, M. J. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-013-9527-7 · Cited by 66 · see citing works

Integrating the UPRmtinto the mitochondrial maintenance network

Fiorese, C. J., & Haynes, C. M. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1291577 · Cited by 66 · see citing works

Base excision DNA repair levels in mitochondrial lysates of Alzheimer's disease

Canugovi, C., Shamanna, R. A., Croteau, D. L., & Bohr, V. A. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.01.004 · Cited by 61 · see citing works

Redox activation of mitochondrial intermembrane space Cu,Zn-superoxide dismutase

Iñarrea, P., Moini, H., Rettori, D., Han, D., MARTÍNEZ, J., García‐Rubio, I., Fernández‐Vizarra, E., Iturralde, M., & Cadenas, E. (2005) · Biochemical Journal · doi:10.1042/bj20041683 · Cited by 59 · see citing works

Search for Alzheimer's Disease Biomarkers in Blood Cells: Hypotheses-Driven Approach

Wojsiat, J., Laskowska-Kaszub, K., Mietelska‐Porowska, A., & Wojda, U. (2017) · Biomarkers in Medicine · doi:10.2217/bmm-2017-0041 · Cited by 58 · see citing works

Superoxide radical as electron donor for oxidative phosphorylation of ADP

Mailer, K. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)91240-s · Cited by 55 · see citing works

Applied Statistics for Network Biology

(2011) · Wiley eBooks · doi:10.1002/9783527638079 · Cited by 54 · see citing works

Lymphocytic mitochondrial aconitase activity is reduced in Alzheimer’s disease and mild cognitive impairment

Mangialasche, F., Baglioni, M., Cecchetti, R., Kivipelto, M., Ruggiero, C., Piobbico, D., Kussmaul, L., Monastero, R., Brancorsini, S., & Mecocci, P. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142052 · Cited by 53 · see citing works

Homeodomain Interacting Protein Kinase 2: A Target for Alzheimer's Beta Amyloid Leading to Misfolded p53 and Inappropriate Cell Survival

Lanni, C., Nardinocchi, L., Puca, R., Stanga, S., Uberti, D. L., Memo, M., Govoni, S. M., D’Orazi, G., & Racchi, M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010171 · Cited by 50 · see citing works

Oxidative Stress and Proteostasis Network: Culprit and Casualty of Alzheimer’s-Like Neurodegeneration

Di Domenico, F., Head, E., Butterfield, D. A., & Perluigi, M. (2014) · Advances in Geriatrics · doi:10.1155/2014/527518 · Cited by 50 · see citing works

Mitochondrial DNA Damage and Diseases

Singh, G., Pachouri, U. C., Khaidem, D. C., Kundu, A., Chopra, C., & Singh, P. P. (2015) · F1000Research · doi:10.12688/f1000research.6665.1 · Cited by 50 · see citing works

Characterization of the Antioxidant Effects of γ‐Oryzanol: Involvement of the Nrf2 Pathway

Rungratanawanich, W., Abate, G., Serafini, M. M., Guarienti, M., Catanzaro, M., Marziano, M., Memo, M., Lanni, C., & Uberti, D. L. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2987249 · Cited by 44 · see citing works

Comparison of Extracellular and Intracellular Blood Compartments Highlights Redox Alterations in Alzheimer's and Mild Cognitive Impairment Patients

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 · see citing works

The role of mitochondrial DNA damage in the citotoxicity of reactive oxygen species

Costa, R. A. P. E., Romagna, C. D., Pereira, J. L., & de Souza-Pinto, N. C. (2011) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-011-9329-8 · Cited by 41 · see citing works

Chronic Inhibition of Mitochondrial Dihydrolipoamide Dehydrogenase (DLDH) as an Approach to Managing Diabetic Oxidative Stress

Yang, X., Song, J., & Yan, L. (2019) · Antioxidants · doi:10.3390/antiox8020032 · Cited by 41 · see citing works

