Hyperglycemia-Driven Inhibition of AMP-Activated Protein Kinase α2 Induces Diabetic Cardiomyopathy by Promoting Mitochondria-Associated Endoplasmic Reticulum Membranes In Vivo
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Background: Fundc1 (FUN14 domain containing 1), an outer mitochondrial membrane protein, is important for mitophagy and mitochondria-associated endoplasmic reticulum membranes (MAMs). The roles of Fundc1 and MAMs in diabetic hearts remain unknown. The aims of this study, therefore, were to determine whether the diabetes mellitus–induced Fundc1 expression could increase MAM formation, and whether disruption of MAM formation improves diabetic cardiac function. Methods: Levels of FUNDC1 were examined in the hearts from diabetic patients and nondiabetic donors. Levels of Fundc1-induced MAMs and mitochondrial and heart function were examined in mouse neonatal cardiomyocytes exposed to high glucose (HG, 30 mmol/L d -glucose for 48 hours), and in streptozotocin-treated cardiac-specific Fundc1 knockout mice and cardiac-specific Fundc1 knockout diabetic Akita mice, as well. Results: FUNDC1 levels were significantly elevated in cardiac tissues from diabetic patients in comparison with those from nondiabetic donors. In cultured mouse neonatal cardiomyocytes, HG conditions increased levels of Fundc1, the inositol 1,4,5-trisphosphate type 2 receptor (Ip 3 r2), and MAMs. Genetic downregulation of either Fundc1 or Ip 3 r2 inhibited MAM formation, reduced endoplasmic reticulum-mitochondrial Ca 2+ flux, and improved mitochondrial function in HG-treated cardiomyocytes. Consistently, adenoviral overexpression of Fundc1 promoted MAM formation, mitochondrial Ca 2+ increase, and mitochondrial dysfunction in cardiomyocytes exposed to normal glucose (5.5 mmol/L d -glucose). In comparison with nondiabetic controls, levels of Fundc1, Ip 3 r2, and MAMs were significantly increased in hearts from streptozotocin-treated mice and Akita mice. Furthermore, in comparison with control hearts, diabetes mellitus markedly increased coimmunoprecipitation of Fundc1 and Ip 3 r2. The binding of Fundc1 to Ip 3 r2 inhibits Ip 3 r2 ubiquitination and proteasome-mediated degradation. Cardiomyocyte-specific Fundc1 deletion ablated diabetes mellitus–induced MAM formation, prevented mitochondrial Ca 2+ increase, mitochondrial fragmentation, and apoptosis with improved mitochondrial functional capacity and cardiac function. In mouse neonatal cardiomyocytes, HG suppressed AMP-activated protein kinase activity. Furthermore, in cardiomyocytes of Prkaa2 knockout mice, expression of Fundc1, MAM formation, and mitochondrial Ca 2+ levels were significantly increased. Finally, adenoviral overexpression of a constitutively active mutant AMP-activated protein kinase ablated HG-induced MAM formation and mitochondrial dysfunction. Conclusions: We conclude that diabetes mellitus suppresses AMP-activated protein kinase, initiating Fundc1-mediated MAM formation, mitochondrial dysfunction, and cardiomyopathy, suggesting that AMP-activated protein kinase–induced Fundc1 suppression is a valid target to treat diabetic cardiomyopathy.
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AMPK activation reversed DCM by suppressing high glucose-induced MAM formation, mitochondrial Ca2+ increase, and mitochondrial dysfunction in cultured mouse neonatal cardiomyocytes.
“In addition, AMPK activation reversed DCM by suppressing high glucose-induced MAM formation, mitochondrial Ca2+ increase, and mitochondrial dysfunction in cultured mouse neonatal cardiomyocytes 139].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [139]
High glucose-driven inactivation of AMPK increased FUNDC1, resulting in aberrant MAM formation, mitochondrial Ca2+ increase, mitochondrial dysfunction, and cardiac dysfunction.
“High glucose-driven inactivation of AMPK increased FUNDC1, resulting in aberrant MAM formation, mitochondrial Ca2+ increase, mitochondrial dysfunction, and cardiac dysfunction [139].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [139]
AMPK activation, likely via downregulation of FUNDC1-related MAMs, represents a new therapeutic avenue for treating DCM.
