The DOI matches its Crossref record; 81 of the 81 references it cites were found in a registry or an index.
Forkhead Box O as a Sensor, Mediator, and Regulator of Redox Signaling
Abstract
The forkhead box O (FOXO) family of transcription factors regulates a variety of cellular programs, including cell cycle arrest, reactive oxygen species (ROS) scavenging, and apoptosis, and are of key importance in the decision over cell fate. In animal model systems it has been shown that FOXO is involved in the regulation of long lifespan. FOXO activity is tightly controlled by the insulin signaling pathway and by a multitude of ROS-induced posttranslational modifications. In the cell, ROS levels can be sensed by virtue of stimulatory and inhibitory oxidative modification of cysteine residues within proteins that control various signaling cascades. Recently, it was shown that cysteines in FOXO can also act as sensors of the local redox state. In this review we have outlined the cysteine-dependent redox switches that regulate both the insulin and ROS signaling pathways upstream of FOXO. Further, we describe how FOXO controls ROS levels by transcriptional regulation of a multilayered antioxidant system. Finally, we will discuss how cysteine-based redox signaling to FOXO could play a role in fine-tuning the optimal cellular response to ROS to control organismal lifespan. Antioxid. Redox Signal. 14, 1093–1106.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Various kinases and transcription factors, involved in neuropeptide regulation, have been reported to be modulated by redox signaling ([33](#B33), [91](#B91)).”
From Mitochondrial fatty acid oxidation in obesity (2013) · cites this paper as [33]
Citations
Cites
Aging: a theory based on free radical and radiation chemistry
Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567
Akt Promotes Cell Survival by Phosphorylating and Inhibiting a Forkhead Transcription Factor
Brunet, A., Bonni, A., Zigmond, M. J., Lin, M. Z., Juo, P., Hu, L. S., Anderson, M. J., Arden, K. C., Blenis, J., & Greenberg, M. E. (1999) · Cell · doi:10.1016/s0092-8674(00)80595-4 · Cited by 5,594
Mitochondrial formation of reactive oxygen species
Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
A C. elegans mutant that lives twice as long as wild type
Kenyon, C., Chang, J., Gensch, E., Rudner, A., & Tabtiang, R. (1993) · Nature · doi:10.1038/366461a0 · Cited by 3,387
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
Maehama, T., & Dixon, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13375 · Cited by 3,104
Genes that act downstream of DAF-16 to influence the lifespan of Caenorhabditis elegans
Murphy, C. T., McCarroll, S. A., Bargmann, C. I., Fraser, A., Kamath, R. S., Ahringer, J., Li, H., & Kenyon, C. (2003) · Nature · doi:10.1038/nature01789 · Cited by 2,280
Bjelakovic, G., Nikolova, D., Gluud, L. L., Simonetti, R. G., & Gluud, C. (2007) · JAMA · doi:10.1001/jama.297.8.842 · Cited by 2,275
Elchebly, M., Payette, P., Michaliszyn, E., Cromlish, W., Collins, S., Loy, A. L., Normandin, D., Cheng, A., Himms-Hagen, J., Chan, C.-C., et al. (1999) · Science · doi:10.1126/science.283.5407.1544 · Cited by 2,210
Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
Burgering, B. M. T., & Coffer, P. J. (1995) · Nature · doi:10.1038/376599a0 · Cited by 2,076
Self-citation
Cited by
Sorted by citations
Signal transduction by reactive oxygen species
Finkel, T. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201102095 · Cited by 2,322
Cellular mechanisms and physiological consequences of redox-dependent signalling
Holmström, K. M., & Finkel, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3801 · Cited by 2,093
Beyond oxidative stress: an immunologist's guide to reactive oxygen species
Nathan, C., & Cunningham-Bussel, A. (2013) · Nature Reviews Immunology · doi:10.1038/nri3423 · Cited by 1,619
