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Volumn 2, Issue , 2015, Pages

Pivotal Importance of STAT3 in Protecting the Heart from Acute and Chronic Stress: New Advancement and Unresolved Issues

Author keywords

cardiac hypertrophy; complex I; heart failure; ischemic pre and post conditioning; mitochondria; myocardial infarction; peripartum cardiomyopathy; U STAT3

Indexed keywords


EID: 84960424658     PISSN: None     EISSN: 2297055X     Source Type: Journal    
DOI: 10.3389/fcvm.2015.00036     Document Type: Review
Times cited : (72)

References (171)
  • 1
    • 84893395842 scopus 로고    scopus 로고
    • Dancing rhinos in stilettos: the amazing saga of the genomic and nongenomic actions of STAT3 in the heart
    • 24069556
    • Zouein FA, Kurdi M, Booz GW. Dancing rhinos in stilettos: the amazing saga of the genomic and nongenomic actions of STAT3 in the heart. JAKSTAT (2013) 2:e24352.10.4161/jkst.2435224069556
    • (2013) JAKSTAT , vol.2 , pp. e24352
    • Zouein, F.A.1    Kurdi, M.2    Booz, G.W.3
  • 2
    • 70350440089 scopus 로고    scopus 로고
    • JAK redux: a second look at the regulation and role of JAKs in the heart
    • 19717737
    • Kurdi M, Booz GW. JAK redux: a second look at the regulation and role of JAKs in the heart. Am J Physiol Heart Circ Physiol (2009) 297:H1545–56.10.1152/ajpheart.00032.200919717737
    • (2009) Am J Physiol Heart Circ Physiol , vol.297 , pp. H1545-H1556
    • Kurdi, M.1    Booz, G.W.2
  • 3
    • 34547951341 scopus 로고    scopus 로고
    • Can the protective actions of JAK-STAT in the heart be exploited therapeutically? Parsing the regulation of interleukin-6-type cytokine signaling
    • 17703129
    • Kurdi M, Booz GW. Can the protective actions of JAK-STAT in the heart be exploited therapeutically? Parsing the regulation of interleukin-6-type cytokine signaling. J Cardiovasc Pharmacol (2007) 50:126–41.10.1097/FJC.0b013e318068dd4917703129
    • (2007) J Cardiovasc Pharmacol , vol.50 , pp. 126-141
    • Kurdi, M.1    Booz, G.W.2
  • 4
    • 84864315728 scopus 로고    scopus 로고
    • Multi-tasking: nuclear transcription factors with novel roles in the mitochondria
    • 22705015
    • Szczepanek K, Lesnefsky EJ, Larner AC. Multi-tasking: nuclear transcription factors with novel roles in the mitochondria. Trends Cell Biol (2012) 22:429–37.10.1016/j.tcb.2012.05.00122705015
    • (2012) Trends Cell Biol , vol.22 , pp. 429-437
    • Szczepanek, K.1    Lesnefsky, E.J.2    Larner, A.C.3
  • 5
    • 84858007745 scopus 로고    scopus 로고
    • Cytoprotection by the modulation of mitochondrial electron transport chain: the emerging role of mitochondrial STAT3
    • 21930250
    • Szczepanek K, Chen Q, Larner AC, Lesnefsky EJ. Cytoprotection by the modulation of mitochondrial electron transport chain: the emerging role of mitochondrial STAT3. Mitochondrion (2012) 12:180–9.10.1016/j.mito.2011.08.01121930250
    • (2012) Mitochondrion , vol.12 , pp. 180-189
    • Szczepanek, K.1    Chen, Q.2    Larner, A.C.3    Lesnefsky, E.J.4
  • 6
    • 84928623386 scopus 로고    scopus 로고
    • Inhibition of mammalian target of rapamycin protects against reperfusion injury in diabetic heart through STAT3 signaling
    • 25911189
    • Das A, Salloum FN, Filippone SM, Durrant DE, Rokosh G, Bolli R, et al. Inhibition of mammalian target of rapamycin protects against reperfusion injury in diabetic heart through STAT3 signaling. Basic Res Cardiol (2015) 110:31.10.1007/s00395-015-0486-525911189
    • (2015) Basic Res Cardiol , vol.110 , pp. 31
    • Das, A.1    Salloum, F.N.2    Filippone, S.M.3    Durrant, D.E.4    Rokosh, G.5    Bolli, R.6
  • 7
    • 79958108043 scopus 로고    scopus 로고
    • Diabetes blockade of sevoflurane postconditioning is not restored by insulin in the rat heart: phosphorylated signal transducer and activator of transcription 3- and phosphatidylinositol 3-kinase-mediated inhibition
    • 21368653
    • Drenger B, Ostrovsky IA, Barak M, Nechemia-Arbely Y, Ziv E, Axelrod JH. Diabetes blockade of sevoflurane postconditioning is not restored by insulin in the rat heart: phosphorylated signal transducer and activator of transcription 3- and phosphatidylinositol 3-kinase-mediated inhibition. Anesthesiology (2011) 114:1364–72.10.1097/ALN.0b013e31820efafd21368653
    • (2011) Anesthesiology , vol.114 , pp. 1364-1372
    • Drenger, B.1    Ostrovsky, I.A.2    Barak, M.3    Nechemia-Arbely, Y.4    Ziv, E.5    Axelrod, J.H.6
  • 8
    • 37849023059 scopus 로고    scopus 로고
    • Cardioprotection by ischemic postconditioning is lost in aged and STAT3-deficient mice
    • 17967780
    • Boengler K, Buechert A, Heinen Y, Roeskes C, Hilfiker-Kleiner D, Heusch G, et al. Cardioprotection by ischemic postconditioning is lost in aged and STAT3-deficient mice. Circ Res (2008) 102:131–5.10.1161/CIRCRESAHA.107.16469917967780
    • (2008) Circ Res , vol.102 , pp. 131-135
    • Boengler, K.1    Buechert, A.2    Heinen, Y.3    Roeskes, C.4    Hilfiker-Kleiner, D.5    Heusch, G.6
  • 9
    • 53749100817 scopus 로고    scopus 로고
    • The myocardial JAK/STAT pathway: from protection to failure
    • 18786563
    • Boengler K, Hilfiker-Kleiner D, Drexler H, Heusch G, Schulz R. The myocardial JAK/STAT pathway: from protection to failure. Pharmacol Ther (2008) 120:172–85.10.1016/j.pharmthera.2008.08.00218786563
    • (2008) Pharmacol Ther , vol.120 , pp. 172-185
    • Boengler, K.1    Hilfiker-Kleiner, D.2    Drexler, H.3    Heusch, G.4    Schulz, R.5
  • 10
    • 0037448803 scopus 로고    scopus 로고
    • Alterations in Janus kinase (JAK)-signal transducers and activators of transcription (STAT) signaling in patients with end-stage dilated cardiomyopathy
    • 12591746
    • Podewski EK, Hilfiker-Kleiner D, Hilfiker A, Morawietz H, Lichtenberg A, Wollert KC, et al. Alterations in Janus kinase (JAK)-signal transducers and activators of transcription (STAT) signaling in patients with end-stage dilated cardiomyopathy. Circulation (2003) 107:798–802.10.1161/01.CIR.0000057545.82749.FF12591746
    • (2003) Circulation , vol.107 , pp. 798-802
    • Podewski, E.K.1    Hilfiker-Kleiner, D.2    Hilfiker, A.3    Morawietz, H.4    Lichtenberg, A.5    Wollert, K.C.6
  • 11
    • 84864704976 scopus 로고    scopus 로고
    • Impaired JAK2-induced activation of STAT3 in failing human myocytes
    • 22735740
    • Cambi GE, Lucchese G, Djeokeng MM, Modesti A, Fiaschi T, Faggian G, et al. Impaired JAK2-induced activation of STAT3 in failing human myocytes. Mol Biosyst (2012) 8:2351–9.10.1039/c2mb25120e22735740
    • (2012) Mol Biosyst , vol.8 , pp. 2351-2359
    • Cambi, G.E.1    Lucchese, G.2    Djeokeng, M.M.3    Modesti, A.4    Fiaschi, T.5    Faggian, G.6
  • 12
    • 84858224724 scopus 로고    scopus 로고
    • 1a-adrenergic receptor differentially regulates STAT3 phosphorylation through PKCЄ and PKCδ in myocytes
    • 1a-adrenergic receptor differentially regulates STAT3 phosphorylation through PKCЄ and PKCδ in myocytes. J Recept Signal Transduct Res (2012) 32:76–86.10.3109/10799893.2011.647353
    • (2012) J Recept Signal Transduct Res , vol.32 , pp. 76-86
    • Shi, T.1    Papay, R.S.2    Perez, D.M.3
  • 13
    • 46849087232 scopus 로고    scopus 로고
    • STAT3 activation in pressure-overloaded feline myocardium: role for integrins and the tyrosine kinase BMX
    • 18612371
    • Willey CD, Palanisamy AP, Johnston RK, Mani SK, Shiraishi H, Tuxworth WJ, et al. STAT3 activation in pressure-overloaded feline myocardium: role for integrins and the tyrosine kinase BMX. Int J Biol Sci (2008) 4:184–99.10.7150/ijbs.4.18418612371
    • (2008) Int J Biol Sci , vol.4 , pp. 184-199
    • Willey, C.D.1    Palanisamy, A.P.2    Johnston, R.K.3    Mani, S.K.4    Shiraishi, H.5    Tuxworth, W.J.6
  • 14
    • 67349278378 scopus 로고    scopus 로고
