The DOI matches its Crossref record; 24 of the 25 references it cites were found in a registry or an index.
Increased Oxidative Stress in the Nucleus Caused by Nox4 Mediates Oxidation of HDAC4 and Cardiac Hypertrophy
Open accessAbstract
Rationale: Oxidation of cysteine residues in class II histone deacetylases (HDACs), including HDAC4, causes nuclear exit, thereby inducing cardiac hypertrophy. The cellular source of reactive oxygen species responsible for oxidation of HDAC4 remains unknown. Objective: We investigated whether nicotinamide adenine dinucleotide phosphate oxidase 4 (Nox4), a major nicotinamide adenine dinucleotide phosphate oxidase, mediates cysteine oxidation of HDAC4. Methods and Results: Phenylephrine (100 μmol/L), an α1 adrenergic agonist, induced upregulation of Nox4 (1.5-fold; P <0.05) within 5 minutes, accompanied by increases in O 2 − (3.5-fold; P <0.01) from the nuclear membrane and nuclear exit of HDAC4 in cardiomyocytes. Knockdown of Nox4, but not Nox2, attenuated O 2 − production in the nucleus and prevented phenylephrine-induced oxidation and nuclear exit of HDAC4. After continuous infusion of phenylephrine (20 mg/kg per day) for 14 days, wild-type and cardiac-specific Nox4 knockout mice exhibited similar aortic pressures. Left ventricular weight/tibial length (5.7±0.2 versus 6.4±0.2 mg/mm; P <0.05) and cardiomyocytes cross-sectional area (223±13 versus 258±12 μm 2 ; P <0.05) were significantly smaller in cardiac-specific Nox4 knockout than in wild-type mice. Nuclear O 2 − production in the heart was significantly lower in cardiac-specific Nox4 knockout than in wild-type mice (4116±314 versus 7057±1710 relative light unit; P <0.05), and cysteine oxidation of HDAC4 was decreased. HDAC4 oxidation and cardiac hypertrophy were also attenuated in cardiac-specific Nox4 knockout mice 2 weeks after transverse aortic constriction. Conclusions: Nox4 plays an essential role in mediating cysteine oxidation and nuclear exit of HDAC4, thereby mediating cardiac hypertrophy in response to phenylephrine and pressure overload.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“ROS influence the activity of epigenetic modulators, such as histone deacetylases (HDACs) or DNA methyltransferases (DNMTs) with consequences that are evident in the expression of the target genes38,39.”
From ROS in cancer therapy: the bright side of the moon (2020) · cites this paper as [38]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
Oxidative stress and heart failure
Tsutsui, H., Kinugawa, S., & Matsushima, S. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00554.2011 · Cited by 1,277
Self-citationA Dynamic Pathway for Calcium-Independent Activation of CaMKII by Methionine Oxidation
Erickson, J. R., Joiner, M.-L. A., Guan, X., Kutschke, W., Yang, J., Oddis, C. V., Bartlett, R. K., Lowe, J. S., O'Donnell, S. E., Aykin-Burns, N., et al. (2008) · Cell · doi:10.1016/j.cell.2008.02.048 · Cited by 1,122
Functional analysis of Nox4 reveals unique characteristics compared to other NADPH oxidases
Martyn, K. D., Frederick, L. M., von Loehneysen, K., Dinauer, M. C., & Knaus, U. G. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.023 · Cited by 783
NADPH oxidase 4 (Nox4) is a major source of oxidative stress in the failing heart
Kuroda, J., Ago, T., Matsushima, S., Zhai, P., Schneider, M. D., & Sadoshima, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002178107 · Cited by 772
Self-citationSumimoto, H. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06488.x · Cited by 740
CaM kinase II selectively signals to histone deacetylase 4 during cardiomyocyte hypertrophy
Backs, J. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27438 · Cited by 514
Ago, T., Kuroda, J., Pain, J., Fu, C., Li, H., & Sadoshima, J. (2010) · Circulation Research · doi:10.1161/circresaha.109.213116 · Cited by 506
Self-citationZhang, M., Brewer, A. C., Schröder, K., Santos, C. X. C., Grieve, D., Wang, M., Anilkumar, N. P., Yu, B., Dong, X., Walker, S. J., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009700107 · Cited by 452
Control of Cardiac Growth by Histone Acetylation/Deacetylation
Backs, J., & Olson, E. N. (2006) · Circulation Research · doi:10.1161/01.res.0000197782.21444.8f · Cited by 440