Baar, M. P., Brandt, R. M. C., Putavet, D. A., Klein, J. D. D., Derks, K. W. J., Bourgeois, B. R. M., Stryeck, S., Rijksen, Y., van Willigenburg, H., Feijtel, D. A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.02.031 · Cited by 1,454
Iron homeostasis and oxidative stress: An intimate relationship
Galaris, D., Barbouti, A., & Pantopoulos, K. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118535 · Cited by 960
Basic Principles and Emerging Concepts in the Redox Control of Transcription Factors
Brigelius‐Flohé, R., & Flohé, L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3534 · Cited by 590
The redox stress hypothesis of aging
Sohal, R. S., & Orr, W. C. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.445 · Cited by 473
SIRT3 regulation of mitochondrial oxidative stress
Bause, A. S., & Haigis, M. C. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2012.08.007 · Cited by 311
Redox homeostasis: the linchpin in stem cell self-renewal and differentiation
Wang, K., Zhang, T., Dong, Q. G., Nice, E. C., Huang, C., & Wei, Y. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.50 · Cited by 298
FoxO proteins restrain osteoclastogenesis and bone resorption by attenuating H2O2 accumulation
Bartell, S. M., Kim, H., Ambrogini, E., Li, H., Iyer, S. V., Ucer, S., Rabinovitch, P. S., Jilka, R. L., Weinstein, R. S., Zhao, H., et al. (2014) · Nature Communications · doi:10.1038/ncomms4773 · Cited by 272
Mitochondrial fatty acid oxidation in obesity
Serra, D., Mera, P., Malandrino, M. I., Mir, J. F., & Herrero, L. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4875 · Cited by 246
Lee, R., Margaritis, M., Channon, K. M., & Antoniades, C. A. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712800493057 · Cited by 233
PTEN in cancer, metabolism, and aging
Ortega-Molina, A., & Serrano, M. (2012) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2012.11.002 · Cited by 207
Brocca, L., Cannavino, J., Coletto, L., Biolo, G., Sandri, M., Bottinelli, R., & Pellegrino, M. A. (2012) · The Journal of Physiology · doi:10.1113/jphysiol.2012.240267 · Cited by 199
Role of Forkhead Transcription Factors in Diabetes-Induced Oxidative Stress
Ponugoti, B., Dong, G., & Graves, D. T. (2012) · Experimental Diabetes Research · doi:10.1155/2012/939751 · Cited by 196
Huang, Z., Zhang, Z., Zhou, C., Liu, L., & Huang, C. (2022) · MedComm · doi:10.1002/mco2.144 · Cited by 179
Redox-Dependent Control of FOXO/DAF-16 by Transportin-1
Putker, M., Madl, T., Vos, H. R., de Ruiter, H., Visscher, M., van den Berg, M. C. W., Kaplan, M., Korswagen, H. C., Boelens, R., Vermeulen, M., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.014 · Cited by 167
Self-citationFOXOs and Sirtuins in Vascular Growth, Maintenance, and Aging
Oellerich, M. F., & Potente, M. (2012) · Circulation Research · doi:10.1161/circresaha.111.246488 · Cited by 161
Dysfunction of Cerebrovascular Endothelial Cells: Prelude to Vascular Dementia
Wang, F., Cao, Y., Ma, L., Pei, H., Rausch, W., & Li, H. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00376 · Cited by 163
Biological Significance of the Importin‐β Family‐Dependent Nucleocytoplasmic Transport Pathways
Kimura, M., & Imamoto, N. (2014) · Traffic · doi:10.1111/tra.12174 · Cited by 150
Cell Survival and Apoptosis Signaling as Therapeutic Target for Cancer: Marine Bioactive Compounds
Kalimuthu, S., & Kim, S. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14022334 · Cited by 145
Reactive oxygen species extend insect life span using components of the insulin-signaling pathway
Zhang, X., Wang, T., Lin, X.-W., Denlinger, D. L., & Xu, W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711042114 · Cited by 135
Reactive Oxygen Species: Physiological Roles in the Regulation of Vascular Cells
Vara, D. S., & Pula, G. (2014) · Current Molecular Medicine · doi:10.2174/1566524014666140603114010 · Cited by 135
The Fountain of Youth by Targeting Senescent Cells?