“These findings illustrating the results of AMPK activation, likely via downregulation of FUNDC1-related MAMs, represent a new therapeutic avenue for treating DCM [139].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [139]
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Biochemistry and molecular cell biology of diabetic complications
Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107 · see citing works
Down-Regulation of Na+/K+ATPase Activity by Human Parvovirus B19 Capsid Protein VP1
Almilaji, A., Szteyn, K., Fein, E., Pakladok, T., Muñoz, C., Elvira, B., Towhid, S. T., Alesutan, I., Shumilina, E. V., Bock, C. –., et al. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350083 · Cited by 8,675 · see citing works
Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652 · see citing works
Cillà, S. D., Farruggio, S., Vujosevic, S., Raina, G., Filippini, D. A., Gatti, V., Clemente, N., Mary, D., Vezzola, D., Casini, G., et al. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479441 · Cited by 5,154 · see citing works
The Pathophysiology of Mitochondrial Cell Death
Green, D. R., & Kroemer, G. (2004) · Science · doi:10.1126/science.1099320 · Cited by 3,416 · see citing works
Regulation of cell death: the calcium–apoptosis link
Orrenius, S., Zhivotovsky, B., & Nicotera, P. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1150 · Cited by 2,990 · see citing works
Mitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442 · see citing works
Dysfunction of Mitochondria in Human Skeletal Muscle in Type 2 Diabetes
Kelley, D. E., He, J., Menshikova, E. V., & Ritov, V. B. (2002) · Diabetes · doi:10.2337/diabetes.51.10.2944 · Cited by 2,321 · see citing works
Mitochondrial dysfunction and type 2 diabetes
Lowell, B. B., & Shulman, G. I. (2005) · Science · doi:10.1126/science.1104343 · Cited by 2,070 · see citing works
Mitochondria as sensors and regulators of calcium signalling
Rizzuto, R., De Stefani, D., Raffaello, A., & Mammucari, C. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3412 · Cited by 1,781 · see citing works
Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells
Liu, L., Feng, D., Chen, G., Chen, M., Zheng, Q., Song, P., Ma, Q., Zhu, C., Wang, R., Qi, W., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2422 · Cited by 1,689 · see citing works
Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores
Minta, A., Kao, J. P. Y., & Tsien, R. Y. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83165-9 · Cited by 1,621 · see citing works
Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413 · see citing works
Mitophagy: mechanisms, pathophysiological roles, and analysis
Ding, W.-X., & Yin, X.-M. (2012) · bchm · doi:10.1515/hsz-2012-0119 · Cited by 1,032 · see citing works
Cárdenas, C., Miller, R. A., Smith, I., Bui, T., Molgó, J., Müller, M., Vais, H., Cheung, K.-H., Yang, J., Parker, I., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.007 · Cited by 1,026 · see citing works
Endoplasmic reticulum-mitochondria contacts: Function of the junction
Rowland, A. A., & Voeltz, G. K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3440 · Cited by 1,018 · see citing works
Isolation of mitochondria-associated membranes and mitochondria from animal tissues and cells
Wieckowski, M. R., Giorgi, C., Lebiedzinska, M., Duszynski, J., & Pinton, P. (2009) · Nature Protocols · doi:10.1038/nprot.2009.151 · Cited by 979 · see citing works
Circularly permuted green fluorescent proteins engineered to sense Ca 2+
Nagai, T., Sakaue-Sawano, A., Park, E. S., & Miyawaki, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051636098 · Cited by 969 · see citing works
Regulation of mitochondrial dehydrogenases by calcium ions
Denton, R. M. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.01.005 · Cited by 885 · see citing works
NCLX is an essential component of mitochondrial Na + /Ca 2+ exchange
Palty, R., Silverman, W. F., Hershfinkel, M., Caporale, T., Sensi, S. L., Parnis, J., Nolte, C., Fishman, D., Shoshan‐Barmatz, V., Herrmann, S., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908099107 · Cited by 789 · see citing works
Arruda, A. P., Pers, B. M., Parlakgül, G., Güney, E., Inouye, K., & Hotamışlıgil, G. S. (2014) · Nature Medicine · doi:10.1038/nm.3735 · Cited by 716 · see citing works
Chen, G., Han, Z., Feng, D., Chen, Y., Chen, L., Wu, H., Huang, L., Zhou, C., Cai, X., Fu, C., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.034 · Cited by 600 · see citing works
Wang, J., Takeuchi, T., Tanaka, S., Kubo, S.-K., Kayo, T., Lu, D., Takata, K., Koizumi, A., & Izumi, T. (1999) · Journal of Clinical Investigation · doi:10.1172/jci4431 · Cited by 572 · see citing works
Endogenous Drp1 Mediates Mitochondrial Autophagy and Protects the Heart Against Energy Stress
Ikeda, Y., Shirakabe, A., Maejima, Y., Zhai, P., Sciarretta, S., Toli, J., Nomura, M., Mihara, K., Egashira, K., Ohishi, M., et al. (2015) · Circulation Research · doi:10.1161/circresaha.116.303356 · Cited by 571 · see citing works
Mitochondrial calcium overload is a key determinant in heart failure
Santulli, G., Xie, W., Reiken, S. R., & Marks, A. R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1513047112 · Cited by 561 · see citing works
The role of mitochondria in the pathogenesis of type 2 diabetes
