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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.
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“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]
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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
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Items 101–189 of 189
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Functional Role of Nox4 in Autophagy
Forte, M., Palmerio, S., Yee, D., Frati, G., & Sciarretta, S. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-55330-6_16 · Cited by 25
Natural Bioactive Compounds Targeting NADPH Oxidase Pathway in Cardiovascular Diseases
Sofiullah, S. S. M., Murugan, D. D., Muid, S. A., Wu, Y. S., Kadir, S. Z. S. A., Abas, R., Ridzuan, N. R. A., Zamakshshari, N. H., & Choy, K. W. (2023) · Molecules · doi:10.3390/molecules28031047 · Cited by 28
NADPH oxidases—do they play a role in TRPC regulation under hypoxia?
Malczyk, M., Veith, C., SCHERMULY, R. T., Gudermann, T. W., Dietrich, A., Sommer, N., Weißmann, N., & Pak, O. (2015) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-015-1731-3 · Cited by 24
The novel heart-specific RING finger protein 207 is involved in energy metabolism in cardiomyocytes
Mizushima, W., Takahashi, H., Watanabe, M., Kinugawa, S., Matsushima, S., Takada, S., Yokota, T., Furihata, T., Matsumoto, J., Tsuda, M., et al. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.09.013 · Cited by 24
Self-citationRole of intracellular angiotensin II
Ré, R. N. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00632.2017 · Cited by 24
Paracrine 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
Liu, J., Wang, L., Ge, L., Sun, W., Song, Z., Lu, X., Jin, C., Wu, S., & Yang, J. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.112831 · Cited by 25
NOX4 inhibition promotes the remodeling of dystrophic muscle
Hammers, D. W. (2022) · JCI Insight · doi:10.1172/jci.insight.158316 · Cited by 22
Harijith, A. K., Basa, P., Ha, A. W., Thomas, J., Jafri, A., Fu, P., MacFarlane, P. M., Raffay, T. M., Natarajan, V., & Sudhadevi, T. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.880878 · Cited by 23
Li, B., Wang, X., Yu, M., Yang, P. C., & Wang, W. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118378 · Cited by 20
Fu, P., Ramchandran, R., Sudhadevi, T., Kumar, P. P., Krishnan, Y., Liu, Y., Zhao, Y., Parinandi, N. L., Harijith, A. K., Sadoshima, J., et al. (2021) · Antioxidants · doi:10.3390/antiox10030477 · Cited by 19
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Yang, W., Liu, Z., Xu, Q., Peng, H., Chen, L., Huang, X. Y., Yang, T., Yu, Z., Cheng, G., Zhang, G., et al. (2016) · Journal of the American Society of Hypertension · doi:10.1016/j.jash.2016.08.002 · Cited by 19
Targeting NRF2 to suppress ferroptosis in brain injury.