    • Native and reconstituted HDL activate Stat3 in ventricular cardiomyocytes via ERK1/2: role of sphingosine-1-phosphate
    • 19151362
    • Frias MA, James RW, Gerber-Wicht C, Lang U. Native and reconstituted HDL activate Stat3 in ventricular cardiomyocytes via ERK1/2: role of sphingosine-1-phosphate. Cardiovasc Res (2009) 82:313–23.10.1093/cvr/cvp02419151362
    • (2009) Cardiovasc Res , vol.82 , pp. 313-323
    • Frias, M.A.1    James, R.W.2    Gerber-Wicht, C.3    Lang, U.4
  • 15
    • 84938903813 scopus 로고    scopus 로고
    • SH2B1 is critical for the regulation of cardiac remodelling in response to pressure overload
    • 26077624
    • Wu G, Liu Y, Huang H, Tang Y, Liu W, Mei Y, et al. SH2B1 is critical for the regulation of cardiac remodelling in response to pressure overload. Cardiovasc Res (2015) 107:203–15.10.1093/cvr/cvv17026077624
    • (2015) Cardiovasc Res , vol.107 , pp. 203-215
    • Wu, G.1    Liu, Y.2    Huang, H.3    Tang, Y.4    Liu, W.5    Mei, Y.6
  • 16
    • 84871598386 scopus 로고    scopus 로고
    • Pressure mediated hypertrophy and mechanical stretch up-regulate expression of the long form of leptin receptor (ob-Rb) in rat cardiac myocytes
    • 23270329
    • Matsui H, Yokoyama T, Tanaka C, Sunaga H, Koitabashi N, Takizawa T, et al. Pressure mediated hypertrophy and mechanical stretch up-regulate expression of the long form of leptin receptor (ob-Rb) in rat cardiac myocytes. BMC Cell Biol (2012) 13:37.10.1186/1471-2121-13-3723270329
    • (2012) BMC Cell Biol , vol.13 , pp. 37
    • Matsui, H.1    Yokoyama, T.2    Tanaka, C.3    Sunaga, H.4    Koitabashi, N.5    Takizawa, T.6
  • 17
    • 79961031623 scopus 로고    scopus 로고
    • H11 kinase/heat shock protein 22 deletion impairs both nuclear and mitochondrial functions of STAT3 and accelerates the transition into heart failure on cardiac overload
    • 21747053
    • Qiu H, Lizano P, Laure L, Sui X, Rashed E, Park JY, et al. H11 kinase/heat shock protein 22 deletion impairs both nuclear and mitochondrial functions of STAT3 and accelerates the transition into heart failure on cardiac overload. Circulation (2011) 124:406–15.10.1161/CIRCULATIONAHA.110.01384721747053
    • (2011) Circulation , vol.124 , pp. 406-415
    • Qiu, H.1    Lizano, P.2    Laure, L.3    Sui, X.4    Rashed, E.5    Park, J.Y.6
  • 18
    • 4544384693 scopus 로고    scopus 로고
    • Activation of distinct signal transduction pathways in hypertrophied hearts by pressure and volume overload
    • 15309410
    • Miyamoto T, Takeishi Y, Takahashi H, Shishido T, Arimoto T, Tomoike H, et al. Activation of distinct signal transduction pathways in hypertrophied hearts by pressure and volume overload. Basic Res Cardiol (2004) 99:328–37.10.1007/s00395-004-0482-715309410
    • (2004) Basic Res Cardiol , vol.99 , pp. 328-337
    • Miyamoto, T.1    Takeishi, Y.2    Takahashi, H.3    Shishido, T.4    Arimoto, T.5    Tomoike, H.6
  • 19
    • 0035933775 scopus 로고    scopus 로고
    • gp130 plays a critical role in pressure overload-induced cardiac hypertrophy
    • 11262406
    • Uozumi H, Hiroi Y, Zou Y, Takimoto E, Toko H, Niu P, et al. gp130 plays a critical role in pressure overload-induced cardiac hypertrophy. J Biol Chem (2001) 276:23115–9.10.1074/jbc.M10081420011262406
    • (2001) J Biol Chem , vol.276 , pp. 23115-23119
    • Uozumi, H.1    Hiroi, Y.2    Zou, Y.3    Takimoto, E.4    Toko, H.5    Niu, P.6
  • 20
    • 13044255533 scopus 로고    scopus 로고
    • Involvement of gp130-mediated signaling in pressure overload-induced activation of the JAK/STAT pathway in rodent heart
    • 10442402
    • Pan J, Fukuda K, Kodama H, Sano M, Takahashi T, Makino S, et al. Involvement of gp130-mediated signaling in pressure overload-induced activation of the JAK/STAT pathway in rodent heart. Heart Vessels (1998) 13:199–208.10.1007/BF0174504510442402
    • (1998) Heart Vessels , vol.13 , pp. 199-208
    • Pan, J.1    Fukuda, K.2    Kodama, H.3    Sano, M.4    Takahashi, T.5    Makino, S.6
  • 21
    • 0033612183 scopus 로고    scopus 로고
    • Mechanical stretch activates the JAK/STAT pathway in rat cardiomyocytes
    • 10347087
    • Pan J, Fukuda K, Saito M, Matsuzaki J, Kodama H, Sano M, et al. Mechanical stretch activates the JAK/STAT pathway in rat cardiomyocytes. Circ Res (1999) 84:1127–36.10.1161/01.RES.84.10.112710347087
    • (1999) Circ Res , vol.84 , pp. 1127-1136
    • Pan, J.1    Fukuda, K.2    Saito, M.3    Matsuzaki, J.4    Kodama, H.5    Sano, M.6
  • 22
    • 0030765570 scopus 로고    scopus 로고
    • Role of angiotensin II in activation of the JAK/STAT pathway induced by acute pressure overload in the rat heart
    • 9314843
    • Pan J, Fukuda K, Kodama H, Makino S, Takahashi T, Sano M, et al. Role of angiotensin II in activation of the JAK/STAT pathway induced by acute pressure overload in the rat heart. Circ Res (1997) 81:611–7.10.1161/01.RES.81.4.6119314843
    • (1997) Circ Res , vol.81 , pp. 611-617
    • Pan, J.1    Fukuda, K.2    Kodama, H.3    Makino, S.4    Takahashi, T.5    Sano, M.6
  • 23
    • 0036852779 scopus 로고    scopus 로고
    • Interplay between the cardiac renin angiotensin system and JAK-STAT signaling: role in cardiac hypertrophy, ischemia/reperfusion dysfunction, and heart failure
    • 12431443
    • Booz GW, Day JN, Baker KM. Interplay between the cardiac renin angiotensin system and JAK-STAT signaling: role in cardiac hypertrophy, ischemia/reperfusion dysfunction, and heart failure. J Mol Cell Cardiol (2002) 34:1443–53.10.1006/jmcc.2002.207612431443
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 1443-1453
    • Booz, G.W.1    Day, J.N.2    Baker, K.M.3
  • 24
    • 0034703035 scopus 로고    scopus 로고
    • Interleukin-6 family of cytokines mediate angiotensin II-induced cardiac hypertrophy in rodent cardiomyocytes
    • 10843995
    • Sano M, Fukuda K, Kodama H, Pan J, Saito M, Matsuzaki J, et al. Interleukin-6 family of cytokines mediate angiotensin II-induced cardiac hypertrophy in rodent cardiomyocytes. J Biol Chem (2000) 275:29717–23.10.1074/jbc.M00312820010843995
    • (2000) J Biol Chem , vol.275 , pp. 29717-29723
    • Sano, M.1    Fukuda, K.2    Kodama, H.3    Pan, J.4    Saito, M.5    Matsuzaki, J.6
  • 25
    • 38349138319 scopus 로고    scopus 로고
    • Angiotensin II activates signal transducer and activators of transcription 3 via Rac1 in atrial myocytes and fibroblasts: implication for the therapeutic effect of statin in atrial structural remodeling
    • 18172037
    • Tsai CT, Lai LP, Kuo KT, Hwang JJ, Hsieh CS, Hsu KL, et al. Angiotensin II activates signal transducer and activators of transcription 3 via Rac1 in atrial myocytes and fibroblasts: implication for the therapeutic effect of statin in atrial structural remodeling. Circulation (2008) 117:344–55.10.1161/CIRCULATIONAHA.107.69534618172037
    • (2008) Circulation , vol.117 , pp. 344-355
    • Tsai, C.T.1    Lai, L.P.2    Kuo, K.T.3    Hwang, J.J.4    Hsieh, C.S.5    Hsu, K.L.6
  • 26
    • 84878911382 scopus 로고    scopus 로고
    • Role of STAT3 in angiotensin II-induced hypertension and cardiac remodeling revealed by mice lacking STAT3 serine 727 phosphorylation
    • 23364341
    • Zouein FA, Zgheib C, Hamza S, Fuseler JW, Hall JE, Soljancic A, et al. Role of STAT3 in angiotensin II-induced hypertension and cardiac remodeling revealed by mice lacking STAT3 serine 727 phosphorylation. Hypertens Res (2013) 36:496–503.10.1038/hr.2012.22323364341
    • (2013) Hypertens Res , vol.36 , pp. 496-503
    • Zouein, F.A.1    Zgheib, C.2    Hamza, S.3    Fuseler, J.W.4    Hall, J.E.5    Soljancic, A.6
  • 27
    • 77958471611 scopus 로고    scopus 로고
    • Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation
    • 20798359