Patti, M.-E., & Corvera, S. (2010) · Endocrine Reviews · doi:10.1210/er.2009-0027 · Cited by 551 · see citing works
Betz, C., Stracka, D., Prescianotto-Baschong, C., Frieden, M., Demaurex, N., & Hall, M. N. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302455110 · Cited by 538 · see citing works
The endoplasmic reticulum–mitochondria connection: One touch, multiple functions
Marchi, S., Patergnani, S., & Pinton, P. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.015 · Cited by 506 · see citing works
Xie, Z., Lau, K., Eby, B., Lozano, P., He, C., Pennington, B., Li, H., Rathi, S., Dong, Y., Tian, R., et al. (2011) · Diabetes · doi:10.2337/db10-0351 · Cited by 490 · see citing works
Song, M., Mihara, K., Chen, Y., Scorrano, L., & Dorn, G. W. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.011 · Cited by 482 · see citing works
Szabadkai, G., Simoni, A. M., Chami, M., Wieckowski, M. R., Youle, R. J., & Rizzuto, R. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.026 · Cited by 468 · see citing works
CaMKII determines mitochondrial stress responses in heart
Joiner, M.-L. A., Koval, O. M., Li, J., He, B. J., Allamargot, C., Gao, Z., Luczak, E. D., Hall, D. D., Fink, B. D., Chen, B., et al. (2012) · Nature · doi:10.1038/nature11444 · Cited by 411 · see citing works
Tubbs, E., Theurey, P., Vial, G., Bendridi, N., Bravard, A., Chauvin, M.-A., Ji-Cao, J., Zoulim, F., Bartosch, B., Ovize, M., et al. (2014) · Diabetes · doi:10.2337/db13-1751 · Cited by 411 · see citing works
Structural and functional link between the mitochondrial network and the endoplasmic reticulum
Giorgi, C., Stefani, D. D., Bononi, A., Rizzuto, R., & Pinton, P. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.04.010 · Cited by 375 · see citing works
Wu, W., Lin, C., Wu, K., Jiang, L., Wang, X., Li, W., Zhuang, H., Zhang, X., Chen, H. H., Li, S., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593102 · Cited by 362 · see citing works
Metabolic stress–induced activation of FoxO1 triggers diabetic cardiomyopathy in mice
Battiprolu, P. K., Hojayev, B., Jiang, N., Wang, Z. V., Luo, X., Iglewski, M., Shelton, J. M., Gerard, R. D., Rothermel, B. A., Gillette, T. G., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci60329 · Cited by 344 · see citing works
Giorgi, C., Missiroli, S., Patergnani, S., Duszyński, J., Wieckowski, M. R., & Pinton, P. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6223 · Cited by 332 · see citing works
Wu, S., Lu, Q., Wang, Q., Ding, Y., Ma, Z., Mao, X., Huang, K., Xie, Z., & Zou, M.-H. (2017) · Circulation · doi:10.1161/circulationaha.117.030235 · Cited by 320 · see citing works
Marchi, S., & Pinton, P. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.268235 · Cited by 295 · see citing works
Zhang, D., Liu, Z.-X., Choi, C. S., Tian, L., Kibbey, R., Dong, J., Cline, G. W., Wood, P. A., & Shulman, G. I. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707060104 · Cited by 291 · see citing works
Ronchi, J. A., Figueira, T. R., Ravagnani, F. G., Oliveira, H. C. F., Vercesi, A. E., & Castilho, R. F. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.049 · Cited by 283 · see citing works
Paillard, M., Tubbs, E., Thiébaut, P., Gomez, L., Fauconnier, J., Silva, C. C. D., Teixeira, G., Mewton, N., Belaïdi, E., Durand, A., et al. (2013) · Circulation · doi:10.1161/circulationaha.113.001225 · Cited by 279 · see citing works
Xie, Z., Dong, Y., Scholz, R., Neumann, D., & Zou, M.-H. (2008) · Circulation · doi:10.1161/circulationaha.107.744490 · Cited by 273 · see citing works
Self-citationDong, Y., Zhang, M., Liang, B., Xie, Z., Zhao, Z., Asfa, S., Choi, H. C., & Zou, M. (2010) · Circulation · doi:10.1161/circulationaha.109.900928 · Cited by 263 · see citing works
Diminished Autophagy Limits Cardiac Injury in Mouse Models of Type 1 Diabetes
Xu, X., Kobayashi, S., Chen, K., Timm, D. J., Volden, P. A., Huang, Y., Gulick, J. M., Yue, Z., Robbins, J. M., Epstein, P. N., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.474650 · Cited by 251 · see citing works
Defective intracellular Ca2+ signaling contributes to cardiomyopathy in Type 1 diabetic rats
Choi, K. M., Zhong, Y., Hoit, B. D., Grupp, I. L., Hahn, H. S., Dilly, K. W., Guatimosim, S., Lederer, W. J., & Matlib, M. A. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00313.2002 · Cited by 251 · see citing works
Rutter, G. A., Burnett, P., Rizzuto, R., Brini, M., Murgia, M., Pozzan, T., Tavaré, J. M., & Denton, R. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5489 · Cited by 241 · see citing works
Recipes for Creating Animal Models of Diabetic Cardiovascular Disease
Hsueh, W. A., Abel, E. D., Breslow, J. L., Maeda, N., Davis, R. C., Fisher, E. A. A., Dansky, H. M., McClain, D. A., McIndoe, R., Wassef, M. K., et al. (2007) · Circulation Research · doi:10.1161/01.res.0000266449.37396.1f · Cited by 219 · see citing works
Evans‐Anderson, H. J., Alfieri, C. M., & Yutzey, K. E. (2008) · Circulation Research · doi:10.1161/circresaha.107.163428 · Cited by 215 · see citing works
Danese, A., Patergnani, S., Bonora, M., Wieckowski, M. R., Previati, M., Giorgi, C., & Pinton, P. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.01.003 · Cited by 184 · see citing works