Dual role of oxygen during lipoxygenase reactions

Ivanov, I., Saam, J., Kühn, H., & Holzhütter, H. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04673.x · Cited by 40 · see citing works

Restoring Calcium Homeostasis to Treat Alzheimer’s Disease: A Future Perspective

Александровна, П. Е., Власова, О. Л., & Борисович, Б. И. (2015) · Neurodegenerative Disease Management · doi:10.2217/nmt.15.36 · Cited by 36 · see citing works

Folic acid reverses nitric oxide synthase uncoupling and prevents cardiac dysfunction in insulin resistance: Role of Ca2+/calmodulin-activated protein kinase II

Roe, N. D., He, E. Y., Wu, Z., & Ren, J. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.042 · Cited by 35 · see citing works

Irreversible oxidative post-translational modifications in heart disease

Tomin, T., Schittmayer, M., Honeder, S. E., Heininger, C., & Birner‐Gruenberger, R. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1645602 · Cited by 35 · see citing works

On Two Classes of Weighted Rank Correlation Measures Deriving from the Spearman’s ρ

Dancelli, L., Manisera, M., & Vezzoli, M. (2013) · Studies in classification, data analysis, and knowledge organization · doi:10.1007/978-3-319-00032-9_13 · Cited by 34 · see citing works

The Role of p53 in Determining Mitochondrial Adaptations to Endurance Training in Skeletal Muscle

Beyfuss, K. A., Erlich, A. T., Triolo, M., & Hood, D. A. (2018) · Scientific Reports · doi:10.1038/s41598-018-32887-0 · Cited by 34 · see citing works

Nitration of Specific Tyrosine Residues of Cytochrome c Is Associated with Caspase-Cascade Inactivation

Nakagawa, H., Komai, N., Takusagawa, M., Miura, Y., Toda, T., Miyata, N., Ozawa, T., & Ikota, N. (2007) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.30.15 · Cited by 33 · see citing works

Carbon monoxide attenuates amyloidogenesis via down‐regulation of NF‐κB‐mediated BACE1 gene expression

Kim, H. J., Joe, Y., Chen, Y., Park, G. H., Kim, U., & Chung, H. (2018) · Aging Cell · doi:10.1111/acel.12864 · Cited by 31 · see citing works

Author Correction: History and progress of hypotheses and clinical trials for Alzheimer’s disease

Liu, P., Xie, Y., Meng, X., & Kang, J. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0071-8 · Cited by 29 · see citing works

The impact of antiretroviral therapy on iron homeostasis and inflammation markers in HIV-infected patients with mild anemia

Inflammation in HIV Study Group, Quirós-Roldán, E., Castelli, F., Lanza, P., Pezzoli, C., Vezzoli, M., Biasiotto, G., & Zanella, I. (2017) · Journal of Translational Medicine · doi:10.1186/s12967-017-1358-6 · Cited by 27 · see citing works

Statistical Models for Data Analysis

Giudici, P., Ingrassia, S., & Vichi, M. (2013) · Studies in classification, data analysis, and knowledge organization · doi:10.1007/978-3-319-00032-9 · Cited by 26 · see citing works

Protein nitration profile of CD3+ lymphocytes from Alzheimer disease patients: Novel hints on immunosenescence and biomarker detection

Tramutola, A., Abate, G., Lanzillotta, C., Triani, F., Barone, E., Iavarone, F., Vincenzoni, F., Castagnola, M., Marziano, M., Memo, M., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.414 · Cited by 26 · see citing works

Activities of cytochrome c oxidase and citrate synthase in lymphocytes of obese and normal-weight subjects

Čapková, M., Houštěk, J., Hansíková, H., Hainer, V., Kunešová, M., & Zeman, J. (2002) · International Journal of Obesity · doi:10.1038/sj.ijo.0802055 · Cited by 23 · see citing works

Hydrogen peroxide in the ER: A tale of triage

Rashdan, N. A., & Pattillo, C. B. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101358 · Cited by 23 · see citing works