Song, S., Gao, Y., Sheng, Y., Rui, T., & Luo, C. (2021) · PubMed · doi:10.14670/hh-18-286 · Cited by 20
Cardiac Cell Senescence and Redox Signaling
Cesselli, D., Aleksova, A., Sponga, S., Cervellin, C., Loreto, C. D., Tell, G., & Beltrami, A. P. (2017) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2017.00038 · Cited by 20
Miao, R., Wang, L., Chen, Z., Ge, S., Li, L., Zhang, K., Chen, Y., Guo, W., Duan, X., Zhu, M., et al. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1000578 · Cited by 18
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Wu, R. F., Liao, C., hatoum, H. H., Fu, G., Ochoa, C. D., & Terada, L. S. (2016) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.116.307922 · Cited by 19
Liu, Y., Shen, H., Wang, X.-Q.-Y., Liu, H.-Q., Zheng, L., & Luo, J. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26862 · Cited by 20
Macedo, F. N., Souza, D. S., Araújo, J. E. D. S., Dantas, C. O., Miguel‐dos‐Santos, R., Silva‐Filha, E., Rabelo, T. K., dos Santos, R. V., Zhang, R., Barreto, A. S., et al. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.005 · Cited by 18
Meneses‐Valdés, R., Gallero, S., Henríquez‐Olguín, C., & Jensen, T. E. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.07.035 · Cited by 17
Nuclear membrane-localised NOX4D generates pro-survival ROS in FLT3-ITD-expressing AML
Moloney, J. N., Jayavelu, A. K., Stanicka, J., Roche, S. L., O’Brien, R. L., Scholl, S., Böhmer, F.-D., & Cotter, T. G. (2017) · Oncotarget · doi:10.18632/oncotarget.22241 · Cited by 19
David, C. E. B., Lucas, A. M. B., Araújo, M. T. S., Coelho, B. N., Neto, J. B. S., Portela, B. R. C., Varela, A. L. N., Kowaltowski, A. J., & Facundo, H. T. (2018) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2018.08.008 · Cited by 17
Chen, L., Zhao, M., Li, J., Wang, Y., Bao, Q., Wu, S., Deng, X., Tang, X., Wu, W., & Liu, X. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1260210 · Cited by 17
Labbé, P., Thorin, É., & Thorin‐Trescases, N. (2025) · Antioxidants · doi:10.3390/antiox14091137 · Cited by 16
Aziz, S. G., Pourheydar, B., Chodari, L., & Hamidifar, F. (2022) · Microvascular Research · doi:10.1016/j.mvr.2022.104380 · Cited by 16
Baqader, N. O., Radulović, M., Crawford, M., Stoeber, K., & Godovac‐Zimmermann, J. (2014) · Journal of Proteome Research · doi:10.1021/pr500638h · Cited by 16
Fernández-Puente, E., & Palomero, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910876 · Cited by 16
Wang, Y., Yuan, J., Liu, H., Chen, J., Zou, J., Zeng, X., Du, L., Sun, X., Xia, Z., Geng, Q., et al. (2023) · Genes & Diseases · doi:10.1016/j.gendis.2023.101100 · Cited by 15
Luminal flow induces NADPH oxidase 4 translocation to the nuclei of thick ascending limbs
Sáez, F., Hong, N. J., & Garvin, J. L. (2016) · Physiological Reports · doi:10.14814/phy2.12724 · Cited by 15
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Ricci, A., Galluzzi, L., Magnani, M., & Menotta, M. (2019) · The FASEB Journal · doi:10.1096/fj.201902039r · Cited by 15
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Zhang, J., & Bar‐Peled, L. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102352 · Cited by 12
Yang, R., Tan, X. L., Ge, L.-J., Sun, J., Peng, X.-D., & Wang, W. (2019) · Nitric Oxide · doi:10.1016/j.niox.2019.09.002 · Cited by 11
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Zhang, R., Xu, X., Chen, X., Hao, C., Ji, Z., Zuo, P., Yang, M., Ma, G., & Li, Y. (2022) · BMC Genomics · doi:10.1186/s12864-022-08778-0 · Cited by 11
Zeng, S., Yan, Q., Yang, L., Mei, Q., & Lu, H. (2020) · Mediators of Inflammation · doi:10.1155/2020/1078365 · Cited by 11
Ferreira, W. A. S., Vitiello, G. A. F., Medina, T. D. S., & de Oliveira, E. H. C. (2022) · Scientific Reports · doi:10.1038/s41598-022-10114-1 · Cited by 12