Cited by
Sorted by citations
ROS in cancer therapy: the bright side of the moon
Perillo, B., Di Donato, M., Pezone, A., Di Zazzo, E., Giovannelli, P., Galasso, G., Castoria, G., & Migliaccio, A. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-0384-2 · Cited by 2,176
Kang, Q., & Yang, C. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101799 · Cited by 1,134
Nrf2 regulates ROS production by mitochondria and NADPH oxidase
Kovac, S., Angelova, P. R., Holmström, K. M., Zhang, Y., Dinkova‐Kostova, A. T., & Abramov, A. Y. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.11.021 · Cited by 621
NADPH oxidases and oxidase crosstalk in cardiovascular diseases: novel therapeutic targets
Zhang, Y., Murugesan, P., Huang, K., & Cai, H. “. (2019) · Nature Reviews Cardiology · doi:10.1038/s41569-019-0260-8 · Cited by 551
Mst1 inhibits autophagy by promoting the interaction between Beclin1 and Bcl-2
Maejima, Y., Kyoi, S., Zhai, P., Liu, T., Li, H., Ivessa, A., Sciarretta, S., Del Re, D. P., Zablocki, D. K., Hsu, C.-P., et al. (2013) · Nature Medicine · doi:10.1038/nm.3322 · Cited by 499
Self-citationAging and Autophagy in the Heart
Shirakabe, A., Ikeda, Y., Sciarretta, S., Zablocki, D., & Sadoshima, J. (2016) · Circulation Research · doi:10.1161/circresaha.116.307474 · Cited by 448
Self-citationSchirone, L., Forte, M., Palmerio, S., Yee, D., Nocella, C., Angelini, F., Pagano, F., Schiavon, S., Bordin, A., Carrizzo, A., et al. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/3920195 · Cited by 454
Oxidative stress alters global histone modification and DNA methylation
Niu, Y., DesMarais, T. L., Tong, Z., Yao, Y., & Costa, M. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.01.028 · Cited by 362
Oxidative stress and epigenetic modifications in the pathogenesis of diabetic retinopathy
Kowluru, R. A., Kowluru, A., Mishra, M., & Kumar, B. (2015) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2015.05.001 · Cited by 339
ROS signaling and ER stress in cardiovascular disease
Ochoa, C. D., Wu, R.-F., & Terada, L. (2018) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2018.03.002 · Cited by 286
Egea, J., Fabregat, I., Frapart, Y., Ghezzi, P., Görlach, A., Kietzmann, T., Kubaichuk, K. I., Knaus, U. G., López, M. G., González, G. O., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.05.007 · Cited by 321
Oxidative Stress and the Use of Antioxidants in Stroke
Shirley, R. B., Ord, E., & Work, L. M. (2014) · Antioxidants · doi:10.3390/antiox3030472 · Cited by 295
Oxidative Stress Signaling to Chromatin in Health and Disease
Kreuz, S., & Fischle, W. (2016) · Epigenomics · doi:10.2217/epi-2016-0002 · Cited by 265
Trehalose-Induced Activation of Autophagy Improves Cardiac Remodeling After Myocardial Infarction
Sciarretta, S., Yee, D., Nagarajan, N., Bianchi, F., Saito, T., Valenti, V., Tong, M., Re, D. P. D., Vecchione, C., Schirone, L., et al. (2018) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2018.02.066 · Cited by 249
Self-citationZhao, Q. D., Viswanadhapalli, S., Williams, P., Shi, Q., Tan, C., Yi, X., Bhandari, B., & Abboud, H. E. (2015) · Circulation · doi:10.1161/circulationaha.114.011079 · Cited by 248
HDAC4: Mechanism of Regulation and Biological Functions
Wang, Z., Qin, G., & Zhao, T. C. (2014) · Epigenomics · doi:10.2217/epi.13.73 · Cited by 239
Oxidative Stress and Huntington’s Disease: The Good, the Bad, and the Ugly
Kumar, A., & Ratan, R. R. (2016) · Journal of Huntington s Disease · doi:10.3233/jhd-160205 · Cited by 236
Sciarretta, S., Zhai, P., Shao, D., Zablocki, D., Nagarajan, N., Terada, L. S., Volpe, M., & Sadoshima, J. (2013) · Circulation Research · doi:10.1161/circresaha.113.301787 · Cited by 201
Self-citationNox NADPH Oxidases and the Endoplasmic Reticulum
Laurindo, F. R. M., Araujo, T. L. S., & Abrahão, T. B. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5605 · Cited by 194
Varga, Z. V., Kupai, K., Szűcs, G., Gáspár, R., Pálóczi, J., Faragó, N., Zvara, Á., Puskás, L. G., Rázga, Z., Tiszlavicz, L., et al. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.05.009 · Cited by 174
Novel aspects of ROS signalling in heart failure