de Keizer, P. L. J. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.11.006 · Cited by 127
Reciprocal Control of the Circadian Clock and Cellular Redox State - a Critical Appraisal
Putker, M., & O'Neill, J. S. (2016) · Molecules and Cells · doi:10.14348/molcells.2016.2323 · Cited by 94
Redox signaling in the pancreas in health and disease
Sastre, J., Pérez, S., Sabater-Orti, L., & Rius‐Pérez, S. (2024) · Physiological Reviews · doi:10.1152/physrev.00044.2023 · Cited by 101
Emerging role of SIRT3 in mitochondrial dysfunction and cardiovascular diseases
Wu, J., Zeng, Z., Zhang, W., Deng, Z., Wan, Y., Zhang, Y., An, S. L., Huang, Q., & Chen, Z. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1549732 · Cited by 83
Unraveling the role of FoxOs in bone—Insights from mouse models
Almeida, M. (2011) · Bone · doi:10.1016/j.bone.2011.05.023 · Cited by 85
Novel insights into redox system and the mechanism of redox regulation
Wang, X., & Hai, C. (2016) · Molecular Biology Reports · doi:10.1007/s11033-016-4022-y · Cited by 84
Ye, S., Lowther, S., & Stambas, J. (2014) · Journal of Virology · doi:10.1128/jvi.03529-14 · Cited by 78
Lin, C., Huang, W., Li, H., Huang, C., Hsieh, S., Lai, C., & Lu, F. (2015) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2015.07.013 · Cited by 75
The role of reactive oxygen species in bone cell physiology and pathophysiology
Marques-Carvalho, A., Kim, H., & Almeida, M. (2023) · Bone Reports · doi:10.1016/j.bonr.2023.101664 · Cited by 80
Cordeiro, L. M., Machado, M. L., da Silva, A. F., Baptista, F. B. O., da Silveira, T. L., Soares, F. A. A., & Arantes, L. P. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111323 · Cited by 72
A Peroxidase Peroxiredoxin 1-Specific Redox Regulation of the Novel FOXO3 microRNA Target let-7
Hopkins, B., Nadler, M. J. S., Skoko, J., Bertomeu, T., Pelosi, A., Mousavi-Shafaei, P., Levine, K. M., Schempf, A. M., Pennarun, B., Yang, B., et al. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6871 · Cited by 67
Senolytic targets and new strategies for clearing senescent cells
Ge, M., Hu, L., Ao, H.-S., Zi, M., Kong, Q., & He, Y. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111468 · Cited by 64
Resveratrol prevents osteoporosis by upregulating FoxO1 transcriptional activity
Feng, Y., Jiang, X., Ma, F.-F., Han, J., & Tang, X. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3208 · Cited by 62
Wu, R., Sun, Y., Zhou, T., Zhu, Z.-Y., Zhuang, J., Tang, X., Chen, J., Hu, L., & Shen, X. (2014) · Acta Pharmacologica Sinica · doi:10.1038/aps.2014.70 · Cited by 60
Wang, X., & Hai, C. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.07.012 · Cited by 59
Involvement of Redox State in the Aging of Drosophila melanogaster
Orr, W. C., Radyuk, S. N., & Sohal, R. S. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5002 · Cited by 55
Li, Y., Guo, Y. C., Xi, M., Yang, P., Zhou, X., Yin, S., Hai, C., Li, J., & Qin, X.-J. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/320513 · Cited by 55
Siendones, E., Calvo, S. S.-C., Martín‐Montalvo, A., Cascajo, M. V., Ariza, J., López‐Lluch, G., Villalba, J. M., Acquaviva, C., Roze, E. F., Bernier, M., et al. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5479 · Cited by 55
Wei, Y., Wang, L., Wang, D., Wang, D., Wen, C., Han, B., & Ouyang, Z. (2018) · Chinese Medicine · doi:10.1186/s13020-018-0205-x · Cited by 54
Redox Homeostasis in Pancreatic β-Cells: From Development to Failure
Benáková, Š., Holendová, B., & Plecitá‐Hlavatá, L. (2021) · Antioxidants · doi:10.3390/antiox10040526 · Cited by 57
Gómez-Crisóstomo, N. P., Rodrı́guez-Martı́nez, E., & Rivas-Arancibia, S. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/805764 · Cited by 52
Kim, S., Grenert, J. P., Patterson, C., & Correia, M. A. (2016) · Scientific Reports · doi:10.1038/srep29423 · Cited by 51