    • Iwasaki H, Kovacic JC, Olive M, Beers JK, Yoshimoto T, Crook MF, et al. Disruption of protein arginine N-methyltransferase 2 regulates leptin signaling and produces leanness in vivo through loss of STAT3 methylation. Circ Res (2010) 107:992–1001.10.1161/CIRCRESAHA.110.22532620798359
    • (2010) Circ Res , vol.107 , pp. 992-1001
    • Iwasaki, H.1    Kovacic, J.C.2    Olive, M.3    Beers, J.K.4    Yoshimoto, T.5    Crook, M.F.6
  • 28
    • 84961290058 scopus 로고    scopus 로고
    • STAT3-driven transcription depends upon the dimethylation of K49 by EZH2
    • 25767098
    • Dasgupta M, Dermawan JK, Willard B, Stark GR. STAT3-driven transcription depends upon the dimethylation of K49 by EZH2. Proc Natl Acad Sci U S A (2015) 112:3985–90.10.1073/pnas.150315211225767098
    • (2015) Proc Natl Acad Sci U S A , vol.112 , pp. 3985-3990
    • Dasgupta, M.1    Dermawan, J.K.2    Willard, B.3    Stark, G.R.4
  • 29
    • 27744499936 scopus 로고    scopus 로고
    • 2-terminal acetylation is activated by the hepatic acute-phase response and required for IL-6 induction of angiotensinogen
    • 16285960
    • 2-terminal acetylation is activated by the hepatic acute-phase response and required for IL-6 induction of angiotensinogen. Gastroenterology (2005) 129:1616–32.10.1053/j.gastro.2005.07.05516285960
    • (2005) Gastroenterology , vol.129 , pp. 1616-1632
    • Ray, S.1    Boldogh, I.2    Brasier, A.R.3
  • 30
    • 57649155188 scopus 로고    scopus 로고
    • 2-terminal domain stabilizes enhanceosome assembly by interacting with the p300 bromodomain
    • 18782771
    • 2-terminal domain stabilizes enhanceosome assembly by interacting with the p300 bromodomain. J Biol Chem (2008) 283:30725–34.10.1074/jbc.M80594120018782771
    • (2008) J Biol Chem , vol.283 , pp. 30725-30734
    • Hou, T.1    Ray, S.2    Lee, C.3    Brasier, A.R.4
  • 31
    • 48349105443 scopus 로고    scopus 로고
    • Requirement of histone deacetylase1 (HDAC1) in signal transducer and activator of transcription 3 (STAT3) nucleocytoplasmic distribution
    • 18611949
    • Ray S, Lee C, Hou T, Boldogh I, Brasier AR. Requirement of histone deacetylase1 (HDAC1) in signal transducer and activator of transcription 3 (STAT3) nucleocytoplasmic distribution. Nucleic Acids Res (2008) 36:4510–20.10.1093/nar/gkn41918611949
    • (2008) Nucleic Acids Res , vol.36 , pp. 4510-4520
    • Ray, S.1    Lee, C.2    Hou, T.3    Boldogh, I.4    Brasier, A.R.5
  • 32
    • 84864327504 scopus 로고    scopus 로고
    • The Sin3a repressor complex is a master regulator of STAT transcriptional activity
    • 22783022
    • Icardi L, Mori R, Gesellchen V, Eyckerman S, De Cauwer L, Verhelst J, et al. The Sin3a repressor complex is a master regulator of STAT transcriptional activity. Proc Natl Acad Sci U S A (2012) 109:12058–63.10.1073/pnas.120645810922783022
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 12058-12063
    • Icardi, L.1    Mori, R.2    Gesellchen, V.3    Eyckerman, S.4    De Cauwer, L.5    Verhelst, J.6
  • 33
    • 84897486329 scopus 로고    scopus 로고
    • 2 terminal mono-ubiquitination promotes BRD4 complex formation to regulate apoptosis
    • 24657799
    • 2 terminal mono-ubiquitination promotes BRD4 complex formation to regulate apoptosis. Cell Signal (2014) 26:1445–55.10.1016/j.cellsig.2014.03.00724657799
    • (2014) Cell Signal , vol.26 , pp. 1445-1455
    • Ray, S.1    Zhao, Y.2    Jamaluddin, M.3    Edeh, C.B.4    Lee, C.5    Brasier, A.R.6
  • 34
    • 78650717706 scopus 로고    scopus 로고
    • Reversible methylation of promoter-bound STAT3 by histone-modifying enzymes
    • 21098664
    • Yang J, Huang J, Dasgupta M, Sears N, Miyagi M, Wang B, et al. Reversible methylation of promoter-bound STAT3 by histone-modifying enzymes. Proc Natl Acad Sci U S A (2010) 107:21499–504.10.1073/pnas.101614710721098664
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 21499-21504
    • Yang, J.1    Huang, J.2    Dasgupta, M.3    Sears, N.4    Miyagi, M.5    Wang, B.6
  • 35
    • 84879000598 scopus 로고    scopus 로고
    • Phosphorylation of EZH2 activates STAT3 signaling via STAT3 methylation and promotes tumorigenicity of glioblastoma stem-like cells
    • 23684459
    • Kim E, Kim M, Woo DH, Shin Y, Shin J, Chang N, et al. Phosphorylation of EZH2 activates STAT3 signaling via STAT3 methylation and promotes tumorigenicity of glioblastoma stem-like cells. Cancer Cell (2013) 23:839–52.10.1016/j.ccr.2013.04.00823684459
    • (2013) Cancer Cell , vol.23 , pp. 839-852
    • Kim, E.1    Kim, M.2    Woo, D.H.3    Shin, Y.4    Shin, J.5    Chang, N.6
  • 36
    • 84900403543 scopus 로고    scopus 로고
    • STAT3 regulation by S-nitrosylation: implication for inflammatory disease
    • 24063605
    • Kim J, Won JS, Singh AK, Sharma AK, Singh I. STAT3 regulation by S-nitrosylation: implication for inflammatory disease. Antioxid Redox Signal (2014) 20:2514–27.10.1089/ars.2013.522324063605
    • (2014) Antioxid Redox Signal , vol.20 , pp. 2514-2527
    • Kim, J.1    Won, J.S.2    Singh, A.K.3    Sharma, A.K.4    Singh, I.5
  • 37
  • 38
    • 0036217995 scopus 로고    scopus 로고
    • Angiotensinogen gene expression is dependent on signal transducer and activator of transcription 3-mediated p300/cAMP response element binding protein-binding protein coactivator recruitment and histone acetyltransferase activity
    • 11923478
    • Ray S, Sherman CT, Lu M, Brasier AR. Angiotensinogen gene expression is dependent on signal transducer and activator of transcription 3-mediated p300/cAMP response element binding protein-binding protein coactivator recruitment and histone acetyltransferase activity. Mol Endocrinol (2002) 16:824–36.10.1210/mend.16.4.081111923478
    • (2002) Mol Endocrinol , vol.16 , pp. 824-836
    • Ray, S.1    Sherman, C.T.2    Lu, M.3    Brasier, A.R.4
  • 39
    • 15744385061 scopus 로고    scopus 로고
    • Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation
    • 15649887
    • Wang R, Cherukuri P, Luo J. Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation. J Biol Chem (2005) 280:11528–34.10.1074/jbc.M41393020015649887
    • (2005) J Biol Chem , vol.280 , pp. 11528-11534
    • Wang, R.1    Cherukuri, P.2    Luo, J.3
  • 40
    • 84861215508 scopus 로고    scopus 로고
    • Acetylated STAT3 is crucial for methylation of tumor-suppressor gene promoters and inhibition by resveratrol results in demethylation
    • 22547799
    • Lee H, Zhang P, Herrmann A, Yang C, Xin H, Wang Z, et al. Acetylated STAT3 is crucial for methylation of tumor-suppressor gene promoters and inhibition by resveratrol results in demethylation. Proc Natl Acad Sci U S A (2012) 109:7765–9.10.1073/pnas.120513210922547799
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 7765-7769
    • Lee, H.1    Zhang, P.2    Herrmann, A.3    Yang, C.4    Xin, H.5    Wang, Z.6
  • 41
    • 84908364682 scopus 로고    scopus 로고
    • The STAT3-DNMT1 connection
    • 24058781
    • Thomas NS. The STAT3-DNMT1 connection. JAKSTAT (2012) 1:257–60.10.4161/jkst.2243624058781
    • (2012) JAKSTAT , vol.1 , pp. 257-260
    • Thomas, N.S.1
  • 42
    • 84908577138 scopus 로고    scopus 로고
    • Critical role for lysine 685 in gene expression mediated by transcription factor unphosphorylated STAT3
    • 25217633
    • Dasgupta M, Unal H, Willard B, Yang J, Karnik SS, Stark GR. Critical role for lysine 685 in gene expression mediated by transcription factor unphosphorylated STAT3. J Biol Chem (2014) 289:30763–71.10.1074/jbc.M114.60389425217633
    • (2014) J Biol Chem , vol.289 , pp. 30763-30771
    • Dasgupta, M.1    Unal, H.2    Willard, B.3    Yang, J.4    Karnik, S.S.5    Stark, G.R.6
  • 43
  • 44
    • 0035917876 scopus 로고    scopus 로고
    • Ser727-dependent transcriptional activation by association of p300 with STAT3 upon IL-6 stimulation
    • 11322950