Electrochemical detection of different p53 conformations by using nanostructured surfaces

Tonello, S., Stradolini, F., Abate, G., Uberti, D. L., Serpelloni, M., Carrara, S., & Sardini, E. (2019) · Scientific Reports · doi:10.1038/s41598-019-53994-6 · Cited by 21 · see citing works

Autoantibodies Profile in Matching CSF and Serum from AD and aMCI patients: Potential Pathogenic Role and Link to Oxidative Damage

Domenico, F. D., Pupo, G., Giraldo, E., Lloret, A., Badía, M.-C., Schininà, M. E., Giorgi, A., Butterfield, D. A., Viña, J., & Marzia Perluigi, A. (2015) · Current Alzheimer Research · doi:10.2174/1567205013666151218131424 · Cited by 20 · see citing works

Mitochondrial DNA Integrity Is Maintained by APE1 in Carcinogen-Induced Colorectal Cancer

Ballista-Hernández, J., Martínez-Ferrer, M., Vélez, R., Climent, C., Sánchez-Vázquez, M. M., Torres-Ortiz⁎, C., Rodríguez‐Muñoz, A., Ayala‐Peña, S., & Torres‐Ramos, C. A. (2017) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-16-0218 · Cited by 18 · see citing works

Correlation Network Analysis and Knowledge Integration

Plasterer, T. N., Stanley, R., & Gombocz, E. (2011) · doi:10.1002/9783527638079.ch12 · Cited by 4 · see citing works

Flavonols and Flavones as Potential anti‐Inflammatory, Antioxidant, and Antibacterial Compounds

Chagas, M. D. S. S., Behrens, M. D., Moragas-Tellis, C. J., Penedo, G. X. M., Silva, A. R., & Gonçalves-de-Albuquerque, C. F. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/9966750 · Cited by 492 · see citing works

Redox imbalance links COVID-19 and myalgic encephalomyelitis/chronic fatigue syndrome

Paul, B. D., Lemle, M. D., Komaroff, A. L., & Snyder, S. H. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024358118 · Cited by 271 · see citing works

Aging of mesenchymal stem cell: machinery, markers, and strategies of fighting

Al‐Azab, M., Safi, M., Idiiatullina, E., Al‐Shaebi, F., & Zaky, M. Y. (2022) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-022-00366-0 · Cited by 172 · see citing works

Role of Nrf2 in Synaptic Plasticity and Memory in Alzheimer’s Disease

Davies, D. A., Adlimoghaddam, A., & Albensi, B. C. (2021) · Cells · doi:10.3390/cells10081884 · Cited by 111 · see citing works

Crosstalk between Neuron and Glial Cells in Oxidative Injury and Neuroprotection

Lee, K. H., Cha, M., & Lee, B. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413315 · Cited by 104 · see citing works

Myalgic Encephalomyelitis/Chronic Fatigue Syndrome: the biology of a neglected disease

Arron, H. E., Marsh, B. D., Khan, M. A., Jaeger, B., Kell, D., & Pretorius, E. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1386607 · Cited by 111 · see citing works

Altered Metabolism in Alzheimer Disease Brain: Role of Oxidative Stress

Rummel, N. G., & Butterfield, D. A. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0177 · Cited by 105 · see citing works

Potential and Limits of Cannabinoids in Alzheimer’s Disease Therapy

Abate, G., Uberti, D. L., & Tambaro, S. (2021) · Biology · doi:10.3390/biology10060542 · Cited by 101 · see citing works

A Functionalized Octahedral Palladium Nanozyme as a Radical Scavenger for Ameliorating Alzheimer’s Disease

Zhi, J., Yuan, X., Wei, J., Guo, X., Gong, Y., Li, J., Zhou, H., Zhang, L., & Liu, J. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c06687 · Cited by 97 · see citing works

Variation in Phytochemical, Antioxidant and Volatile Composition of Pomelo Fruit (Citrus grandis (L.) Osbeck) during Seasonal Growth and Development