Hafstad, A. D., Nabeebaccus, A., & Shah, A. M. (2013) · Basic Research in Cardiology · doi:10.1007/s00395-013-0359-8 · Cited by 171
Bürli, R. W., Luckhurst, C. A., Aziz, O., Matthews, K. L., Yates, D., Lyons, K. A., Beconi, M., McAllister, G., Breccia, P., Stott, A. J., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4011884 · Cited by 153
Mitochondrial Dysfunction and Therapeutic Perspectives in Cardiovascular Diseases
Liu, Y., Huang, Y., Xu, C. B., An, P., Luo, Y., Jiao, L., Luo, J., & Li, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232416053 · Cited by 151
Nox4 and diabetic nephropathy: With a friend like this, who needs enemies?
Gorin, Y. C., & Block, K. L. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.03.014 · Cited by 136
Physiological and pathological functions of NADPH oxidases during myocardial ischemia–reperfusion
Matsushima, S., Tsutsui, H., & Sadoshima, J. (2014) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2014.03.003 · Cited by 132
Self-citationZhao, H., Zhang, M., Zhou, F., Cao, W., Bi, L., Xie, Y., Yang, Q., & Wang, S. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.10.017 · Cited by 124
Reactive oxygen species in haematopoiesis: leukaemic cells take a walk on the wild side
Prieto-Bermejo, R., Romo-González, M., Pérez‐Fernández, A., Ijurko, C., & Hernández‐Hernández, Á. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0797-0 · Cited by 126
Dysregulation of Histone Acetyltransferases and Deacetylases in Cardiovascular Diseases
Wang, Y., Miao, X., Liu, Y., Li, F., Liu, Q., Sun, J., & Cai, L. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/641979 · Cited by 119
Manea, S., Constantin, A. L., Manda, G., Sasson, S., & Manea, A. (2015) · Redox Biology · doi:10.1016/j.redox.2015.06.012 · Cited by 119
The mitochondrial-targeted peptide, SS-31, improves glomerular architecture in mice of advanced age
Sweetwyne, M. T., Pippin, J. W., Eng, D. G., Hudkins, K. L., Chiao, Y. A., Campbell, M. D., Marcinek, D. J., Alpers, C. E., Szeto, H. H., Rabinovitch, P. S., et al. (2017) · Kidney International · doi:10.1016/j.kint.2016.10.036 · Cited by 110
Mielcarek, M., Zielonka, D., Carnemolla, A., Marcinkowski, T., & Guidez, F. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00042 · Cited by 111
Monji, A., Mitsui, T., Bando, Y., Aoyama, M., Shigeta, T., & Murohara, T. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00990.2012 · Cited by 108
Stanicka, J., Russell, E. G., Woolley, J. F., & Cotter, T. G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510495 · Cited by 101
Recent Developments in Heart Failure
Dassanayaka, S., & Jones, S. P. (2015) · Circulation Research · doi:10.1161/circresaha.115.305765 · Cited by 103
Redox-mediated signal transduction by cardiovascular Nox NADPH oxidases
Brandes, R. P., Weißmann, N., & Schröder, K. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.02.006 · Cited by 94
Redox stress in Marfan syndrome: Dissecting the role of the NADPH oxidase NOX4 in aortic aneurysm
Jiménez‐Altayó, F., Meirelles, T., Crosas‐Molist, E., Sorolla, M. A., del Blanco, D. G., López‐Luque, J., Mas‐Stachurska, A., Siegert, A.-M., Bonorino, F., Barberà, L., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.02.023 · Cited by 90
Targeting Mitochondrial Calcium Handling and Reactive Oxygen Species in Heart Failure
Dietl, A., & Maack, C. (2017) · Current Heart Failure Reports · doi:10.1007/s11897-017-0347-7 · Cited by 89
Tyrosine kinase FYN negatively regulates NOX4 in cardiac remodeling
Matsushima, S., Kuroda, J., Zhai, P., Liu, T., Ikeda, S., Nagarajan, N., Oka, S., Yokota, T., Kinugawa, S., Hsu, C., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci85624 · Cited by 84
Self-citationOn the epigenetic role of guanosine oxidation
Giorgio, M., Dellino, G. I., Gambino, V., Roda, N., & Pelicci, P. G. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101398 · Cited by 82
Cytosolic Accumulation of Small Nucleolar RNAs (snoRNAs) Is Dynamically Regulated by NADPH Oxidase
Holley, C. L., Li, M. W., Scruggs, B. S., Matkovich, S. J., Ory, D. S., & Schaffer, J. E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.637413 · Cited by 81
Epigenetics: a new mechanism of regulation of heart failure?