    • Schuringa JJ, Schepers H, Vellenga E, Kruijer W. Ser727-dependent transcriptional activation by association of p300 with STAT3 upon IL-6 stimulation. FEBS Lett (2001) 495:71–6.10.1016/S0014-5793(01)02354-711322950
    • (2001) FEBS Lett , vol.495 , pp. 71-76
    • Schuringa, J.J.1    Schepers, H.2    Vellenga, E.3    Kruijer, W.4
  • 45
    • 84874066734 scopus 로고    scopus 로고
    • The import of the transcription factor STAT3 into mitochondria depends on GRIM-19, a component of the electron transport chain
    • 23271731
    • Tammineni P, Anugula C, Mohammed F, Anjaneyulu M, Larner AC, Sepuri NB. The import of the transcription factor STAT3 into mitochondria depends on GRIM-19, a component of the electron transport chain. J Biol Chem (2013) 288:4723–32.10.1074/jbc.M112.37898423271731
    • (2013) J Biol Chem , vol.288 , pp. 4723-4732
    • Tammineni, P.1    Anugula, C.2    Mohammed, F.3    Anjaneyulu, M.4    Larner, A.C.5    Sepuri, N.B.6
  • 46
    • 59849101586 scopus 로고    scopus 로고
    • Function of mitochondrial Stat3 in cellular respiration
    • Wegrzyn J, Potla R, Chwae YJ, Sepuri NB, Zhang Q, Koeck T, et al. Function of mitochondrial Stat3 in cellular respiration. Science (2009) 323:793–7.10.1126/science.1164551
    • (2009) Science , vol.323 , pp. 793-797
    • Wegrzyn, J.1    Potla, R.2    Chwae, Y.J.3    Sepuri, N.B.4    Zhang, Q.5    Koeck, T.6
  • 47
    • 84896691813 scopus 로고    scopus 로고
    • The MEK-ERK pathway is necessary for serine phosphorylation of mitochondrial STAT3 and Ras-mediated transformation
    • 24312439
    • Gough DJ, Koetz L, Levy DE. The MEK-ERK pathway is necessary for serine phosphorylation of mitochondrial STAT3 and Ras-mediated transformation. PLoS One (2013) 8:e83395.10.1371/journal.pone.008339524312439
    • (2013) PLoS One , vol.8 , pp. e83395
    • Gough, D.J.1    Koetz, L.2    Levy, D.E.3
  • 48
    • 84886678359 scopus 로고    scopus 로고
    • Mitochondrial localized Stat3 promotes breast cancer growth via phosphorylation of serine 727
    • 24019511
    • Zhang Q, Raje V, Yakovlev VA, Yacoub A, Szczepanek K, Meier J, et al. Mitochondrial localized Stat3 promotes breast cancer growth via phosphorylation of serine 727. J Biol Chem (2013) 288:31280–8.10.1074/jbc.M113.50505724019511
    • (2013) J Biol Chem , vol.288 , pp. 31280-31288
    • Zhang, Q.1    Raje, V.2    Yakovlev, V.A.3    Yacoub, A.4    Szczepanek, K.5    Meier, J.6
  • 49
    • 0037258756 scopus 로고    scopus 로고
    • Angiotensin II effects on STAT3 phosphorylation in cardiomyocytes: evidence for Erk-dependent Tyr705 dephosphorylation
    • 12494267
    • Booz GW, Day JN, Baker KM. Angiotensin II effects on STAT3 phosphorylation in cardiomyocytes: evidence for Erk-dependent Tyr705 dephosphorylation. Basic Res Cardiol (2003) 98:33–8.10.1007/s00395-003-0387-x12494267
    • (2003) Basic Res Cardiol , vol.98 , pp. 33-38
    • Booz, G.W.1    Day, J.N.2    Baker, K.M.3
  • 50
    • 84906316130 scopus 로고    scopus 로고
    • Cytokine-induced slowing of STAT3 nuclear import; faster basal trafficking of the STAT3β isoform
    • 24903907
    • Ng IH, Bogoyevitch MA, Jans DA. Cytokine-induced slowing of STAT3 nuclear import; faster basal trafficking of the STAT3β isoform. Traffic (2014) 15:946–60.10.1111/tra.1218124903907
    • (2014) Traffic , vol.15 , pp. 946-960
    • Ng, I.H.1    Bogoyevitch, M.A.2    Jans, D.A.3
  • 51
    • 0042925385 scopus 로고    scopus 로고
    • The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3
    • 12867595
    • Zhang J, Yang J, Roy SK, Tininini S, Hu J, Bromberg JF, et al. The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3. Proc Natl Acad Sci U S A (2003) 100:9342–7.10.1073/pnas.163351610012867595
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9342-9347
    • Zhang, J.1    Yang, J.2    Roy, S.K.3    Tininini, S.4    Hu, J.5    Bromberg, J.F.6
  • 52
    • 13744255376 scopus 로고    scopus 로고
    • Cell signaling. Stat acetylation – a key facet of cytokine signaling?
    • O’Shea JJ, Kanno Y, Chen X, Levy DE. Cell signaling. Stat acetylation – a key facet of cytokine signaling? Science (2005) 307:217–8.10.1126/science.1108164
    • (2005) Science , vol.307 , pp. 217-218
    • O’Shea, J.J.1    Kanno, Y.2    Chen, X.3    Levy, D.E.4
  • 53
    • 79952538100 scopus 로고    scopus 로고
    • Lysine methylation of promoter-bound transcription factors and relevance to cancer
    • 21151202
    • Stark GR, Wang Y, Lu T. Lysine methylation of promoter-bound transcription factors and relevance to cancer. Cell Res (2011) 21:375–80.10.1038/cr.2010.17421151202
    • (2011) Cell Res , vol.21 , pp. 375-380
    • Stark, G.R.1    Wang, Y.2    Lu, T.3
  • 55
    • 67649886861 scopus 로고    scopus 로고
    • S-glutathionylation impairs signal transducer and activator of transcription 3 activation and signaling
    • 18988672
    • Xie Y, Kole S, Precht P, Pazin MJ, Bernier M. S-glutathionylation impairs signal transducer and activator of transcription 3 activation and signaling. Endocrinology (2009) 150:1122–31.10.1210/en.2008-124118988672
    • (2009) Endocrinology , vol.150 , pp. 1122-1131
    • Xie, Y.1    Kole, S.2    Precht, P.3    Pazin, M.J.4    Bernier, M.5
  • 56
    • 84906214869 scopus 로고    scopus 로고
    • S-Glutathionylation at Cys328 and Cys542 impairs STAT3 phosphorylation
    • 24941337
    • Butturini E, Darra E, Chiavegato G, Cellini B, Cozzolino F, Monti M, et al. S-Glutathionylation at Cys328 and Cys542 impairs STAT3 phosphorylation. ACS Chem Biol (2014) 9:1885–93.10.1021/cb500407d24941337
    • (2014) ACS Chem Biol , vol.9 , pp. 1885-1893
    • Butturini, E.1    Darra, E.2    Chiavegato, G.3    Cellini, B.4    Cozzolino, F.5    Monti, M.6
  • 57
    • 4444375662 scopus 로고    scopus 로고
    • A STAT3 dimer formed by inter-chain disulphide bridging during oxidative stress
    • 15336564
    • Li L, Shaw PE. A STAT3 dimer formed by inter-chain disulphide bridging during oxidative stress. Biochem Biophys Res Commun (2004) 322:1005–11.10.1016/j.bbrc.2004.08.01415336564
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 1005-1011
    • Li, L.1    Shaw, P.E.2
  • 59
    • 78049300452 scopus 로고    scopus 로고
    • Modulation of gene expression and tumor cell growth by redox modification of STAT3
    • 20807804
    • Li L, Cheung SH, Evans EL, Shaw PE. Modulation of gene expression and tumor cell growth by redox modification of STAT3. Cancer Res (2010) 70:8222–32.10.1158/0008-5472.CAN-10-089420807804
    • (2010) Cancer Res , vol.70 , pp. 8222-8232
    • Li, L.1    Cheung, S.H.2    Evans, E.L.3    Shaw, P.E.4
  • 60
    • 84866522166 scopus 로고    scopus 로고
    • Depletion of cellular glutathione modulates LIF-induced JAK1-STAT3 signaling in cardiac myocytes
    • 22939972
    • Kurdi M, Sivakumaran V, Duhe RJ, Aon MA, Paolocci N, Booz GW. Depletion of cellular glutathione modulates LIF-induced JAK1-STAT3 signaling in cardiac myocytes. Int J Biochem Cell Biol (2012) 44:2106–15.10.1016/j.biocel.2012.08.01622939972
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 2106-2115
    • Kurdi, M.1    Sivakumaran, V.2    Duhe, R.J.3    Aon, M.A.4    Paolocci, N.5    Booz, G.W.6
  • 61
    • 84865053350 scopus 로고    scopus 로고
    • Acyloxy nitroso compounds inhibit LIF signaling in endothelial cells and cardiac myocytes: evidence that STAT3 signaling is redox-sensitive
    • 22905257
    • Zgheib C, Kurdi M, Zouein FA, Gunter BW, Stanley BA, Zgheib J, et al. Acyloxy nitroso compounds inhibit LIF signaling in endothelial cells and cardiac myocytes: evidence that STAT3 signaling is redox-sensitive. PLoS One (2012) 7:e43313.10.1371/journal.pone.004331322905257
    • (2012) PLoS One , vol.7 , pp. e43313
    • Zgheib, C.1    Kurdi, M.2    Zouein, F.A.3    Gunter, B.W.4    Stanley, B.A.5    Zgheib, J.6
  • 62
    • 84878075520 scopus 로고    scopus 로고
    • LIF and the heart: just another brick in the wall?