Gupta, A. K., Dhua, S., Sahu, P. P., Abate, G., Mishra, P., & Mastinu, A. (2021) · Plants · doi:10.3390/plants10091941 · Cited by 85 · see citing works

Oxidative Stress and Bio-Regulation

Yoshikawa, T., & You, F. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063360 · Cited by 89 · see citing works

CISD2 maintains cellular homeostasis

Shen, Z., Huang, Y., Teng, Y., Wang, T.-W., Kao, C., Yeh, C., & Tsai, T. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.118954 · Cited by 82 · see citing works

Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes

Piccialli, I., Tedeschi, V., Caputo, L., D’Errico, S., Ciccone, R., De Feo, V., Secondo, A., & Pannaccione, A. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.876614 · Cited by 73 · see citing works

Plant Foods Rich in Antioxidants and Human Cognition: A Systematic Review

Baroni, L., Sarni, A. R., & Zuliani, C. (2021) · Antioxidants · doi:10.3390/antiox10050714 · Cited by 74 · see citing works

Phosphorylated tau as a toxic agent in synaptic mitochondria: implications in aging and Alzheimer’s disease

Tapia‐Rojas, C., Torres, A., Rivera, B., Polanco, C. M., & Jara, C. (2021) · Neural Regeneration Research · doi:10.4103/1673-5374.332125 · Cited by 48 · see citing works

Oxidative Stress and Vascular Damage in the Context of Obesity: The Hidden Guest

Martínez‐Martínez, E., Souza‐Neto, F. V., Jiménez‐González, S., & Cachofeiro, V. (2021) · Antioxidants · doi:10.3390/antiox10030406 · Cited by 42 · see citing works

Methylglyoxal affects cognitive behaviour and modulates RAGE and Presenilin-1 expression in hippocampus of aged mice

Pucci, M., Aria, F., Premoli, M., Maccarinelli, G., Mastinu, A., Bonini, S. A., Memo, M., Uberti, D. L., & Abate, G. (2021) · Food and Chemical Toxicology · doi:10.1016/j.fct.2021.112608 · Cited by 41 · see citing works

Post-translational Modifications of the p53 Protein and the Impact in Alzheimer’s Disease: A Review of the Literature

Clark, J., Kayed, R., Abate, G., Uberti, D. L., Kinnon, P., & Piccirella, S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.835288 · Cited by 37 · see citing works

A novel chitosan antioxidant bearing sulfhydryl group: Synthesis, characterization and activity assessment

Han, X., Mi, Y., Ji, Y., Sun, M., Tang, H., Dong, F., & Guo, Z. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.129816 · Cited by 35 · see citing works

Naringin protects mice from D-galactose-induced lung aging and mitochondrial dysfunction: Implication of SIRT1 pathways

Salama, A., Yassen, N. N., & Mansour, H. M. (2023) · Life Sciences · doi:10.1016/j.lfs.2023.121471 · Cited by 35 · see citing works

A Conformation Variant of p53 Combined with Machine Learning Identifies Alzheimer Disease in Preclinical and Prodromal Stages

Abate, G., Vezzoli, M., Polito, L., Guaita, A., Albani, D., Marizzoni, M., Garrafa, E., Marengoni, A., Forloni, G., Frisoni, G. B., et al. (2020) · Journal of Personalized Medicine · doi:10.3390/jpm11010014 · Cited by 31 · see citing works

BACE1 Aptamer-Modified Tetrahedral Framework Nucleic Acid to Treat Alzheimer’s Disease in an APP-PS1 Animal Model

Wang, Y., Zhu, J., Jia, W., Xiong, H., Qiu, W., Xu, R., & Lin, Y. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c14626 · Cited by 25 · see citing works

Causes of symptoms and symptom persistence in long COVID and myalgic encephalomyelitis/chronic fatigue syndrome

Komaroff, A. L., & Dantzer, R. (2025) · Cell Reports Medicine · doi:10.1016/j.xcrm.2025.102259 · Cited by 22 · see citing works