Kwon, D., Kim, S., & Correia, M. A. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.11.002 · Cited by 53
FoxO3a Is an Antimelanogenic Factor that Mediates Antioxidant-Induced Depigmentation
Kim, J., Choi, H., Cho, E., & Lee, T. R. (2013) · Journal of Investigative Dermatology · doi:10.1038/jid.2013.510 · Cited by 47
Redox Molecular Machines Involved in Tumor Progression
Parri, M., & Chiarugi, P. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5040 · Cited by 47
The role of mitochondrial reactive oxygen species in insulin resistance
Ayer, A., Fazakerley, D. J., James, D. E., & Stocker, R. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.11.007 · Cited by 50
The c10orf10 gene product is a new link between oxidative stress and autophagy
Stepp, M. W., Folz, R. J., Yu, J., & Zelko, I. N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.02.003 · Cited by 45
Novel role of forkhead box O 4 transcription factor in cancer: Bringing out the good or the bad
Jiang, S., Yang, Z. P., Di, S., Hu, W., Ma, Z., Chen, F., & Yang, Y. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.04.007 · Cited by 47
Barger, J. L., Kayo, T., Pugh, T. D., Vann, J. M., Power, R. F., Dawson, K. A., Weindruch, R. H., & Prolla, T. A. (2011) · Genes & Nutrition · doi:10.1007/s12263-011-0243-9 · Cited by 45
Maghsoudi, A. S., Hassani, S., Momtaz, S., Shadboorestan, A., Ganjali, M. R., Ghahremani, M. H., Hosseini, R., Norouzi, P., & Abdollahi, M. R. (2018) · Toxicology · doi:10.1016/j.tox.2018.10.014 · Cited by 45
Noncoding RNA Regulation of Dormant States in Evolutionarily Diverse Animals
Reynolds, J. A. (2019) · Biological Bulletin · doi:10.1086/705484 · Cited by 40
A potential link of oxidative stress and cell cycle regulation for development of endometriosis
Shigetomi, H., Higashiura, Y., Kajihara, H., & Kobayashi, H. (2012) · Gynecological Endocrinology · doi:10.3109/09513590.2012.683071 · Cited by 40
Ansong, C. K., Sadler, N., Hill, E. A., Lewis, M. P., Zink, E., Smith, R. D., Beliaev, A. S., Konopka, A. E., & Wright, A. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00325 · Cited by 40
FoxOs: Unifying Links Between Oxidative Stress and Skeletal Homeostasis
Kousteni, S. (2011) · Current Osteoporosis Reports · doi:10.1007/s11914-011-0054-3 · Cited by 42
FoxO induces pupal diapause by decreasing TGFβ signaling
Zhang, X.-S., Wang, Z.-H., Li, W., & Xu, W. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210404119 · Cited by 39
Romero-Aristizabal, C., Marks, D. S., Fontana, W., & Apfeld, J. (2014) · Nature Communications · doi:10.1038/ncomms6020 · Cited by 39
Mitochondrial and postmitochondrial survival signaling in cancer
Yadav, N., & Chandra, D. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.11.005 · Cited by 39
Protein Promiscuity in H 2 O 2 Signaling
Young, D., Pedre, B., Ezeriņa, D., Smet, B. D., Lewandowska, A., Tossounian, M., Bodra, N., Huang, J., Rosado, L. A., Breusegem, F. V., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7013 · Cited by 39
Nuclear FOXO3 predicts adverse clinical outcome and promotes tumor angiogenesis in neuroblastoma
Hagenbuchner, J., Rupp, M., Salvador, C., Meister, B., Kiechl‐Kohlendorfer, U., Müller, T., Geiger, K., Sergi, C. M., Obexer, P., & Ausserlechner, M. J. (2016) · Oncotarget · doi:10.18632/oncotarget.12728 · Cited by 39
Targeting Reactive Oxygen Species Metabolism to Induce Myeloma Cell Death
Caillot, M., Dakik, H., Mazurier, F., & Sola, B. (2021) · Cancers · doi:10.3390/cancers13102411 · Cited by 37
Oxidative stress reduces trophoblast FOXO1 and integrin β3 expression that inhibits cell motility
Chen, C., Chen, C.-Y., Wu, Y., & Chen, C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.06.006 · Cited by 37
Oli, V., Gupta, R. V., & Kumar, P. (2021) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2021.102012 · Cited by 36