    • 23661360
    • Zouein FA, Kurdi M, Booz GW. LIF and the heart: just another brick in the wall? Eur Cytokine Netw (2013) 24:11–9.10.1684/ecn.2013.033523661360
    • (2013) Eur Cytokine Netw , vol.24 , pp. 11-19
    • Zouein, F.A.1    Kurdi, M.2    Booz, G.W.3
  • 63
    • 4043082106 scopus 로고    scopus 로고
    • Genetic depletion of cardiac myocyte STAT-3 abolishes classical preconditioning
    • 15306216
    • Smith RM, Suleman N, Lacerda L, Opie LH, Akira S, Chien KR, et al. Genetic depletion of cardiac myocyte STAT-3 abolishes classical preconditioning. Cardiovasc Res (2004) 63:611–6.10.1016/j.cardiores.2004.06.01915306216
    • (2004) Cardiovasc Res , vol.63 , pp. 611-616
    • Smith, R.M.1    Suleman, N.2    Lacerda, L.3    Opie, L.H.4    Akira, S.5    Chien, K.R.6
  • 64
    • 3342889421 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription 3 is required for myocardial capillary growth, control of interstitial matrix deposition, and heart protection from ischemic injury
    • 15192020
    • Hilfiker-Kleiner D, Hilfiker A, Fuchs M, Kaminski K, Schaefer A, Schieffer B, et al. Signal transducer and activator of transcription 3 is required for myocardial capillary growth, control of interstitial matrix deposition, and heart protection from ischemic injury. Circ Res (2004) 95:187–95.10.1161/01.RES.0000134921.50377.6115192020
    • (2004) Circ Res , vol.95 , pp. 187-195
    • Hilfiker-Kleiner, D.1    Hilfiker, A.2    Fuchs, M.3    Kaminski, K.4    Schaefer, A.5    Schieffer, B.6
  • 65
    • 23744438811 scopus 로고    scopus 로고
    • STAT3-mediated activation of myocardial capillary growth
    • 16099380
    • Hilfiker-Kleiner D, Limbourg A, Drexler H. STAT3-mediated activation of myocardial capillary growth. Trends Cardiovasc Med (2005) 15:152–7.10.1016/j.tcm.2005.05.00216099380
    • (2005) Trends Cardiovasc Med , vol.15 , pp. 152-157
    • Hilfiker-Kleiner, D.1    Limbourg, A.2    Drexler, H.3
  • 66
    • 0037155205 scopus 로고    scopus 로고
    • Cardiac-specific activation of signal transducer and activator of transcription 3 promotes vascular formation in the heart
    • 11744720
    • Osugi T, Oshima Y, Fujio Y, Funamoto M, Yamashita A, Negoro S, et al. Cardiac-specific activation of signal transducer and activator of transcription 3 promotes vascular formation in the heart. J Biol Chem (2002) 277:6676–81.10.1074/jbc.M10824620011744720
    • (2002) J Biol Chem , vol.277 , pp. 6676-6681
    • Osugi, T.1    Oshima, Y.2    Fujio, Y.3    Funamoto, M.4    Yamashita, A.5    Negoro, S.6
  • 67
    • 0034616028 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription 3 is required for glycoprotein 130-mediated induction of vascular endothelial growth factor in cardiac myocytes
    • 10744750
    • Funamoto M, Fujio Y, Kunisada K, Negoro S, Tone E, Osugi T, et al. Signal transducer and activator of transcription 3 is required for glycoprotein 130-mediated induction of vascular endothelial growth factor in cardiac myocytes. J Biol Chem (2000) 275:10561–6.10.1074/jbc.275.14.1056110744750
    • (2000) J Biol Chem , vol.275 , pp. 10561-10566
    • Funamoto, M.1    Fujio, Y.2    Kunisada, K.3    Negoro, S.4    Tone, E.5    Osugi, T.6
  • 68
    • 0035964305 scopus 로고    scopus 로고
    • Activation of signal transducer and activator of transcription 3 protects cardiomyocytes from hypoxia/reoxygenation-induced oxidative stress through the upregulation of manganese superoxide dismutase
    • 11524388
    • Negoro S, Kunisada K, Fujio Y, Funamoto M, Darville MI, Eizirik DL, et al. Activation of signal transducer and activator of transcription 3 protects cardiomyocytes from hypoxia/reoxygenation-induced oxidative stress through the upregulation of manganese superoxide dismutase. Circulation (2001) 104:979–81.10.1161/hc3401.09594711524388
    • (2001) Circulation , vol.104 , pp. 979-981
    • Negoro, S.1    Kunisada, K.2    Fujio, Y.3    Funamoto, M.4    Darville, M.I.5    Eizirik, D.L.6
  • 69
    • 79952070542 scopus 로고    scopus 로고
    • A murine model of inducible, cardiac-specific deletion of STAT3: its use to determine the role of STAT3 in the upregulation of cardioprotective proteins by ischemic preconditioning
    • 21223971
    • Bolli R, Stein AB, Guo Y, Wang OL, Rokosh G, Dawn B, et al. A murine model of inducible, cardiac-specific deletion of STAT3: its use to determine the role of STAT3 in the upregulation of cardioprotective proteins by ischemic preconditioning. J Mol Cell Cardiol (2011) 50:589–97.10.1016/j.yjmcc.2011.01.00221223971
    • (2011) J Mol Cell Cardiol , vol.50 , pp. 589-597
    • Bolli, R.1    Stein, A.B.2    Guo, Y.3    Wang, O.L.4    Rokosh, G.5    Dawn, B.6
  • 70
    • 84938564607 scopus 로고    scopus 로고
    • Cardiac-specific ablation of the STAT3 gene in the subacute phase of myocardial infarction exacerbated cardiac remodeling
    • 26055795
    • Enomoto D, Obana M, Miyawaki A, Maeda M, Nakayama H, Fujio Y. Cardiac-specific ablation of the STAT3 gene in the subacute phase of myocardial infarction exacerbated cardiac remodeling. Am J Physiol Heart Circ Physiol (2015) 309:H471–80.10.1152/ajpheart.00730.201426055795
    • (2015) Am J Physiol Heart Circ Physiol , vol.309 , pp. H471-H480
    • Enomoto, D.1    Obana, M.2    Miyawaki, A.3    Maeda, M.4    Nakayama, H.5    Fujio, Y.6
  • 71
    • 67949100572 scopus 로고    scopus 로고
    • Avoidance of transient cardiomyopathy in cardiomyocyte-targeted tamoxifen-induced MerCreMer gene deletion models
    • 19520971
    • Koitabashi N, Bedja D, Zaiman AL, Pinto YM, Zhang M, Gabrielson KL, et al. Avoidance of transient cardiomyopathy in cardiomyocyte-targeted tamoxifen-induced MerCreMer gene deletion models. Circ Res (2009) 105:12–5.10.1161/CIRCRESAHA.109.19841619520971
    • (2009) Circ Res , vol.105 , pp. 12-15
    • Koitabashi, N.1    Bedja, D.2    Zaiman, A.L.3    Pinto, Y.M.4    Zhang, M.5    Gabrielson, K.L.6
  • 72
    • 84857341993 scopus 로고    scopus 로고
    • Cardiac-specific deletion of SOCS-3 prevents development of left ventricular remodeling after acute myocardial infarction
    • 22361405
    • Oba T, Yasukawa H, Hoshijima M, Sasaki K, Futamata N, Fukui D, et al. Cardiac-specific deletion of SOCS-3 prevents development of left ventricular remodeling after acute myocardial infarction. J Am Coll Cardiol (2012) 59:838–52.10.1016/j.jacc.2011.10.88722361405
    • (2012) J Am Coll Cardiol , vol.59 , pp. 838-852
    • Oba, T.1    Yasukawa, H.2    Hoshijima, M.3    Sasaki, K.4    Futamata, N.5    Fukui, D.6
  • 73
    • 84930226410 scopus 로고    scopus 로고
    • Cardiac-specific SOCS3 deletion prevents in vivo myocardial ischemia reperfusion injury through sustained activation of cardioprotective signaling molecules
    • 26010537
    • Nagata T, Yasukawa H, Kyogoku S, Oba T, Takahashi J, Nohara S, et al. Cardiac-specific SOCS3 deletion prevents in vivo myocardial ischemia reperfusion injury through sustained activation of cardioprotective signaling molecules. PLoS One (2015) 10:e0127942.10.1371/journal.pone.012794226010537
    • (2015) PLoS One , vol.10 , pp. e0127942
    • Nagata, T.1    Yasukawa, H.2    Kyogoku, S.3    Oba, T.4    Takahashi, J.5    Nohara, S.6
  • 74
    • 77954762928 scopus 로고    scopus 로고
    • Continuous glycoprotein-130-mediated signal transducer and activator of transcription-3 activation promotes inflammation, left ventricular rupture, and adverse outcome in subacute myocardial infarction
    • 20585009
    • Hilfiker-Kleiner D, Shukla P, Klein G, Schaefer A, Stapel B, Hoch M, et al. Continuous glycoprotein-130-mediated signal transducer and activator of transcription-3 activation promotes inflammation, left ventricular rupture, and adverse outcome in subacute myocardial infarction. Circulation (2010) 122:145–55.10.1161/CIRCULATIONAHA.109.93312720585009
    • (2010) Circulation , vol.122 , pp. 145-155
    • Hilfiker-Kleiner, D.1    Shukla, P.2    Klein, G.3    Schaefer, A.4    Stapel, B.5    Hoch, M.6
  • 75
    • 84869083970 scopus 로고    scopus 로고
    • Differential STAT3 signaling in the heart: impact of concurrent signals and oxidative stress
    • 23904970
    • Zgheib C, Zouein FA, Kurdi M, Booz GW. Differential STAT3 signaling in the heart: impact of concurrent signals and oxidative stress. JAKSTAT (2012) 1:101–10.10.4161/jkst.1977623904970