NCLX: The mitochondrial sodium calcium exchanger
Boyman, L., Williams, G. S. B., Khananshvili, D., Sekler, I., & Lederer, W. J. (2013) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2013.03.012 · Cited by 172 · see citing works
Mitochondria and cardioprotection
Lisa, F. D., Canton, M., Menabò, R., Kaludercic, N., & Bernardi, P. (2007) · Heart Failure Reviews · doi:10.1007/s10741-007-9028-z · Cited by 170 · see citing works
Barlow, A. L., MacLeod, A., Noppen, S., Sanderson, J., & Guérin, C. J. (2010) · Microscopy and Microanalysis · doi:10.1017/s143192761009389x · Cited by 166 · see citing works
Basu, R., Oudit, G. Y., Wang, X., Zhang, L., Ussher, J. R., Lopaschuk, G. D., & Kassiri, Z. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00452.2009 · Cited by 161 · see citing works
Localization and Processing of the Amyloid-β Protein Precursor in Mitochondria-Associated Membranes
Prete, D. D., Suski, J. M., Oulès, B., Debayle, D., Gay, A.-S., Lacas‐Gervais, S., Bussiere, R., Bauer, C., Pinton, P., Paterlini-Bréchot, P., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160953 · Cited by 161 · see citing works
Meng, S., Cao, J., He, Q., Xiong, L., Chang, E., Radovick, S., Wondisford, F. E., & He, L. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.604421 · Cited by 146 · see citing works
FoxO1 is crucial for sustaining cardiomyocyte metabolism and cell survival
Puthanveetil, P., Wan, A., & Rodrigues, B. B. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs426 · Cited by 134 · see citing works
Calcium and mitochondria: mechanisms and functions of a troubled relationship
Bianchi, K., Rimessi, A., Prandini, A., Szabadkai, G., & Rizzuto, R. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.015 · Cited by 128 · see citing works
The mitochondrial membrane potential and Ca2+ oscillations in smooth muscle
Chalmers, S., & McCarron, J. G. (2007) · Journal of Cell Science · doi:10.1242/jcs.014522 · Cited by 110 · see citing works
Lu, J. P., Wang, Y., Sliter, D. A., Pearce, M. M. P., & Wojcikiewicz, R. J. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.251983 · Cited by 102 · see citing works
Joseph, L. C., Barca, E., Subramanyam, P., Komrowski, M., Pajvani, U., Colecraft, H. M., Hirano, M., & Morrow, J. P. (2016) · PLOS ONE · doi:10.1371/journal.pone.0145750 · Cited by 99 · see citing works
New mouse model to study islet transplantation in insulin-dependent diabetes mellitus
Mathews, C. E., Langley, S. H., & Leiter, E. H. (2002) · Transplantation · doi:10.1097/00007890-200204270-00024 · Cited by 95 · see citing works
Regulation of intracellular Ca2+ in the heart during diabetes
Pierce, G. N. (1997) · Cardiovascular Research · doi:10.1016/s0008-6363(97)00010-2 · Cited by 91 · see citing works
Qi, Y., Zhu, Q., Zhang, K., Thomas, C., Wu, Y., Kumar, R., Baker, K. M., Xu, Z., Chen, S., & Guo, S. (2014) · Circulation Heart Failure · doi:10.1161/circheartfailure.114.001457 · Cited by 91 · see citing works
Bonora, M., Morganti, C., Morciano, G., Giorgi, C., Wieckowski, M. R., & Pinton, P. (2016) · Nature Protocols · doi:10.1038/nprot.2016.064 · Cited by 79 · see citing works
Measurements of mitochondrial calcium in vivo
Pozzan, T., & Rudolf, R. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.11.012 · Cited by 75 · see citing works
Updating Experimental Models of Diabetic Cardiomyopathy
Fuentes‐Antrás, J., Picatoste, B., Gómez‐Hernández, A., Egido, J., Tuñón, J., & Lorenzo, Ó. (2015) · Journal of Diabetes Research · doi:10.1155/2015/656795 · Cited by 72 · see citing works
Nita, I. I., Hershfinkel, M., Fishman, D., Ozeri, E., Rutter, G. A., Sensi, S. L., Khananshvili, D., Lewis, E. C., & Sekler, I. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046649 · Cited by 72 · see citing works
Voccoli, V., Tonazzini, I., Signore, G., Caleo, M., & Cecchini, M. G. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.483 · Cited by 70 · see citing works
Vance, J. E., Stone, S. J., & Faust, J. R. (1997) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/s0005-2760(96)00153-1 · Cited by 69 · see citing works
Boutagy, N. E., Rogers, G. W., Pyne, E. S., Ali, M. M., Hulver, M. W., & Frisard, M. I. (2015) · Journal of Visualized Experiments · doi:10.3791/53216 · Cited by 53 · see citing works
Studying mitochondrial Ca2+ uptake – A revisit
Jean-Quartier, C., Bondarenko, A. I., Alam, M. R., Trenker, M., Waldeck‐Weiermair, M., Malli, R., & Graier, W. F. (2011) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2011.10.033 · Cited by 52 · see citing works
Wendt, E., Ferry, H., Greaves, D. R., & Keshav, S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119532 · Cited by 40 · see citing works
Talbot, J. D., Barrett, J. N., Barrett, E. F., & David, G. (2007) · The Journal of Physiology · doi:10.1113/jphysiol.2006.126383 · Cited by 37 · see citing works
Regulation of metabolism in individual mitochondria during excitation–contraction coupling
Gong, G., Liu, X., & Wang, W. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.09.012 · Cited by 37 · see citing works
Figueira, T. R. (2013) · Experimental Physiology · doi:10.1113/expphysiol.2013.074682 · Cited by 15 · see citing works
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Ren, J., Bi, Y., Sowers, J. R., Hetz, C., & Zhang, Y. (2021) · Nature Reviews Cardiology · doi:10.1038/s41569-021-00511-w · Cited by 708 · see citing works