HDAC2 regulates FoxO1 during RANKL-induced osteoclastogenesis
Dou, C., Li, N., Ding, N., Liu, C., Yang, X., Kang, F., Cao, Z., Quan, H., Hou, T., Xu, J., et al. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00351.2015 · Cited by 36
van den Berg, M. C. W., Gogh, I. J. A. E., de Vries-Smits, A. M. M., van Triest, M. H., Dansen, T. B., Visscher, M., Polderman, P. E., Vliem, M. J., Rehmann, H., & Burgering, B. M. T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463885 · Cited by 36
Self-citationCappelli, A. P. G., Zoppi, C. C., Barbosa, H., Costa, J. M., Protzek, A. O. P., Morato, P. N., Boschero, A. C., & Carneiro, E. M. (2013) · Liver International · doi:10.1111/liv.12291 · Cited by 33
FOXO3-mediated chemo-protection in high-stage neuroblastoma depends on wild-type TP53 and SESN3
Rupp, M., Hagenbuchner, J., Rass, B., Fiegl, H., Kiechl‐Kohlendorfer, U., Obexer, P., & Ausserlechner, M. J. (2017) · Oncogene · doi:10.1038/onc.2017.288 · Cited by 32
Bai, H., Fang, C., Shi, Y., Zhai, S., Jiang, A., Li, Y.-N., Wang, L., Liu, Q., Zhou, G., Cao, J.-H., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05744-w · Cited by 33
Hydrogen peroxide induced tendinopathic changes in a rat model of patellar tendon injury
Fu, S., Yeung, M. Y., Rolf, C. G., Yung, P. S., Chan, K., & Hung, L. (2018) · Journal of Orthopaedic Research® · doi:10.1002/jor.24119 · Cited by 32
The FOXO signaling axis displays conjoined functions in redox homeostasis and stemness
Soh, R., Hardy, A., & Nieden, N. I. Z. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.04.022 · Cited by 33
The Peroxide Dilemma: Opposing and Mediating Insulin Action
Szypowska, A. A., & Burgering, B. M. T. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3794 · Cited by 33
Self-citationShifting the balance of mitochondrial apoptosis: therapeutic perspectives
Fulda, S. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00121 · Cited by 31
A Protocol for Quantifying Lipid Peroxidation in Cellular Systems by F2-Isoprostane Analysis
Labuschagne, C. F., van den Broek, N. J. F., Postma, P., Berger, R., & Brenkman, A. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080935 · Cited by 30
The circadian clock in adult neural stem cell maintenance
Draijer, S., Chaves, I., & Hoekman, M. F. M. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.05.007 · Cited by 31
van den Berg, M. C. W., Gogh, I. J. A. E., de Vries-Smits, A. M. M., van Triest, M. H., Dansen, T. B., Visscher, M., Polderman, P. E., Vliem, M. J., Rehmann, H., & Burgering, B. M. T. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.a113.463885 · Cited by 29
Self-citationSang, T., Cao, Q., Wang, Y., Liu, F., & Chen, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0101703 · Cited by 25
Lin, C.-H., Lee, H., Chang, W., Lee, F., Chen, L.-C., Lu, L., & Lin, Y. (2020) · Cancers · doi:10.3390/cancers12092690 · Cited by 24
FoxO4 inhibits atherosclerosis through its function in bone marrow derived cells
Zhu, M., Zhang, Q.-J., Wang, L., Li, H., & Liu, Z.-P. (2011) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2011.09.038 · Cited by 24
Intermolecular disulfide-dependent redox signalling
Putker, M., Vos, H. R., & Dansen, T. B. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140097 · Cited by 24
Self-citationParacrine Mechanisms of Redox Signalling for Postmitotic Cell and Tissue Regeneration
Hervera, A., Santos, C. X. C., Virgiliis, F. D., Shah, A. M., & Giovanni, S. D. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.01.006 · Cited by 24
Proteomic Characterization of Reversible Thiol Oxidations in Proteomes and Proteins
Boronat, S., Domènech, A., & Hidalgo, E. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6720 · Cited by 21
Opportunities and challenges for the development of covalent chemical immunomodulators