    • (2012) JAKSTAT , vol.1 , pp. 101-110
    • Zgheib, C.1    Zouein, F.A.2    Kurdi, M.3    Booz, G.W.4
  • 76
    • 84924123511 scopus 로고    scopus 로고
    • Molecular basis of cardioprotection: signal transduction in ischemic pre-, post-, and remote conditioning
    • 25677517
    • Heusch G. Molecular basis of cardioprotection: signal transduction in ischemic pre-, post-, and remote conditioning. Circ Res (2015) 116:674–99.10.1161/CIRCRESAHA.116.30534825677517
    • (2015) Circ Res , vol.116 , pp. 674-699
    • Heusch, G.1
  • 78
    • 50249152907 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription 3 is involved in the cardioprotective signalling pathway activated by insulin therapy at reperfusion
    • 18500485
    • Fuglesteg BN, Suleman N, Tiron C, Kanhema T, Lacerda L, Andreasen TV, et al. Signal transducer and activator of transcription 3 is involved in the cardioprotective signalling pathway activated by insulin therapy at reperfusion. Basic Res Cardiol (2008) 103:444–53.10.1007/s00395-008-0728-x18500485
    • (2008) Basic Res Cardiol , vol.103 , pp. 444-453
    • Fuglesteg, B.N.1    Suleman, N.2    Tiron, C.3    Kanhema, T.4    Lacerda, L.5    Andreasen, T.V.6
  • 79
    • 84937562950 scopus 로고    scopus 로고
    • Across-species transfer of protection by remote ischemic preconditioning with species-specific myocardial signal transduction by reperfusion injury salvage kinase and survival activating factor enhancement pathways
    • 26058828
    • Skyschally A, Gent S, Amanakis G, Schulte C, Kleinbongard P, Heusch G. Across-species transfer of protection by remote ischemic preconditioning with species-specific myocardial signal transduction by reperfusion injury salvage kinase and survival activating factor enhancement pathways. Circ Res (2015) 117:279–88.10.1161/CIRCRESAHA.117.30687826058828
    • (2015) Circ Res , vol.117 , pp. 279-288
    • Skyschally, A.1    Gent, S.2    Amanakis, G.3    Schulte, C.4    Kleinbongard, P.5    Heusch, G.6
  • 80
    • 84855341208 scopus 로고    scopus 로고
    • STAT5 activation and cardioprotection by remote ischemic preconditioning in humans: short communication
    • 22116817
    • Heusch G, Musiolik J, Kottenberg E, Peters J, Jakob H, Thielmann M. STAT5 activation and cardioprotection by remote ischemic preconditioning in humans: short communication. Circ Res (2012) 110:111–5.10.1161/CIRCRESAHA.111.25955622116817
    • (2012) Circ Res , vol.110 , pp. 111-115
    • Heusch, G.1    Musiolik, J.2    Kottenberg, E.3    Peters, J.4    Jakob, H.5    Thielmann, M.6
  • 81
    • 84864465355 scopus 로고    scopus 로고
    • Interplay between SAFE and RISK pathways in sphingosine-1-phosphate-induced cardioprotection
    • 22392184
    • Somers SJ, Frias M, Lacerda L, Opie LH, Lecour S. Interplay between SAFE and RISK pathways in sphingosine-1-phosphate-induced cardioprotection. Cardiovasc Drugs Ther (2012) 26:227–37.10.1007/s10557-012-6376-222392184
    • (2012) Cardiovasc Drugs Ther , vol.26 , pp. 227-237
    • Somers, S.J.1    Frias, M.2    Lacerda, L.3    Opie, L.H.4    Lecour, S.5
  • 82
    • 84862768130 scopus 로고    scopus 로고
    • Remote ischemic preconditioning confers late protection against myocardial ischemia-reperfusion injury in mice by upregulating interleukin-10
    • 22752341
    • Cai ZP, Parajuli N, Zheng X, Becker L. Remote ischemic preconditioning confers late protection against myocardial ischemia-reperfusion injury in mice by upregulating interleukin-10. Basic Res Cardiol (2012) 107:277.10.1007/s00395-012-0277-122752341
    • (2012) Basic Res Cardiol , vol.107 , pp. 277
    • Cai, Z.P.1    Parajuli, N.2    Zheng, X.3    Becker, L.4
  • 83
    • 84938082304 scopus 로고    scopus 로고
    • CXCR4 attenuates cardiomyocytes mitochondrial dysfunction to resist ischaemia-reperfusion injury
    • 25824297
    • Cai WF, Kang K, Huang W, Liang JL, Feng YL, Liu GS, et al. CXCR4 attenuates cardiomyocytes mitochondrial dysfunction to resist ischaemia-reperfusion injury. J Cell Mol Med (2015) 19:1825–35.10.1111/jcmm.1255425824297
    • (2015) J Cell Mol Med , vol.19 , pp. 1825-1835
    • Cai, W.F.1    Kang, K.2    Huang, W.3    Liang, J.L.4    Feng, Y.L.5    Liu, G.S.6
  • 84
    • 34249681852 scopus 로고    scopus 로고
    • An RNA-binding protein αCP-1 is involved in the STAT3-mediated suppression of NF-κB transcriptional activity
    • Nishinakamura H, Minoda Y, Saeki K, Koga K, Takaesu G, Onodera M, et al. An RNA-binding protein αCP-1 is involved in the STAT3-mediated suppression of NF-κB transcriptional activity. Int Immunol (2007) 19:609–19.10.1093/intimm/dxm026
    • (2007) Int Immunol , vol.19 , pp. 609-619
    • Nishinakamura, H.1    Minoda, Y.2    Saeki, K.3    Koga, K.4    Takaesu, G.5    Onodera, M.6
  • 85
    • 33644876126 scopus 로고    scopus 로고
    • Pharmacological preconditioning with tumor necrosis factor-alpha activates signal transducer and activator of transcription-3 at reperfusion without involving classic prosurvival kinases (Akt and extracellular signal-regulated kinase)
    • 16344382
    • Lecour S, Suleman N, Deuchar GA, Somers S, Lacerda L, Huisamen B, et al. Pharmacological preconditioning with tumor necrosis factor-alpha activates signal transducer and activator of transcription-3 at reperfusion without involving classic prosurvival kinases (Akt and extracellular signal-regulated kinase). Circulation (2005) 112:3911–8.10.1161/CIRCULATIONAHA.105.58105816344382
    • (2005) Circulation , vol.112 , pp. 3911-3918
    • Lecour, S.1    Suleman, N.2    Deuchar, G.A.3    Somers, S.4    Lacerda, L.5    Huisamen, B.6
  • 86
    • 84860134497 scopus 로고    scopus 로고
    • The mPTP and its regulatory proteins: final common targets of signalling pathways for protection against necrosis
    • 22072634
    • Miura T, Tanno M. The mPTP and its regulatory proteins: final common targets of signalling pathways for protection against necrosis. Cardiovasc Res (2012) 94:181–9.10.1093/cvr/cvr30222072634
    • (2012) Cardiovasc Res , vol.94 , pp. 181-189
    • Miura, T.1    Tanno, M.2
  • 87
    • 78649324875 scopus 로고    scopus 로고
    • Inhibition of permeability transition pore opening by mitochondrial STAT3 and its role in myocardial ischemia/reperfusion
    • 20960209
    • Boengler K, Hilfiker-Kleiner D, Heusch G, Schulz R. Inhibition of permeability transition pore opening by mitochondrial STAT3 and its role in myocardial ischemia/reperfusion. Basic Res Cardiol (2010) 105:771–85.10.1007/s00395-010-0124-120960209
    • (2010) Basic Res Cardiol , vol.105 , pp. 771-785
    • Boengler, K.1    Hilfiker-Kleiner, D.2    Heusch, G.3    Schulz, R.4
  • 88
    • 80051943914 scopus 로고    scopus 로고
    • Mitochondrial-targeted signal transducer and activator of transcription 3 (STAT3) protects against ischemia-induced changes in the electron transport chain and the generation of reactive oxygen species
    • 21715323
    • Szczepanek K, Chen Q, Derecka M, Salloum FN, Zhang Q, Szelag M, et al. Mitochondrial-targeted signal transducer and activator of transcription 3 (STAT3) protects against ischemia-induced changes in the electron transport chain and the generation of reactive oxygen species. J Biol Chem (2011) 286:29610–20.10.1074/jbc.M111.22620921715323
    • (2011) J Biol Chem , vol.286 , pp. 29610-29620
    • Szczepanek, K.1    Chen, Q.2    Derecka, M.3    Salloum, F.N.4    Zhang, Q.5    Szelag, M.6
  • 89
    • 81355146580 scopus 로고    scopus 로고
    • Mitochondrial STAT3 activation and cardioprotection by ischemic postconditioning in pigs with regional myocardial ischemia/reperfusion
    • 21980124
    • Heusch G, Musiolik J, Gedik N, Skyschally A. Mitochondrial STAT3 activation and cardioprotection by ischemic postconditioning in pigs with regional myocardial ischemia/reperfusion. Circ Res (2011) 109:1302–8.10.1161/CIRCRESAHA.111.25560421980124
    • (2011) Circ Res , vol.109 , pp. 1302-1308
    • Heusch, G.1    Musiolik, J.2    Gedik, N.3    Skyschally, A.4
  • 90
    • 84861469940 scopus 로고    scopus 로고
    • Cardiac vulnerability to ischemia/reperfusion injury drastically increases in late pregnancy
    • 22648276
    • Li J, Umar S, Iorga A, Youn JY, Wang Y, Regitz-Zagrosek V, et al. Cardiac vulnerability to ischemia/reperfusion injury drastically increases in late pregnancy. Basic Res Cardiol (2012) 107:271.10.1007/s00395-012-0271-722648276