Papait, R., Greco, C. M., Kunderfranco, P., Latronico, M. V. G., & Condorelli, G. (2013) · Basic Research in Cardiology · doi:10.1007/s00395-013-0361-1 · Cited by 78
Zawada, W. M., Mrak, R. E., Biedermann, J., Palmer, Q. D., Gentleman, S. M., Aboud, O., & Griffin, W. S. T. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0189-z · Cited by 78
Rac1-Mediated Activation of Mineralocorticoid Receptor in Pressure Overload–Induced Cardiac Injury
Ayuzawa, N., Nagase, M., Ueda, K., Nishimoto, M., Kawarazaki, W., Marumo, T., Aiba, A., Sakurai, T., Shindo, T., & Fujita, T. (2015) · Hypertension · doi:10.1161/hypertensionaha.115.06054 · Cited by 77
Mitochondria and Cardiac Hypertrophy.
Facundo, H. D. T. F., Brainard, R. E., Caldas, F. R. D. L., & Lucas, A. M. B. (2017) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-55330-6_11 · Cited by 70
Hendrix, J., Nijs, J., Ickmans, K., Godderis, L., Ghosh, M., & Polli, A. (2020) · Antioxidants · doi:10.3390/antiox9111166 · Cited by 78
He, J., Li, X., Luo, H., Li, T., Zhao, L., Qi, Q., Liu, Y., & Yu, Z. (2017) · Journal of the American Society of Hypertension · doi:10.1016/j.jash.2017.03.008 · Cited by 70
Zhai, M., Liu, Z., Zhang, B., Jing, L., Li, B., Li, K., Chen, X., Zhang, M., Yu, B., Ren, K., et al. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12433 · Cited by 69
Saeedi Saravi, S. S., Pugin, B., Constancias, F., Shabanian, K., Spalinger, M., Thomas, A., Le Gludic, S., Shabanian, T., Karsai, G., Colucci, M., et al. (2025) · Nature Aging · doi:10.1038/s43587-025-00864-8 · Cited by 68
Weyemi, U., Redon, C. E., Aziz, T., Choudhuri, R., Maeda, D., Parekh, P. R., Bonner, M. Y., Arbiser, J. L., & Bonner, W. M. (2015) · Radiation Research · doi:10.1667/rr13799.1 · Cited by 70
Modulation of signaling mechanisms in the heart by thioredoxin 1
Nagarajan, N., Oka, S., & Sadoshima, J. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.020 · Cited by 69
Self-citationChristiansen, L. B., Dela, F., Koch, J., HANSEN, C. N., Leifsson, P. S., & Yokota, T. (2015) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00727.2014 · Cited by 67
Zhang, M., Mongue‐Din, H., Martin, D., Catibog, N., Smyrnias, I., Zhang, X., Yu, B., Wang, M., Brandes, R. P., Schröder, K., et al. (2017) · Cardiovascular Research · doi:10.1093/cvr/cvx204 · Cited by 67
Kang, J., Mun, D., Chun, Y., Park, D., Kim, H., Yun, N., & Joung, B. (2023) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12371 · Cited by 70
Ebenezer, D. L., Fu, P., Suryadevara, V., Zhao, Y., & Natarajan, V. (2016) · Advances in Biological Regulation · doi:10.1016/j.jbior.2016.09.007 · Cited by 66
NOX Inhibitors: From Bench to Naxibs to Bedside
Elbatreek, M. H., Mucke, H. A., & Schmidt, H. H. H. W. (2020) · Handbook of experimental pharmacology · doi:10.1007/164_2020_387 · Cited by 68
Kritzer, M. D., Li, J., Passariello, C. L., Gayanilo, M., Thakur, H. S., Dayan, J. E., Dodge‐Kafka, K. L., & Kapiloff, M. S. (2014) · Circulation Heart Failure · doi:10.1161/circheartfailure.114.001266 · Cited by 63
Fisetin inhibits cardiac hypertrophy by suppressing oxidative stress
Dong, B., Liu, C., Xue, R., Wang, Y., Sun, Y., Liang, Z., Fan, W., Jiang, J., Zhao, J., Su, Q., et al. (2018) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2018.08.010 · Cited by 62
Endothelial and vascular smooth muscle dysfunction in hypertension
de Oliveira, M. G., Nadruz, W., & Mónica, F. Z. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115263 · Cited by 64