Obesity cardiomyopathy: evidence, mechanisms, and therapeutic implications
Ren, J. T., Wu, N. N., Wang, S., Sowers, J. R., & Zhang, Y. (2021) · Physiological Reviews · doi:10.1152/physrev.00030.2020 · Cited by 377 · see citing works
Regulation of Mitochondrial ATP Production: Ca2+ Signaling and Quality Control
Boyman, L., Karbowski, M., & Lederer, W. J. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.10.007 · Cited by 309 · see citing works
AMPK, Mitochondrial Function, and Cardiovascular Disease
Wu, S., & Zou, M.-H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144987 · Cited by 286 · see citing works
Mitochondrial ROS Formation in the Pathogenesis of Diabetic Cardiomyopathy
Kaludercic, N., & Lisa, F. D. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.00012 · Cited by 264 · see citing works
Yu, L., Dong, X., Xue, X., Xu, S. C., Zhang, X., Xu, Y., Wang, Z., Wang, Y., Gao, H., Liang, Y., et al. (2020) · Journal of Pineal Research · doi:10.1111/jpi.12698 · Cited by 222 · see citing works
Cai, Y., Yang, E., Yao, X., Zhang, X., Wang, Q., Wang, Y., Liu, J., Fan, W., Yi, K., Kang, C., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101792 · Cited by 198 · see citing works
Potential role of mitochondria-associated endoplasmic reticulum membrane proteins in diseases
Mao, H. Z., Chen, W., Chen, L., & Li, L. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115011 · Cited by 157 · see citing works
Pei, Z., Liu, Y., Liu, S., Wei, J. J., Luo, Y., Sun, M., Duan, Y., Ajoolabady, A., Sowers, J. R., Fang, Y., et al. (2021) · Metabolism · doi:10.1016/j.metabol.2021.154840 · Cited by 152 · see citing works
Dia, M., Gomez, L., Thibault, H., Tessier, N., Léon, C., Chouabe, C., Ducreux, S., Gallo-Bona, N., Tubbs, E., Bendridi, N., et al. (2020) · Basic Research in Cardiology · doi:10.1007/s00395-020-00835-7 · Cited by 151 · see citing works
Schiattarella, G. G., Altamirano, F. J., Kim, S. Y., Tong, D., Ferdous, A., Piristine, H. C., Dasgupta, S., Wang, X., French, K. M., Villalobos, E., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21931-9 · Cited by 144 · see citing works
Xie, S., Liu, S., Zhang, T., Shi, W., Xing, Y., Fang, W., Zhang, M., Chen, M.-Y., Xu, S., Fan, M.-Q., et al. (2023) · Circulation · doi:10.1161/circulationaha.123.065603 · Cited by 143 · see citing works
Mitochondrial quality surveillance as a therapeutic target in myocardial infarction
Zhu, H., Toan, S., Mui, D., & Zhou, H. (2020) · Acta Physiologica · doi:10.1111/apha.13590 · Cited by 142 · see citing works
Ren, J. T., Sun, M., Zhou, H., Ajoolabady, A., Zhou, Y., Tao, J., Sowers, J. R., & Zhang, Y. (2020) · Science Advances · doi:10.1126/sciadv.abc8561 · Cited by 137 · see citing works
Wang, C., Dai, X., Wu, S., Xu, W., Song, P., Huang, K., & Zou, M. (2021) · Nature Communications · doi:10.1038/s41467-021-22771-3 · Cited by 133 · see citing works
Mitochondria-Associated Endoplasmic Reticulum Membranes in Cardiovascular Diseases
Gao, P., Yan, Z., & Zhu, Z. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.604240 · Cited by 129 · see citing works
Peng, C. Y., Zhang, Y., Lang, X., & Zhang, Y. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-03928-8 · Cited by 123 · see citing works
Molecular Mechanisms and Regulation of Mammalian Mitophagy
Choubey, V., Zeb, A., & Kaasik, A. (2021) · Cells · doi:10.3390/cells11010038 · Cited by 123 · see citing works
Zhao, W., & Sheng, R. (2024) · Acta Pharmacologica Sinica · doi:10.1038/s41401-024-01359-9 · Cited by 122 · see citing works
Qi, B., He, L., Zhao, Y., Zhang, L., He, Y., Li, J., Li, C., Zhang, B., Huang, Q., Xing, J., et al. (2020) · Diabetologia · doi:10.1007/s00125-020-05103-w · Cited by 116 · see citing works
Song, Z., Song, H., Liu, D., Yan, B., Wang, D., Zhang, Y., Zhao, X., Tian, X., Yan, C., & Han, Y. (2022) · Theranostics · doi:10.7150/thno.65716 · Cited by 115 · see citing works
Endoplasmic reticulum–mitochondria signaling in neurons and neurodegenerative diseases
Markovinović, A., Greig, J., Martín‐Guerrero, S. M., Salam, S., & Paillusson, S. (2022) · Journal of Cell Science · doi:10.1242/jcs.248534 · Cited by 114 · see citing works
Insights into SGLT2 inhibitor treatment of diabetic cardiomyopathy: focus on the mechanisms
Huang, K., Luo, X., Liao, B., Li, G., & Feng, J. (2023) · Cardiovascular Diabetology · doi:10.1186/s12933-023-01816-5 · Cited by 112 · see citing works
Wei, X., Wei, X., Lu, Z., Li, L., Hu, Y., Sun, F., Jiang, Y., Ma, H., Zheng, H., Yang, G., et al. (2020) · Metabolism · doi:10.1016/j.metabol.2020.154182 · Cited by 109 · see citing works
Ma, W., Sun, X., Zhu, Y., & Liu, N. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03162-w · Cited by 108 · see citing works
Luan, Y., Luan, Y., Yuan, R., Feng, Q., Chen, X., & Yang, Y. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/4578809 · Cited by 105 · see citing works
Mu, J., Zhang, D., Tian, Y., Xie, Z., & Zou, M. (2020) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2020.09.003 · Cited by 102 · see citing works
Mitophagy in Diabetic Cardiomyopathy: Roles and Mechanisms
Zheng, H., Zhu, H., Liu, X., Huang, X., Huang, A., & Huang, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.750382 · Cited by 100 · see citing works