Backus, K. M., Cao, J. X., & Maddox, S. M. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.05.050 · Cited by 21
Modulating FOXO3 transcriptional activity by small, DBD-binding molecules
Hagenbuchner, J., Obšilová, V., Kaserer, T., Kaiser, N., Rass, B., Pšenáková, K., Dočekal, V., Alblova, M., Kohoutová, K., Schuster, D., et al. (2019) · eLife · doi:10.7554/elife.48876 · Cited by 20
Raju, I., Kannan, K., & Abraham, E. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067126 · Cited by 21
Zhang, H., Lin, X., Yang, B., Zhang, L., & Liu, Z. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c02495 · Cited by 20
Zhang, L., Liu, X., Huang, M., Wang, R., Zhu, W., Li, Y., Shen, L., & Li, C. (2022) · Clinical Cosmetic and Investigational Dermatology · doi:10.2147/ccid.s368845 · Cited by 19
Challenges facing nanotoxicology and nanomedicine due to cellular diversity
Akhtar, M. J., Ahamed, M., & Alhadlaq, H. A. (2018) · Clinica Chimica Acta · doi:10.1016/j.cca.2018.10.004 · Cited by 19
Mehri, F., Ranjbar, A., Shirafkan, N., Asl, S. S., & Esfahani, M. (2022) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23063 · Cited by 19
Perrelli, A., Ferraris, C., Berni, E., Glading, A., & Retta, S. F. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0263 · Cited by 17
Jindal, E., & Goswami, S. K. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.07.008 · Cited by 18
Ma, X., Tian, Y. E., Xue, K., Huai, Y., Patil, S., Deng, X., Hao, Q., Li, D., Miao, Z., Zhang, W., et al. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174555 · Cited by 16
Li, H., Li, W., Li, J., Li, S., Kuang, L., Pang, F., Jiang, H., Jin, H., & Bian, X. (2022) · Cells · doi:10.3390/cells11223562 · Cited by 15
Wen, X., Feng, K., Peng, W., Li, J., Li, M., Dou, W., Guo, Z., Zhang, Y., & He, L. (2025) · Communications Biology · doi:10.1038/s42003-025-08726-0 · Cited by 13
Modaghegh, M. H. S., Saberianpour, S., Amoueian, S., Shahri, J. J., & Rahimi, H. R. (2021) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2021.101025 · Cited by 13
Hwang, C. Y., Lee, S.-M., Park, S. S., & Kwon, K. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.07.059 · Cited by 13
Ghandadi, M., Behravan, J., Abnous, K., & Mosaffa, F. (2015) · Oncology Research and Treatment · doi:10.1159/000442144 · Cited by 13
Effects of Vitamin C on Cytotherapy-Mediated Muscle Regeneration
Kim, A.-Y., Lee, E. M., Lee, E. H., Min, C., Kang, K., Park, J., Hong, I., Ishigami, A., Tremblay, J. P., & Jeong, K. (2013) · Cell Transplantation · doi:10.3727/096368912x657846 · Cited by 12
Resveratrol: a panacea compound for diazinon-induced renal toxicity
Esfahani, M., Rahbar, A. H., Asl, S. S., & Mehri, F. (2021) · Toxin Reviews · doi:10.1080/15569543.2021.2008452 · Cited by 11
Metadata
- Authors
- de Keizer, P. L. J., Burgering, B. M. T., & Dansen, T. B.
- Affiliations
- University Medical Center Utrecht
- University Medical Center Utrecht (NL)
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2011-03
- Volume
- 14
- Issue
- 6
- Pages
- 1093-1106
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W1986717393
- Cited by
- 131
- References
- 80
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 3 · 2023: 7 · 2022: 10 · 2021: 11 · 2020: 3 · 2019: 7 · 2018: 13 · 2017: 6 · 2016: 8 · 2015: 5 · 2014: 14 · 2013: 15 · 2012: 13
- FWCI
- 1.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › FOXO transcription factor regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- FOXO transcription factors, forkhead box O, redox signaling, reactive oxygen species, insulin signaling, lifespan regulation, oxidative stress, apoptosis, cell cycle arrest
- MeSH terms
- Animals, Cysteine, Humans, Models, Biological, Oxidation-Reduction, Signal Transduction, Reactive Oxygen Species, Forkhead Transcription Factors
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