    • (2012) Basic Res Cardiol , vol.107 , pp. 271
    • Li, J.1    Umar, S.2    Iorga, A.3    Youn, J.Y.4    Wang, Y.5    Regitz-Zagrosek, V.6
  • 91
    • 33846815521 scopus 로고    scopus 로고
    • A cathepsin D-cleaved 16 kDa form of prolactin mediates postpartum cardiomyopathy
    • 17289576
    • Hilfiker-Kleiner D, Kaminski K, Podewski E, Bonda T, Schaefer A, Sliwa K, et al. A cathepsin D-cleaved 16 kDa form of prolactin mediates postpartum cardiomyopathy. Cell (2007) 128:589–600.10.1016/j.cell.2006.12.03617289576
    • (2007) Cell , vol.128 , pp. 589-600
    • Hilfiker-Kleiner, D.1    Kaminski, K.2    Podewski, E.3    Bonda, T.4    Schaefer, A.5    Sliwa, K.6
  • 92
    • 84901485282 scopus 로고    scopus 로고
    • Opposing roles of Akt and STAT3 in the protection of the maternal heart from peripartum stress
    • 24448315
    • Ricke-Hoch M, Bultmann I, Stapel B, Condorelli G, Rinas U, Sliwa K, et al. Opposing roles of Akt and STAT3 in the protection of the maternal heart from peripartum stress. Cardiovasc Res (2014) 101:587–96.10.1093/cvr/cvu01024448315
    • (2014) Cardiovasc Res , vol.101 , pp. 587-596
    • Ricke-Hoch, M.1    Bultmann, I.2    Stapel, B.3    Condorelli, G.4    Rinas, U.5    Sliwa, K.6
  • 93
    • 84906047643 scopus 로고    scopus 로고
    • Titin gene mutations are common in families with both peripartum cardiomyopathy and dilated cardiomyopathy
    • 24558114
    • van Spaendonck-Zwarts KY, Posafalvi A, van den Berg MP, Hilfiker-Kleiner D, Bollen IA, Sliwa K, et al. Titin gene mutations are common in families with both peripartum cardiomyopathy and dilated cardiomyopathy. Eur Heart J (2014) 35:2165–73.10.1093/eurheartj/ehu05024558114
    • (2014) Eur Heart J , vol.35 , pp. 2165-2173
    • van Spaendonck-Zwarts, K.Y.1    Posafalvi, A.2    van den Berg, M.P.3    Hilfiker-Kleiner, D.4    Bollen, I.A.5    Sliwa, K.6
  • 94
    • 79957523514 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription 3-mediated regulation of miR-199a-5p links cardiomyocyte and endothelial cell function in the heart: a key role for ubiquitin-conjugating enzymes
    • 20965886
    • Haghikia A, Missol-Kolka E, Tsikas D, Venturini L, Brundiers S, Castoldi M, et al. Signal transducer and activator of transcription 3-mediated regulation of miR-199a-5p links cardiomyocyte and endothelial cell function in the heart: a key role for ubiquitin-conjugating enzymes. Eur Heart J (2011) 32:1287–97.10.1093/eurheartj/ehq36920965886
    • (2011) Eur Heart J , vol.32 , pp. 1287-1297
    • Haghikia, A.1    Missol-Kolka, E.2    Tsikas, D.3    Venturini, L.4    Brundiers, S.5    Castoldi, M.6
  • 95
    • 84864277489 scopus 로고    scopus 로고
    • Interleukin-10 treatment attenuates pressure overload-induced hypertrophic remodeling and improves heart function via signal transducers and activators of transcription 3-dependent inhibition of nuclear factor-κB
    • 22705886
    • Verma SK, Krishnamurthy P, Barefield D, Singh N, Gupta R, Lambers E, et al. Interleukin-10 treatment attenuates pressure overload-induced hypertrophic remodeling and improves heart function via signal transducers and activators of transcription 3-dependent inhibition of nuclear factor-κB. Circulation (2012) 126:418–29.10.1161/CIRCULATIONAHA.112.11218522705886
    • (2012) Circulation , vol.126 , pp. 418-429
    • Verma, S.K.1    Krishnamurthy, P.2    Barefield, D.3    Singh, N.4    Gupta, R.5    Lambers, E.6
  • 96
    • 78651481470 scopus 로고    scopus 로고
    • The functions of signal transducers and activators of transcriptions 1 and 3 as cytokine-inducible proteins
    • 21166594
    • Cheon H, Yang J, Stark GR. The functions of signal transducers and activators of transcriptions 1 and 3 as cytokine-inducible proteins. J Interferon Cytokine Res (2011) 31:33–40.10.1089/jir.2010.010021166594
    • (2011) J Interferon Cytokine Res , vol.31 , pp. 33-40
    • Cheon, H.1    Yang, J.2    Stark, G.R.3
  • 97
    • 72049117143 scopus 로고    scopus 로고
    • Role of nuclear unphosphorylated STAT3 in angiotensin II type 1 receptor-induced cardiac hypertrophy
    • 19696070
    • Yue H, Li W, Desnoyer R, Karnik SS. Role of nuclear unphosphorylated STAT3 in angiotensin II type 1 receptor-induced cardiac hypertrophy. Cardiovasc Res (2010) 85:90–9.10.1093/cvr/cvp28519696070
    • (2010) Cardiovasc Res , vol.85 , pp. 90-99
    • Yue, H.1    Li, W.2    Desnoyer, R.3    Karnik, S.S.4
  • 98
    • 34249868449 scopus 로고    scopus 로고
    • Unphosphorylated STAT3 accumulates in response to IL-6 and activates transcription by binding to NFκB
    • Yang J, Liao X, Agarwal MK, Barnes L, Auron PE, Stark GR. Unphosphorylated STAT3 accumulates in response to IL-6 and activates transcription by binding to NFκB. Genes Dev (2007) 21:1396–408.10.1101/gad.1553707
    • (2007) Genes Dev , vol.21 , pp. 1396-1408
    • Yang, J.1    Liao, X.2    Agarwal, M.K.3    Barnes, L.4    Auron, P.E.5    Stark, G.R.6
  • 99
    • 85027947959 scopus 로고    scopus 로고
    • New take on the role of angiotensin II in cardiac hypertrophy and fibrosis
    • Kurdi M, Booz GW. New take on the role of angiotensin II in cardiac hypertrophy and fibrosis. Hypertension (2011) 57:1034–8.10.1161/HYPERTENSIONAHA.111.172700
    • (2011) Hypertension , vol.57 , pp. 1034-1038
    • Kurdi, M.1    Booz, G.W.2
  • 101
    • 79251540845 scopus 로고    scopus 로고
    • Unphosphorylated STAT and heterochromatin protect genome stability
    • 20847228
    • Yan SJ, Lim SJ, Shi S, Dutta P, Li WX. Unphosphorylated STAT and heterochromatin protect genome stability. FASEB J (2011) 25:232–41.10.1096/fj.10-16936720847228
    • (2011) FASEB J , vol.25 , pp. 232-241
    • Yan, S.J.1    Lim, S.J.2    Shi, S.3    Dutta, P.4    Li, W.X.5
  • 102
    • 43149084600 scopus 로고    scopus 로고
    • Drosophila STAT is required for directly maintaining HP1 localization and heterochromatin stability
    • 18344984
    • Shi S, Larson K, Guo D, Lim SJ, Dutta P, Yan SJ, et al. Drosophila STAT is required for directly maintaining HP1 localization and heterochromatin stability. Nat Cell Biol (2008) 10:489–96.10.1038/ncb171318344984
    • (2008) Nat Cell Biol , vol.10 , pp. 489-496
    • Shi, S.1    Larson, K.2    Guo, D.3    Lim, S.J.4    Dutta, P.5    Yan, S.J.6
  • 103
    • 84904769747 scopus 로고    scopus 로고
    • Drosophila linker histone H1 coordinates STAT-dependent organization of heterochromatin and suppresses tumorigenesis caused by hyperactive JAK-STAT signaling
    • 25177369
    • Xu N, Emelyanov AV, Fyodorov DV, Skoultchi AI. Drosophila linker histone H1 coordinates STAT-dependent organization of heterochromatin and suppresses tumorigenesis caused by hyperactive JAK-STAT signaling. Epigenetics Chromatin (2014) 7:16.10.1186/1756-8935-7-1625177369
    • (2014) Epigenetics Chromatin , vol.7 , pp. 16
    • Xu, N.1    Emelyanov, A.V.2    Fyodorov, D.V.3    Skoultchi, A.I.4
  • 104
    • 84879292795 scopus 로고    scopus 로고
    • Unphosphorylated STAT5A stabilizes heterochromatin and suppresses tumor growth
    • 23733954
    • Hu X, Dutta P, Tsurumi A, Li J, Wang J, Land H, et al. Unphosphorylated STAT5A stabilizes heterochromatin and suppresses tumor growth. Proc Natl Acad Sci U S A (2013) 110:10213–8.10.1073/pnas.122124311023733954
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 10213-10218
    • Hu, X.1    Dutta, P.2    Tsurumi, A.3    Li, J.4    Wang, J.5    Land, H.6
  • 105
    • 0036055754 scopus 로고    scopus 로고
    • Cell type-specific and tyrosine phosphorylation-independent nuclear presence of STAT1 and STAT3
    • 11740864
    • Meyer T, Gavenis K, Vinkemeier U. Cell type-specific and tyrosine phosphorylation-independent nuclear presence of STAT1 and STAT3. Exp Cell Res (2002) 272:45–55.10.1006/excr.2001.540511740864
    • (2002) Exp Cell Res , vol.272 , pp. 45-55
    • Meyer, T.1    Gavenis, K.2    Vinkemeier, U.3
  • 106
    • 20444400857 scopus 로고    scopus 로고
    • STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-α3
    • Liu L, McBride KM, Reich NC. STAT3 nuclear import is independent of tyrosine phosphorylation and mediated by importin-α3. Proc Natl Acad Sci U S A (2005) 102:8150–5.10.1073/pnas.0501643102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 8150-8155
    • Liu, L.1    McBride, K.M.2    Reich, N.C.3
  • 107
    • 79956285590 scopus 로고    scopus 로고