Lu, J. G., Chen, P. P., Zhang, J. X., Li, X. Q., Wang, G. H., Yuan, B. Y., Huang, S. J., Liu, X. Q., Jiang, T., Wang, M. Y., et al. (2021) · Theranostics · doi:10.7150/thno.56598 · Cited by 95 · see citing works
Cheng, H., Gang, X., He, G., Liu, Y., Wang, Y., Zhao, X. Y., & Wang, G. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.592129 · Cited by 88 · see citing works
Li, G., Li, J., Shao, R., Zhao, J., & Chen, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.788634 · Cited by 88 · see citing works
Yang, H., Jiang, H., Tao, J., Zhang, C., Xiong, J., Yang, J., Liu, Y., Zhong, W., Guan, X., Duan, J., et al. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00889-8 · Cited by 88 · see citing works
Liu, Y., Qi, Z., Ling, M., Ma, R., Chen, H., Lin, F., Zhao, L., & Pan, L. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.729094 · Cited by 86 · see citing works
Li, Y. E., Sowers, J. R., Hetz, C. A., & Ren, J. T. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04942-2 · Cited by 86 · see citing works
Zhang, W. (2020) · Genes & Diseases · doi:10.1016/j.gendis.2020.08.011 · Cited by 81 · see citing works
The role of FUNDC1 in mitophagy, mitochondrial dynamics and human diseases
Liu, H., Zang, C., Yuan, F., Ju, C., Shang, M., Ning, J., Yang, Y., Ma, J., Li, G. L., Bao, X., et al. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114891 · Cited by 81 · see citing works
Zhang, N., Yu, H., Liu, T., Zhou, Z., Feng, B., Wang, Y., Qian, Z., Hou, X., & Zou, J. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102788 · Cited by 81 · see citing works
Ferroptosis at the nexus of metabolism and metabolic diseases
Li, S. Y., Zhang, G., Hu, J., Tian, Y., & Fu, X. (2024) · Theranostics · doi:10.7150/thno.100080 · Cited by 79 · see citing works
Mitochondrial quality control in cardiomyocytes: safeguarding the heart against disease and ageing
Ravindran, R., & Gustafsson, Å. B. (2025) · Nature Reviews Cardiology · doi:10.1038/s41569-025-01142-1 · Cited by 86 · see citing works
Zhou, Q., Yang, J., Wang, W., Shao, C., Hua, X., & Tang, Y. (2023) · Cardiovascular Diabetology · doi:10.1186/s12933-023-01908-2 · Cited by 81 · see citing works
Relationship between stress hyperglycaemic ratio (SHR) and critical illness: a systematic review
Song, G., Liu, X., Lu, Z., Guan, J., Chen, X., Li, Y., Liu, G., Wang, G., & Ma, F. (2025) · Cardiovascular Diabetology · doi:10.1186/s12933-025-02751-3 · Cited by 88 · see citing works
ER membranes associated with mitochondria: Possible therapeutic targets in heart-associated diseases
Silva‐Palacios, A., Zazueta, C., & Pedraza‐Chaverrí, J. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104758 · Cited by 74 · see citing works
He, Q., Qu, M., Shen, T., Su, J.-K., Xu, Y., Xu, C.-Y., Barkat, M., Cai, J.-B., Zhu, H.-B., Zeng, L.-H., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101920 · Cited by 75 · see citing works
Liu, Y., Huo, J., Ren, K., Pan, S., Liu, H., Zheng, Y., Chen, J., Qiao, Y., Yang, Y., & Feng, Q. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01918-3 · Cited by 72 · see citing works
Dludla, P. V., Nkambule, B. B., Mazibuko-Mbeje, S. E., Nyambuya, T. M., Marcheggiani, F., Cirilli, I., Ziqubu, K., Shabalala, S. C., Johnson, R., Louw, J., et al. (2020) · Antioxidants · doi:10.3390/antiox9121283 · Cited by 69 · see citing works
Exercise protects aged mice against coronary endothelial senescence via FUNDC1-dependent mitophagy
Ma, L., Li, K., Wei, W., Zhou, J., Li, Z., Zhang, T., Wangsun, Y., Tian, F., Dong, Q., Zhang, H., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102693 · Cited by 67 · see citing works
Li, A., Lian, L., Chen, X.-N., Cai, W.-H., Fan, X., Fan, Y.-J., Li, T., Xie, Y., & Zhang, J. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.08.009 · Cited by 67 · see citing works
He, W., Sun, Z., Tong, G., Zeng, L., He, W., Chen, X., Zhen, C., Chen, P., Tan, N., & He, P. (2024) · Theranostics · doi:10.7150/thno.92771 · Cited by 66 · see citing works
Zhang, D., Ning, J., Ramprasath, T., Yu, C., Zheng, X., Song, P., Xie, Z., & Zou, M. (2022) · Nature Communications · doi:10.1038/s41467-022-33734-7 · Cited by 64 · see citing works
RetractedChang, Y., Wang, C., Zhu, J., Zheng, S., Sun, S., Wu, Y., Jiang, X., Li, L., Ma, R., & Li, G. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04246-9 · Cited by 65 · see citing works
Xue, M., Fang, T., Sun, H., Cheng, Y., Li, T., Xu, C., Tang, C., Liu, X., Sun, B., & Chen, L. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04408-x · Cited by 65 · see citing works
Gong, Y., Lin, J., Ma, Z., Yu, M., Wang, M., Lai, D., & Fu, G. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119511 · Cited by 58 · see citing works
Liu, Y., Lin, S., Xu, Z., Wu, Y., Wang, G., Yang, G., Cao, L., Chang, H., Zhou, M., & Jiang, X. (2024) · Advanced Science · doi:10.1002/advs.202309491 · Cited by 57 · see citing works
Mitophagy in Cell Death Regulation: Insights into Mechanisms and Disease Implications
Lin, J., Chen, X., Du, Y., Li, J., Tingting, G., & Luo, S. (2024) · Biomolecules · doi:10.3390/biom14101270 · Cited by 60 · see citing works
Imbalance of ER and Mitochondria Interactions: Prelude to Cardiac Ageing and Disease?