A correlation between oxidative stress and diabetic retinopathy: An updated review
Hussain, A., Ashique, S., Afzal, O., Altamimi, M. A., Malik, A., Kumar, S., Garg, A., Sharma, N., Farid, A., Khan, T., et al. (2023) · Experimental Eye Research · doi:10.1016/j.exer.2023.109650 · Cited by 70
Potential Role of Epigenetic Mechanism in Manganese Induced Neurotoxicity
Tarale, P., Chakrabarti, T., Sivanesan, S., Naoghare, P. K., Bafana, A., & Krishnamurthi, K. (2016) · BioMed Research International · doi:10.1155/2016/2548792 · Cited by 63
Redox signaling in the cardiomyocyte: From physiology to failure
Santos, C. X. C., Raza, S., & Shah, A. M. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.03.002 · Cited by 54
NADPH Oxidases in Diastolic Dysfunction and Heart Failure with Preserved Ejection Fraction
Teuber, J. P., Essandoh, K., Hummel, S. L., Madamanchi, N. R., & Brody, M. J. (2022) · Antioxidants · doi:10.3390/antiox11091822 · Cited by 55
Singh, M. V., Cicha, M. Z., Meyerholz, D. K., Chapleau, M. W., & Abboud, F. M. (2015) · Hypertension · doi:10.1161/hypertensionaha.115.06011 · Cited by 50
Wang, B., Yang, Q., Bai, W., Xing, Y., Lu, X., Sun, Y., & Zhao, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098047 · Cited by 50
The role of Nox-mediated oxidation in the regulation of cytoskeletal dynamics
Valdivia, A., Duran, C., & Martín, A. S. (2015) · Current Pharmaceutical Design · doi:10.2174/1381612821666151029112624 · Cited by 51
HDAC5 catalytic activity suppresses cardiomyocyte oxidative stress and NRF2 target gene expression
Hu, T., Schreiter, F. C., Bagchi, R. A., Tatman, P. D., Hannink, M., & McKinsey, T. A. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007006 · Cited by 50
Lung Ischaemia–Reperfusion Injury: The Role of Reactive Oxygen Species
Pak, O., Sydykov, A. S., Kosanovic, D., SCHERMULY, R. T., Dietrich, A., Schröder, K., Brandes, R. P., Gudermann, T. W., Sommer, N., & Weißmann, N. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-63245-2_12 · Cited by 53
Fu, P., Ebenezer, D. L., Ha, A. W., Suryadevara, V., Harijith, A. K., & Natarajan, V. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26707 · Cited by 49
Yin and Yang of NADPH Oxidases in Myocardial Ischemia-Reperfusion
Matsushima, S., & Sadoshima, J. (2022) · Antioxidants · doi:10.3390/antiox11061069 · Cited by 47
Self-citationLi, H., Xu, C.-Q., Li, Q.-F., Gao, X.-X., Sugano, E., Tomita, H., Yang, L.-M., & Shi, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091958 · Cited by 40
NADPH oxidase 4 is a critical mediator in Ataxia telangiectasia disease
Weyemi, U., Redon, C. E., Aziz, T., Choudhuri, R., Maeda, D., Parekh, P. R., Bonner, M. Y., Arbiser, J. L., & Bonner, W. M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1418139112 · Cited by 47
Steinhorn, B. S., Sartoretto, J. L., Sorrentino, A., Romero, N., Kalwa, H., Abel, E. D., & Michel, T. M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.09.006 · Cited by 45
Okabe, K., Matsushima, S., Ikeda, S., Ikeda, M., Ishikita, A., Tadokoro, T., Enzan, N., Yamamoto, T., Sada, M., Deguchi, H., et al. (2020) · Hypertension · doi:10.1161/hypertensionaha.119.14400 · Cited by 44
Self-citationAlternative Splicing of NOX4 in the Failing Human Heart
Varga, Z. V., Pipicz, M., Baán, J. A., Baranyai, T., Koncsos, G., Leszek, P., Kuśmierczyk, M., Sánchez-Cabo, F., García-Pavía, P., Brenner, G. J., et al. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00935 · Cited by 43