Ahmad, M. B., Islam, A. U., Hassan, S., Tarfeen, N., Nisa, K. U., Nisar, K., Hassan, T., Ganiee, S. A., Bhat, A. R., & Ganai, B. A. (2025) · The Nucleus · doi:10.1007/s13237-024-00529-8 · Cited by 10
Mishra, A. P., Kumar, R., Harilal, S., Nigam, M., Datta, D., Singh, S. K., Waranuch, N., & Chittasupho, C. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03469-x · Cited by 9
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Yan, H. M., Yin, Y., Zhou, Y., Li, Z., Li, Y., Ren, L., Wen, J., & Wang, W. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103379 · Cited by 8
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He, X., Liu, J., Gu, F., Chen, J., Lu, Y. W., Ding, J., Guo, H., Nie, M., Kataoka, M., Lin, Z., et al. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.08.022 · Cited by 8
Lin, Y., Zhang, H., Jiang, Y., & Tian, W. (2025) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2025.1662989 · Cited by 5
Byrne, N. J., Koentges, C., Khan, E., Pfeil, K., Sandulescu, R., Bakshi, S., Költgen, C., Vosko, I., Gollmer, J., Rathner, T., et al. (2025) · Journal of Molecular and Cellular Cardiology Plus · doi:10.1016/j.jmccpl.2025.100299 · Cited by 5
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Ansari, U., Behnes, M., Hoffmann, J., Weidner, K., Kuche, P., Rusnak, J., Kim, S., Natale, M., Reckord, N., Lang, S., et al. (2021) · Scandinavian Cardiovascular Journal · doi:10.1080/14017431.2021.1995036 · Cited by 5
Upadhyay, R. K., Kumar, K., Vishwakarma, V. K., Singh, N., Narang, R., Parakh, N., Yadav, M., Yadav, S., Kumar, S., Goyal, A., et al. (2024) · Current Vascular Pharmacology · doi:10.2174/0115701611308870240910115023 · Cited by 6
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Angelini, A., Pi, X., & Xie, L. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.01044 · Cited by 6
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Jin, M. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103852 · Cited by 6
Pal, N., Kesarwani, R., Mandal, T. K., & Bhabak, K. P. (2025) · ACS Applied Bio Materials · doi:10.1021/acsabm.5c02154 · Cited by 3
Lucas, A. M. B., Palácio, P. B., Cunha, P. L. O., & Facundo, H. T. (2024) · Free Radical Research · doi:10.1080/10715762.2024.2342962 · Cited by 3
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Ma, X., Wei, R., Song, A., Zhang, X., Zou, J., & Hao, S. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5599 · Cited by 2
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Qin, S., Chen, C. F., Wang, X., Deng, L., Wang, J., Zhu, C., Zhu, C., Cao, Y., & Zhang, S. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.153230 · Cited by 2
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Labbé, P., Martel, C., Shi, Y., Montezano, A. C. I., He, Y., Gillis, M., Higgins, M., Villeneuve, L. R., Touyz, R. M., Tardif, J., et al. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1320065 · Cited by 2
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Isayama, Y. S., Matsushima, S., Shinohara, K., Isayama, K., Enzan, N., Yamamoto, T., Sada, M., Miyake, R., Tsutsui, Y., Toyohara, T., et al. (2025) · Hypertension Research · doi:10.1038/s41440-025-02348-z · Cited by 1
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Jia, J., Ji, K., Zhou, Y., Huang, Y., Li, A., Fan, Y., Huang, W., Chen, F., & Lu, G. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-03113-y · Cited by 1
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Wang, Y., Ben, T., Fang, J., Li, Z., Ding, J., Xu, L., Lin, K., & Jiang, L. (2026) · Experimental Biology and Medicine · doi:10.3389/ebm.2026.10941 · Cited by 2
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Prasad, A., Kushwaha, R., Alugoju, P., Pospíšil, P., & Rathi, D. (2026) · Journal of Immunology Research · doi:10.1155/jimr/2847417 · Cited by 1
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Hecker, L., Kato, K., & Griendling, K. K. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_12 · Cited by 2