Li, J., Zhang, D., Brundel, B. J. J. M., & Wiersma, M. (2019) · Cells · doi:10.3390/cells8121617 · Cited by 55 · see citing works
Wang, X., Zhang, X., Cao, K. J., Zeng, M., Fu, X., Zheng, A., Zhang, F., Gao, F., Zou, X., Li, H., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31548-1 · Cited by 57 · see citing works
Targeting mitochondrial shape: at the heart of cardioprotection
Hernández‐Reséndiz, S., Prakash, A., Loo, S. J., Semenzato, M., Chinda, K., Crespo-Avilan, G. E., Dam, L. C., Lu, S., Scorrano, L., & Hausenloy, D. J. (2023) · Basic Research in Cardiology · doi:10.1007/s00395-023-01019-9 · Cited by 55 · see citing works
Jiang, T., Peng, D., Shi, W., Guo, J., Huo, S., Men, L., Zhang, C., Li, S., Lv, J., & Lin, L. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.790612 · Cited by 54 · see citing works
Lipid Metabolism at Membrane Contacts: Dynamics and Functions Beyond Lipid Homeostasis
Xu, J., & Huang, X. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.615856 · Cited by 54 · see citing works
Tao, L., Huang, X., Xu, M., Yang, L., & Hua, F. (2019) · The FASEB Journal · doi:10.1096/fj.201901838r · Cited by 53 · see citing works
Yao, S., Wei, X., Deng, W., Wang, B., Cai, J., Huang, Y., Lai, X., Qiu, Y., Wang, Y., Guan, Y., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31755-w · Cited by 49 · see citing works
Chang, P., Zhang, X., Zhang, J., Wang, J., Wang, X., Li, M., Wang, R., Yu, J., & Fu, F. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102702 · Cited by 49 · see citing works
Hui, Y., Xu, Z., Li, J., Kuang, L., Zhong, Y., Tang, Y., Wei, J., Zhou, H., & Zheng, T. (2022) · Metabolism · doi:10.1016/j.metabol.2022.155340 · Cited by 48 · see citing works
Standpoints in mitochondrial dysfunction: Underlying mechanisms in search of therapeutic strategies
Videla, L. A., Mariman, A. P., Ramos, B., Silva, M. J., & del Campo, A. (2022) · Mitochondrion · doi:10.1016/j.mito.2021.12.006 · Cited by 48 · see citing works
Sarcoplasmic reticulum and calcium signaling in muscle cells: Homeostasis and disease
Bravo, R., Parra, V., Muñoz‐Córdova, F., Sánchez-Aguilera, P., Garrido, V., Contreras‐Ferrat, A. E., Chiong, M., & Lavandero, S. (2020) · International review of cytology · doi:10.1016/bs.ircmb.2019.12.007 · Cited by 46 · see citing works
Tan, Y., Zhang, Y., He, J., Wu, F., Wu, D., Shi, N., Liu, W., Li, Z., Liu, W., Zhou, H., et al. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101567 · Cited by 47 · see citing works
Gu, J., Zhang, T., Guo, J., Chen, K., Li, H., & Wang, J. (2020) · Shock · doi:10.1097/shk.0000000000001534 · Cited by 44 · see citing works
Mao, S., Tian, S., Luo, X., Zhou, M., Cao, Z., & Li, J. (2021) · Bioengineered · doi:10.1080/21655979.2021.1938500 · Cited by 45 · see citing works
Wang, Y., Zhang, X., Wen, Y., Li, S., Lu, X., Xu, R., & Li, C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.774989 · Cited by 44 · see citing works
Li, Y., Li, H., Shao, J., Zhu, L., Xie, T., Cai, J., Wang, W., Cai, M.-X., Wang, Z., Yao, Y., et al. (2022) · Biomolecules · doi:10.3390/biom12121778 · Cited by 43 · see citing works
Zhang, L., Wang, Y., Ju, J., Shabanova, A., Li, Y., Fang, R., Sun, J., Guo, Y., Jin, T., Liu, Y., et al. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0489-0 · Cited by 42 · see citing works
Xie, S., Zhang, M., Shi, W., Xing, Y., Huang, Y. Q., Fang, W., Liu, S., Chen, M., Zhang, T., Chen, S., et al. (2022) · Journal of the American Heart Association · doi:10.1161/jaha.122.026728 · Cited by 41 · see citing works
Canagliflozin Mitigates Diabetic Cardiomyopathy through Enhanced PINK1-Parkin Mitophagy
Yang, C., Xiao, C., Ding, Z., Zhai, X., Liu, J. Y., & Yu, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137008 · Cited by 41 · see citing works
Tang, X., Wang, Z., Hu, S., & Zhou, B. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14071313 · Cited by 40 · see citing works
Zhong, W., Wang, X., Yang, L., Wang, Y., Xiao, Q., Yu, S., Cannon, R. D., Bai, Y., Zhang, C., Chen, D., et al. (2022) · ACS Nano · doi:10.1021/acsnano.2c08146 · Cited by 40 · see citing works
Angebault, C., Panel, M., Lacôte, M., Rieusset, J., Lacampagne, A., & Fauconnier, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.609493 · Cited by 40 · see citing works
Jiang, T., Ruan, N., Luo, P., Wang, Q., Wei, X., Li, Y., Dai, Y., Li, L., Lv, J., Liu, Y., et al. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102320 · Cited by 41 · see citing works
Rani, M. R. P., Raj, P. S., Nair, A., Ranjith, S., Rajankutty, K., & Raghu, K. G. (2021) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2021.109755 · Cited by 39 · see citing works
Raj, P. S., Nair, A., Rani, M. R. P., Rajankutty, K., Ranjith, S., & Raghu, K. G. (2022) · International Journal of Cardiology · doi:10.1016/j.ijcard.2022.12.003 · Cited by 38 · see citing works
Chen, C., Dai, G., Fan, M., Wang, X., Niu, K., & Gao, W. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06262-3 · Cited by 38 · see citing works
Mitochondria‐Associated Endoplasmic Reticulum Membranes in Human Health and Diseases
Liu, Y., Mao, Z., Huang, J., Wang, H., Zhang, X., Zhou, X., Xu, Y., Pan, S., Liu, D., Liu, Z., et al. (2025) · MedComm · doi:10.1002/mco2.70259 · Cited by 41 · see citing works
Wang, H., Gong, J., Chen, W., Sun, Q., Zhang, T., Lin, Y., & Cai, X. (2024) · Nano Today · doi:10.1016/j.nantod.2024.102252 · Cited by 37 · see citing works