Cannabidiol as a multifaceted therapeutic agent: mitigating Alzheimer's disease pathology and enhancing cognitive function

Raïch, I., Lillo, J., Rebassa, J. B., Griñán‐Ferré, C., Bellver‐Sanchís, A., Reyes‐Resina, I., Franco, R., Pallàs, M., & Navarro, G. (2025) · Alzheimer s Research & Therapy · doi:10.1186/s13195-025-01756-0 · Cited by 20 · see citing works

Mitochondrial Dysfunction in Peripheral Blood Mononuclear Cells as Novel Diagnostic Tools for Non-Alcoholic Fatty Liver Disease: Visualizing Relationships with Known and Potential Disease Biomarkers

Garrafa, E., Segala, A., Vezzoli, M., Bottani, E., Zanini, B., Vetturi, A., Bracale, R., Ricci, C., & Valerio, A. (2023) · Diagnostics · doi:10.3390/diagnostics13142363 · Cited by 17 · see citing works

A Chiral Nanocomplex for Multitarget Therapy to Alleviate Neuropathology and Rescue Alzheimer's Cognitive Deficits

Tan, H., Huang, Y., Dong, S., Bai, Z., Chen, C., Wu, X., Chao, M., Yan, H., Wang, S., Geng, D., et al. (2023) · Small · doi:10.1002/smll.202303530 · Cited by 17 · see citing works

Why Have the Benefits of DHA Not Been Borne Out in the Treatment and Prevention of Alzheimer’s Disease? A Narrative Review Focused on DHA Metabolism and Adipose Tissue

Heath, R. J., & Wood, T. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111826 · Cited by 17 · see citing works

Reliable New Biomarkers of Mitochondrial Oxidative Stress and Neuroinflammation in Cerebrospinal Fluid and Plasma from Alzheimer’s Disease Patients: A Pilot Study

Lorenzo, R. D., Zecca, C., Chimienti, G., Latronico, T., Liuzzi, G. M., Pesce, V., Dell’Abate, M. T., Borlizzi, F., Giugno, A., Urso, D., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167792 · Cited by 17 · see citing works

Dynamic Interplay between Copper Toxicity and Mitochondrial Dysfunction in Alzheimer’s Disease

Tassone, G., Kola, A., Valensin, D., & Pozzi, C. (2021) · Life · doi:10.3390/life11050386 · Cited by 16 · see citing works

Quercetin preserves mitochondria-endoplasmic reticulum contact sites improving mitochondrial dynamics in aged myocardial cells

Jiménez, R., Zúñiga-Muñoz, A. M., Álvarez-León, E., García‐Niño, W. R., Navarrete-Anastasio, G., Soria‐Castro, E., Pérez-Torres, I., Lira‐Silva, E., Pavón, N., Cruz‐Gregorio, A., et al. (2024) · Biogerontology · doi:10.1007/s10522-024-10174-y · Cited by 15 · see citing works

Dual-responsive zeolitic imidazolate framework-90 for the combined detection and intracellular imaging of ATP and ROS

Shi, X., Ji, L., Hu, Y., Gu, J., Wang, L., Lu, W., Meng, J., Du, Y., Huang, L., Nie, D., et al. (2022) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2022.131848 · Cited by 12 · see citing works

Chronic Treatment of Ascorbic Acid Leads to Age-Dependent Neuroprotection against Oxidative Injury in Hippocampal Slice Cultures

Lee, K. H., Kim, U. J., Cha, M., & Lee, B. H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041608 · Cited by 12 · see citing works

NF-κB/c-Rel DNA-binding is reduced in substantia nigra and peripheral blood mononuclear cells of Parkinson's disease patients

Porrini, V., Pilotto, A., Vezzoli, M., Lanzillotta, A., Gennari, M. M., Bonacina, S., Alberici, A., Turrone, R., Bellucci, A., Antonini, A., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106067 · Cited by 11 · see citing works