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Bansal, M. P. (2023) · Springer eBooks · doi:10.1007/978-981-99-7342-2_8 · Cited by 1
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Kartha, C. C. (2021) · Springer eBooks · doi:10.1007/978-3-030-85536-9_15 · Cited by 1
Lin, J., Zheng, Y., Wan, G., & Gu, X. (2020) · doi:10.22541/au.159007727.72815269 · Cited by 1
Pathogenesis of Macrovascular Complications in Diabetes
Østergaard, J. A., Block, T. J., Dahm, S. I., Khan, W., & Jandeleit-Dahm, K. A. M. (2024) · Wiley eBooks · doi:10.1002/9781119697473.ch46 · Cited by 1
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Keijer, J. P., Polderman, P. E., Alcaraz, P. S., van Es, R. M., González, D. M., Kok, R. N. U., Baghdadi, S. E., Gulersonmez, C. M. C., Stigter, E. C. A., Vos, H. R., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.13.724825 · Cited by 1
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Hong, K. U., & Moore, J. B. (2013) · Circulation Research · doi:10.1161/circresaha.113.302990
Ranayhossaini, D. (2014) · D-Scholarship@Pitt (University of Pittsburgh)
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Jaishy, B. P. (2013)
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Kronlage, M., Katus, H. A., & Backs, J. (2016) · Cardiac and vascular biology · doi:10.1007/978-3-319-41457-7_8
Application of redox biosensor mouse models to study redox processes in cardiomyocytes
Nanadikar, M. S. (2019) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7597
Soft electrophile inhibition of selenoenzymes in disease pathologies
Ralston, N. V. C., & Raymond, L. J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819092-0.00040-6
松島, 将., Sadoshima, J., & 裕之, 筒. (2017) · Journal of JCS Cardiologists · doi:10.1253/jjcsc.25.2_157
Self-citationFernández-Puente, E., & Palomero, J. (2022) · Vide Leaf, Hyderabad eBooks · doi:10.37247/pamol3ed.3.2022.16
Zhang, R., Xu, X., Chen, X., Hao, C., Ji, Z., Zuo, P., Yang, M., Ma, G., & Li, Y. (2022) · Figshare · doi:10.6084/m9.figshare.20486800
Zhang, R., Xu, X., Chen, X., Hao, C., Ji, Z., Zuo, P., Yang, M., Ma, G., & Li, Y. (2022) · Figshare · doi:10.6084/m9.figshare.20486809
Zhang, R., Xu, X., Chen, X. X., Hao, C., Ji, Z., Zuo, P., Yang, M., Ma, G., & Li, Y. (2022) · Figshare · doi:10.6084/m9.figshare.20486806
Zhang, R., Xu, X., Chen, X., Hao, C., Ji, Z., Zuo, P., Yang, M., Ma, G., & Li, Y. (2022) · Figshare · doi:10.6084/m9.figshare.20486803
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Shabanian, K., Shabanian, T., Karsai, G., Lettlová, S., Pontiggia, L., Ruschitzka, F. T., Beer, J. H., & Saravi, S. S. S. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4818945
Li, F., Zhuo, L., Xie, F., Luo, H., Li, Y., Lin, H., & Li, X. (2024) · Vascular · doi:10.1177/17085381241273289
Zhang, R., Xu, X., Chen, X., Hao, C., Ji, Z., Zuo, P., Yang, M., Ma, G., & Li, Y. (2022) · Figshare · doi:10.6084/m9.figshare.20486812
Huang, C., Yang, Y., Wu, S., Liu, Z., Chen, L., Yan, D., Wei, M., Yan, K., Wang, R., Hu, J., et al. (2026) · BMC Pharmacology and Toxicology · doi:10.1186/s40360-025-01078-9
Musikhina, N. A., Евгеньевич, Ш. Н., Викторовна, Д. Н., Gorbatenko, E. A., Larionova, O. N., Tuzmukhametova, O. H., & Анатольевич, А. Д. (2026) · Arterial’naya Gipertenziya (Arterial Hypertension) · doi:10.18705/1607-419x-2025-2576
Characterization of an auranofin-resistant ovarian cancer cell line A2780
Limaj, X. (2024) · theses.fr (ABES) · doi:10.70675/5f21b24bzd436z4168z8555zdc660e2b2aca
Pan, X., Yang, Y., Liu, C., Xu, L., Yu, J., Ge, S., Wang, W., Wang, C., Wei, W., Wu, S., et al. (2026) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2026.179127
BindingDB (2020) · UC San Diego · doi:10.7270/q2vd722w
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
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