Fibroblast growth factor 18 alleviates stress-induced pathological cardiac hypertrophy in male mice
Chen, G., An, N., Shen, J., Chen, H., Chen, Y., Sun, J. M., Hu, Z., Qiu, J., Jin, C., He, S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36895-1 · Cited by 43
Blasco, N., Cámara, Y., Núñez, E., Beà, A., Barés, G., Forné, C., Ruiz‐Meana, M., Girón, C., Barba, I., García‐Arumí, E., et al. (2018) · Redox Biology · doi:10.1016/j.redox.2018.02.021 · Cited by 43
Wright, L. H., & Menick, D. R. (2016) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00271.2016 · Cited by 42
Li, B., Chi, R., Qin, F., & Guo, X. (2016) · Experimental Physiology · doi:10.1113/ep085586 · Cited by 41
Mhatre, K. N., Wakula, P., Klein, O., Bisping, E. H., Voelkl, J. G. J., Pieske, B. M., & Heinzel, F. R. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2885-x · Cited by 41
Roles and post‐translational regulation of cardiac class IIa histone deacetylase isoforms
Weeks, K. L., & Avkiran, M. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.282442 · Cited by 40
Li, Y., He, B., Zhang, C., He, Y., Xia, T., & Zeng, C. (2023) · Nutrients · doi:10.3390/nu15061340 · Cited by 38
Epigenetics in cardiac development, function, and disease
Nührenberg, T. G., Gilsbach, R., Preißl, S., Schnick, T., & Hein, L. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1887-8 · Cited by 39
Tănase, D. M., Valasciuc, E., Gosav, E. M., Floria, M., Costea, C. F., Dima, N., Tudorancea, I., Maranducă, M. A., & Șerban, I. L. (2022) · Cells · doi:10.3390/cells11172663 · Cited by 37
Role of NADPH oxidase in the regulation of autophagy in cardiomyocytes
Sciarretta, S., Yee, D., Ammann, P. B., Nagarajan, N., Volpe, M., Frati, G., & Sadoshima, J. (2014) · Clinical Science · doi:10.1042/cs20140336 · Cited by 36
Self-citationHong, S., Hwang, H., Kim, J. W., Kim, J. A., Lee, Y., Roh, E., Choi, K. M., Baik, S. H., & Yoo, H. J. (2019) · Journal of Ginseng Research · doi:10.1016/j.jgr.2019.08.006 · Cited by 35
Tong, Q., Zhu, Y., Galaske, J. W., Kosmacek, E. A., Chatterjee, A., Dickinson, B. C., & Oberley‐Deegan, R. E. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.09.019 · Cited by 34
Angelini, F., Pagano, F., Bordin, A., Milan, M., Chimenti, I., Peruzzi, M., Valenti, V., Marullo, A. G. M., Schirone, L., Palmerio, S., et al. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/2712751 · Cited by 34
Nox4 genetic inhibition in experimental hypertension and metabolic syndrome
About, G. B., Ayme‐Dietrich, E., Jacob, H., Champy, M., Birling, M., Pavlovic, G., Madeira, L., Fertak, L. E., Petit‐Demoulière, B., Sorg, T., et al. (2017) · Archives of cardiovascular diseases · doi:10.1016/j.acvd.2017.03.011 · Cited by 33
Zeng, S., Yang, L., Lu, H., Yan, Q., Gao, L., & Qin, X. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14308 · Cited by 32
Role of CyPA in cardiac hypertrophy and remodeling
Cao, M., Yuan, W., Peng, M., Mao, Z., Zhao, Q., Sun, X., & Yan, J. (2019) · Bioscience Reports · doi:10.1042/bsr20193190 · Cited by 32
Yang, Y., Zhou, M., & Liu, H. (2021) · Physiology International · doi:10.1556/2060.2021.00148 · Cited by 32
NADPH Oxidase 4 Contributes to Myoblast Fusion and Skeletal Muscle Regeneration
Youm, T. H., Woo, S., Kwon, E., & Park, S. S. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/3585390 · Cited by 31
Wei, S., Ma, W., Jiang, C., Liu, J., Liu, J., Zhang, B., & Li, W. (2023) · Phytotherapy Research · doi:10.1002/ptr.7900 · Cited by 30