In Silico Prediction of Quercetin Analogs for Targeting Death-Associated Protein Kinase 1 (DAPK1) Against Alzheimer’s Disease

Sun, Y., Zhao, J. W., Lu, Y., Ngo, F. Y., Shuai, B., Zhang, Z., Feng, Y., & Rong, J. (2024) · Current Neuropharmacology · doi:10.2174/1570159x22666240515090434 · Cited by 8 · see citing works

Proanthocyanidins supplemented diet alter anti-aging-markers and improved lifespan in Drosophila melanogaster model

Mohammed, J. S., Muhammad, S. A., Mohammed, Z. K., Yakubu, A., & Razis, A. F. A. (2024) · Beni-Suef University Journal of Basic and Applied Sciences · doi:10.1186/s43088-024-00469-x · Cited by 5 · see citing works

Oxidative stress and pancreatic cancer: a dual role in tumorigenesis and drug toxicity

Limbu, K. R., Chhetri, R. B., Oh, Y. S., Oak, M., Beak, D. J., & Park, E. (2025) · Toxicological Research · doi:10.1007/s43188-025-00301-3 · Cited by 6 · see citing works

Revealing the Oxidative Stress-Related Molecular Characteristics and Potential Therapeutic Targets of Schizophrenia through Integrated Gene Expression Data Analysis

Zhu, X., Chen, X., Ba, H., Yang, C., Liu, J., Guo, R., Li, S., Huang, P., Li, C., & Zhang, S. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04924-3 · Cited by 4 · see citing works

Reactive Oxygen Species in Neurodegenerative Disorders

Sharma, A., Tiwari, S., Sharma, H., Pathak, R., & Khan, F. (2025) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/979-8-3693-7919-6.ch012 · Cited by 4 · see citing works

Exploration of Lycorine and Copper(II)’s Association with the N-Terminal Domain of Amyloid β

Kola, A., Vigni, G., & Valensin, D. (2023) · Inorganics · doi:10.3390/inorganics11110443 · Cited by 2 · see citing works

Value-addition of pummelo (Citrus grandis) Peel- A Review

Sowmya, A., & Lakshmi, D. M. (2023) · The Pharma Innovation · doi:10.22271/tpi.2023.v12.i2a.18645 · Cited by 1 · see citing works

Post-translational Modifications of the p53 Protein and the Impact in Alzheimer’s Disease: A Review of the LiteraturePreprint

Clark, J., Piccirella, S., Kayed, R., Abate, G., Uberti, D. L., & Kinnon, P. (2021) · Preprints.org · doi:10.20944/preprints202109.0359.v1 · Cited by 1 · see citing works

How the Disruption of Mitochondrial Redox Signalling Contributes to Ageing

Castejón‐Vega, B., Cordero, M. D., & Sanz, A. (2023) · Antioxidants · doi:10.3390/antiox12040831 · Cited by 30 · see citing works

Age-Related Oxidative Stress-Induced Redox Imbalance

Tan, B. L., & Norhaizan, M. E. (2021) · Springer eBooks · doi:10.1007/978-3-030-82859-2_3 · Cited by 3 · see citing works

Insights into Mitochondrial Dysfunction: Aging, Amyloid-β, and Tau–A Deleterious Trio

Schmitt, K., Grimm, A., Wilkaniec, A., Strosznajder, J. B., Götz, J., & Eckert, A. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4400 · Cited by 132 · see citing works

Mitochondria and Reactive Oxygen Species in Aging and Age-Related Diseases

Giorgi, C., Marchi, S., Simões, I. C. M., Ren, Z., Morciano, G., Perrone, M., Patalas‐Krawczyk, P., Borchard, S., Jędrak, P., Pierzynowska, K., et al. (2018) · International review of cytology · doi:10.1016/bs.ircmb.2018.05.006 · Cited by 467 · see citing works

The Many Roles Mitochondria Play in Mammalian Aging

Batalha, C. M. P. F., Vercesi, A. E., & de Souza-Pinto, N. C. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0074 · Cited by 8 · see citing works