The role of mitochondria in metabolic disease: a special emphasis on heart dysfunction
Federico, M., de la Fuente, S., Palomeque, J., & Sheu, S. (2021) · The Journal of Physiology · doi:10.1113/jp279376 · Cited by 37 · see citing works
Trujillo-Rangel, W. Á., García-Valdés, L., Villar, M. M.-D., Castañeda‐Arellano, R., Totsuka-Sutto, S. E., & García‐Benavides, L. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/8624318 · Cited by 36 · see citing works
LonP1 Links Mitochondria–ER Interaction to Regulate Heart Function
Li, Y., Huang, D., Jia, L., Shangguan, F., Gong, S., Lan, L., Song, Z., Xu, J., Yan, C., Chen, T., et al. (2023) · Research · doi:10.34133/research.0175 · Cited by 38 · see citing works
Jiang, Y., & Zhang, Q. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8743 · Cited by 36 · see citing works
Zhang, Y., Zhang, T., Li, Y., Yu, C., Liu, B., Tian, Y., Wu, P., & Shi, H. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114055 · Cited by 36 · see citing works
Gong, Y., Lu, X., Wang, X. T., Wang, Y., Shen, Z., Gao, Y., Zhuang, L., Yu, L., Chen, J. C., Li, Q., et al. (2025) · Circulation · doi:10.1161/circulationaha.124.069737 · Cited by 35 · see citing works
Structural and Functional Remodeling of Mitochondria in Cardiac Diseases
Sun, X., Alford, J., & Qiu, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22084167 · Cited by 35 · see citing works
Bai, X., Zhang, Z., Li, X., Yang, Y., & Ding, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119151 · Cited by 34 · see citing works
The Emerging Role of FUNDC1-Mediated Mitophagy in Cardiovascular Diseases
Liu, L., Li, Y., & Chen, Q. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.807654 · Cited by 34 · see citing works
de Giusti, C. J., Palomeque, J., & MATTIAZZI, A. R. (2022) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-021-02650-y · Cited by 34 · see citing works
Sapian, S., Taib, I. S., Latip, J., Katas, H., Chin, K., Nor, N. A. M., Jubaidi, F. F., & Budin, S. B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111616 · Cited by 34 · see citing works
Zou, F., Wang, L., Liu, H., Wang, W., Hu, L., Xiong, X., Wu, L., Shen, Y., & Yang, R. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01219 · Cited by 33 · see citing works
Mitochondria-associated endoplasmic reticulum membranes in the heart
Wu, S., & Zou, M. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.12.018 · Cited by 32 · see citing works
Dubois, M., Boulghobra, D., Rochebloine, G., Pallot, F., Yehya, M., Bornard, I., Gayrard, S., Coste, F., Walther, G., Meyer, G., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103044 · Cited by 31 · see citing works
Xu, H., Yu, W., Sun, M., Bi, Y., Wu, N. N., Zhou, Y., Yang, Q., Zhang, M., Ge, J., Zhang, Y., et al. (2023) · Metabolism · doi:10.1016/j.metabol.2023.155551 · Cited by 31 · see citing works
New therapeutic directions in type II diabetes and its complications: mitochondrial dynamics
Wang, S., Zhao, H., Lin, S., Lv, Y., Lin, Y. N., Liu, Y., Peng, R., & Jin, H. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1230168 · Cited by 32 · see citing works
Ye, W., Han, K., Xie, M., Li, S., Chen, G., Wang, Y., & Li, T. (2024) · Chinese Medical Journal · doi:10.1097/cm9.0000000000003075 · Cited by 30 · see citing works
- Authors
- Wu, S., Lu, Q., Ding, Y., Wu, Y., Qiu, Y., Wang, P., Mao, X., Huang, K., Xie, Z., & Zou, M.-H.
- Affiliations
- Georgia State University (US)
- University of Washington (US)
- Wuhan Union Hospital (CN)
- Corresponding author
- Xie, Zhonglin
- Zou, Ming-Hui
- Venue
- Circulation
- Published
- 2019-04-16
- Volume
- 139
- Issue
- 16
- Pages
- 1913-1936
- ISSN
- 0009-7322 (ISSN-L)
- 1524-4539
- PMC
- PMC6465113
- OpenAlex
- W2911037090
- Cited by
- 298
- References
- 78
- Citations by year
- 2026: 37 · 2025: 48 · 2024: 55 · 2023: 43 · 2022: 47 · 2021: 27 · 2020: 32 · 2019: 8 · 2018: 1
- FWCI
- 9.43
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Circulation (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- American Heart Association (16POST31160009, 16GRANT29590003, 16POST29960011)
- University of Washington
- Georgia Research Alliance
- National Institute on Aging (AG047776, R01AG047776)
- National Heart, Lung, and Blood Institute (HL128014, HL137371, R01HL105157, HL 079584, R01HL079584, HL110488, HL140954, HL-080499, R01HL142287, R01HL137371, R01HL132500, R01HL074399, R01HL080499, HL132500, HL-089920, R01HL140954, R01HL110488, HL142287, R01HL128014, R01HL089920, CA213022, R01HL096032)
- National Cancer Institute (CA-213022, R01CA213022)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiovascular Function and Risk Factors
- Keywords
- diabetic cardiomyopathy, hyperglycemia, FUNDC1, mitochondria-associated endoplasmic reticulum membranes, IP3R2, mitochondrial calcium flux, mitophagy, AMPK, mitochondrial dysfunction, cardiomyocytes, streptozotocin-induced diabetes, Akita mice, cardiomyocyte-specific knockout, apoptosis, mitochondrial fragmentation, ubiquitination
- MeSH terms
- Adult, Aged, Animals, Cell Line, Endoplasmic Reticulum, Female, Gene Expression Regulation, Humans, Male, Membrane Proteins, Mice, Inbred C57BL, Middle Aged, Mitochondria, Myocardial Contraction, Mice, Knockout, Calcium Signaling, Mitochondrial Proteins, Myocytes, Cardiac, Mitochondrial Membranes, Mice, Rats, AMP-Activated Protein Kinases, Diabetic Cardiomyopathies
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