Design, synthesis, and biological evaluation of inhibitors of the NADPH oxidase, Nox4
Xu, Q., Kulkarni, A. A., Sajith, A. M., Hussein, D., Brown, D., Güner, O. F., Motati, D. R., Watkins, E. B., Lassegue, B. P., Griendling, K. K., et al. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.12.023 · Cited by 30
Oxidation of HDAC4 by Nox4-derived H2O2 maintains tube formation by endothelial cells
Schader, T., Löwe, O., Reschke, C., Malacarne, P. F., Hahner, F., Müller, N., Gajos‐Draus, A., Backs, J., & Schröder, K. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101669 · Cited by 30
Lucas, A. M. B., Caldas, F. R. D. L., da Silva, A. P., Ventura, M. M., Leite, I. M. R., Filgueiras, A. B. T., Silva, C. G. L., Kowaltowski, A. J., & Facundo, H. T. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.11.012 · Cited by 29
Wang, Z., Zhao, Y., & Zhao, T. C. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370220944128 · Cited by 29
ZYZ-772 Prevents Cardiomyocyte Injury by Suppressing Nox4-Derived ROS Production and Apoptosis
Wang, Y., Zhong, L., Liu, X., & Zhu, Y. Z. (2017) · Molecules · doi:10.3390/molecules22020331 · Cited by 29
Role of c-Src and reactive oxygen species in cardiovascular diseases
Hussain, M., Ikram, W., & Ikram, U. (2023) · Molecular Genetics and Genomics · doi:10.1007/s00438-023-01992-9 · Cited by 27
HAX-1 regulates SERCA2a oxidation and degradation
Bidwell, P. A., Liu, G., Nagarajan, N., Lam, C. K., Haghighi, K., Gardner, G., Cai, W., Zhao, W., Mugge, L. A., Vafiadaki, E., et al. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.11.014 · Cited by 26
Self-citation
Metadata
- Authors
- Matsushima, S., Kuroda, J., Ago, T., Zhai, P., Park, J. Y., Xie, L.-H., Tian, B., & Sadoshima, J.
- Affiliations
- University of Medicine and Dentistry of New Jersey (US)
- ORCID
- Venue
- Circulation Research
- Published
- 2013-02-15
- Volume
- 112
- Issue
- 4
- Pages
- 651-663
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- PMC
- PMC3574183
- OpenAlex
- W2140538799
- Cited by
- 183
- References
- 25
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 11 · 2023: 11 · 2022: 16 · 2021: 9 · 2020: 12 · 2019: 11 · 2018: 11 · 2017: 22 · 2016: 20 · 2015: 16 · 2014: 14 · 2013: 10
- FWCI
- 8.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Circulation Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Japan Society for the Promotion of Science (21390243)
- National Institute on Aging (AG23039, R01AG023039, R21AG042678)
- National Heart, Lung, and Blood Institute (R21HL098802, HL91469, R01HL067724, HL102738, R01HL102738, R01HL112330, HL-67724, R01HL091469, HL112330)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Fibrosis and Remodeling
- Keywords
- NOX4, HDAC4, cysteine oxidation, cardiac hypertrophy, superoxide, class II histone deacetylases, phenylephrine, pressure overload, transverse aortic constriction, cardiomyocytes, oxidative stress
- MeSH terms
- NADPH Oxidase 2, NADPH Oxidase 4, Animals, Aortic Valve Stenosis, Cell Nucleus, Cysteine, Enzyme Activation, Enzyme Induction, Cardiomegaly, Histone Deacetylases, Male, Membrane Glycoproteins, Mice, Transgenic, Nuclear Envelope, Oxidation-Reduction, Phenylephrine, Recombinant Fusion Proteins, Reactive Oxygen Species, Mice, Knockout, Oxidative Stress, NADPH Oxidases, Protein Transport, Myocytes, Cardiac, Cell Size, Mice, Rats
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