    • Dynamics of the STAT3 transcription factor: nuclear import dependent on Ran and importin-β1
    • 21625522
    • Cimica V, Chen HC, Iyer JK, Reich NC. Dynamics of the STAT3 transcription factor: nuclear import dependent on Ran and importin-β1. PLoS One (2011) 6:e20188.10.1371/journal.pone.002018821625522
    • (2011) PLoS One , vol.6 , pp. e20188
    • Cimica, V.1    Chen, H.C.2    Iyer, J.K.3    Reich, N.C.4
  • 108
    • 84902589832 scopus 로고    scopus 로고
    • STATs get their move on
    • 24470978
    • Reich NC. STATs get their move on. JAKSTAT (2013) 2:e27080.10.4161/jkst.2708024470978
    • (2013) JAKSTAT , vol.2 , pp. e27080
    • Reich, N.C.1
  • 109
    • 41849116690 scopus 로고    scopus 로고
    • Roles of unphosphorylated STATs in signaling
    • 18364677
    • Yang J, Stark GR. Roles of unphosphorylated STATs in signaling. Cell Res (2008) 18:443–51.10.1038/cr.2008.4118364677
    • (2008) Cell Res , vol.18 , pp. 443-451
    • Yang, J.1    Stark, G.R.2
  • 110
    • 16244363060 scopus 로고    scopus 로고
    • Extracellular signal-dependent nuclear import of STAT3 is mediated by various importin alphas
    • 15809078
    • Ushijima R, Sakaguchi N, Kano A, Maruyama A, Miyamoto Y, Sekimoto T, et al. Extracellular signal-dependent nuclear import of STAT3 is mediated by various importin alphas. Biochem Biophys Res Commun (2005) 330:880–6.10.1016/j.bbrc.2005.03.06315809078
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 880-886
    • Ushijima, R.1    Sakaguchi, N.2    Kano, A.3    Maruyama, A.4    Miyamoto, Y.5    Sekimoto, T.6
  • 111
    • 33646365075 scopus 로고    scopus 로고
    • Regulation of Stat3 nuclear import by importin α5 and importin α7 via two different functional sequence elements
    • Ma J, Cao X. Regulation of Stat3 nuclear import by importin α5 and importin α7 via two different functional sequence elements. Cell Signal (2006) 18:1117–26.10.1016/j.cellsig.2005.06.016
    • (2006) Cell Signal , vol.18 , pp. 1117-1126
    • Ma, J.1    Cao, X.2
  • 112
    • 0042206459 scopus 로고    scopus 로고
    • A novel sequence in the coiled-coil domain of Stat3 essential for its nuclear translocation
    • 12746441
    • Ma J, Zhang T, Novotny-Diermayr V, Tan AL, Cao X. A novel sequence in the coiled-coil domain of Stat3 essential for its nuclear translocation. J Biol Chem (2003) 278:29252–60.10.1074/jbc.M30419620012746441
    • (2003) J Biol Chem , vol.278 , pp. 29252-29260
    • Ma, J.1    Zhang, T.2    Novotny-Diermayr, V.3    Tan, A.L.4    Cao, X.5
  • 113
    • 79952777363 scopus 로고    scopus 로고
    • The role of the N-terminal domain in dimerization and nucleocytoplasmic shuttling of latent STAT3
    • 21325026
    • Vogt M, Domoszlai T, Kleshchanok D, Lehmann S, Schmitt A, Poli V, et al. The role of the N-terminal domain in dimerization and nucleocytoplasmic shuttling of latent STAT3. J Cell Sci (2011) 124:900–9.10.1242/jcs.07252021325026
    • (2011) J Cell Sci , vol.124 , pp. 900-909
    • Vogt, M.1    Domoszlai, T.2    Kleshchanok, D.3    Lehmann, S.4    Schmitt, A.5    Poli, V.6
  • 114
    • 24644512928 scopus 로고    scopus 로고
    • Nuclear retention of STAT3 through the coiled-coil domain regulates its activity
    • 16140268
    • Sato N, Tsuruma R, Imoto S, Sekine Y, Muromoto R, Sugiyama K, et al. Nuclear retention of STAT3 through the coiled-coil domain regulates its activity. Biochem Biophys Res Commun (2005) 336:617–24.10.1016/j.bbrc.2005.08.14516140268
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 617-624
    • Sato, N.1    Tsuruma, R.2    Imoto, S.3    Sekine, Y.4    Muromoto, R.5    Sugiyama, K.6
  • 115
    • 0037327154 scopus 로고    scopus 로고
    • Regulation of Stat3 nuclear export
    • 12588893
    • Bhattacharya S, Schindler C. Regulation of Stat3 nuclear export. J Clin Invest (2003) 111:553–9.10.1172/JCI1537212588893
    • (2003) J Clin Invest , vol.111 , pp. 553-559
    • Bhattacharya, S.1    Schindler, C.2
  • 116
    • 84906245589 scopus 로고    scopus 로고
    • Regulation and function of signal transducer and activator of transcription 3
    • 24921012
    • Qi QR, Yang ZM. Regulation and function of signal transducer and activator of transcription 3. World J Biol Chem (2014) 5:231–9.10.4331/wjbc.v5.i2.23124921012
    • (2014) World J Biol Chem , vol.5 , pp. 231-239
    • Qi, Q.R.1    Yang, Z.M.2
  • 117
    • 33646591224 scopus 로고    scopus 로고
    • Stat3 activation of NF-κB p100 processing involves CBP/p300-mediated acetylation
    • Nadiminty N, Lou W, Lee SO, Lin X, Trump DL, Gao AC. Stat3 activation of NF-κB p100 processing involves CBP/p300-mediated acetylation. Proc Natl Acad Sci U S A (2006) 103:7264–9.10.1073/pnas.0509808103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7264-7269
    • Nadiminty, N.1    Lou, W.2    Lee, S.O.3    Lin, X.4    Trump, D.L.5    Gao, A.C.6
  • 118
    • 63249092765 scopus 로고    scopus 로고
    • Persistently activated Stat3 maintains constitutive NF-κB activity in tumors
    • Lee H, Herrmann A, Deng JH, Kujawski M, Niu G, Li Z, et al. Persistently activated Stat3 maintains constitutive NF-κB activity in tumors. Cancer Cell (2009) 15:283–93.10.1016/j.ccr.2009.02.015
    • (2009) Cancer Cell , vol.15 , pp. 283-293
    • Lee, H.1    Herrmann, A.2    Deng, J.H.3    Kujawski, M.4    Niu, G.5    Li, Z.6
  • 119
    • 0035380308 scopus 로고    scopus 로고
    • Pro- versus anti-inflammatory cytokines: myth or reality
    • 11502077
    • Cavaillon JM. Pro- versus anti-inflammatory cytokines: myth or reality. Cell Mol Biol (Noisy-le-grand) (2001) 47:695–702.11502077
    • (2001) Cell Mol Biol (Noisy-le-grand) , vol.47 , pp. 695-702
    • Cavaillon, J.M.1
  • 120
    • 67649988989 scopus 로고    scopus 로고
    • Mitochondrial STAT3 supports Ras-dependent oncogenic transformation
    • 19556508
    • Gough DJ, Corlett A, Schlessinger K, Wegrzyn J, Larner AC, Levy DE. Mitochondrial STAT3 supports Ras-dependent oncogenic transformation. Science (2009) 324:1713–6.10.1126/science.117172119556508
    • (2009) Science , vol.324 , pp. 1713-1716
    • Gough, D.J.1    Corlett, A.2    Schlessinger, K.3    Wegrzyn, J.4    Larner, A.C.5    Levy, D.E.6
  • 121
    • 84907684949 scopus 로고    scopus 로고
    • STAT3 supports experimental K-RasG12D-induced murine myeloproliferative neoplasms dependent on serine phosphorylation
    • 25150294
    • Gough DJ, Marie IJ, Lobry C, Aifantis I, Levy DE. STAT3 supports experimental K-RasG12D-induced murine myeloproliferative neoplasms dependent on serine phosphorylation. Blood (2014) 124:2252–61.10.1182/blood-2013-02-48419625150294
    • (2014) Blood , vol.124 , pp. 2252-2261
    • Gough, D.J.1    Marie, I.J.2    Lobry, C.3    Aifantis, I.4    Levy, D.E.5
  • 122
    • 84938598880 scopus 로고    scopus 로고
    • Mitochondrial STAT3 contributes to transformation of Barrett’s epithelial cells that express oncogenic Ras in a p53-independent fashion
    • 26045618
    • Yu C, Huo X, Agoston AT, Zhang X, Theiss AL, Cheng E, et al. Mitochondrial STAT3 contributes to transformation of Barrett’s epithelial cells that express oncogenic Ras in a p53-independent fashion. Am J Physiol Gastrointest Liver Physiol (2015) 309:G146–61.10.1152/ajpgi.00462.201426045618
    • (2015) Am J Physiol Gastrointest Liver Physiol , vol.309 , pp. G146-G161
    • Yu, C.1    Huo, X.2    Agoston, A.T.3    Zhang, X.4    Theiss, A.L.5    Cheng, E.6
  • 123
    • 77954927294 scopus 로고    scopus 로고
    • Stoichiometry of STAT3 and mitochondrial proteins: implications for the regulation of oxidative phosphorylation by protein-protein interactions
    • 20558729
    • Phillips D, Reilley MJ, Aponte AM, Wang G, Boja E, Gucek M, et al. Stoichiometry of STAT3 and mitochondrial proteins: implications for the regulation of oxidative phosphorylation by protein-protein interactions. J Biol Chem (2010) 285:23532–6.10.1074/jbc.C110.15265220558729
    • (2010) J Biol Chem , vol.285 , pp. 23532-23536
    • Phillips, D.1    Reilley, M.J.2    Aponte, A.M.3    Wang, G.4    Boja, E.5    Gucek, M.6
  • 124
    • 33846335174 scopus 로고    scopus 로고
    • Modulation of electron transport protects cardiac mitochondria and decreases myocardial injury during ischemia and reperfusion
    • 16971498
    • Chen Q, Camara AK, Stowe DF, Hoppel CL, Lesnefsky EJ. Modulation of electron transport protects cardiac mitochondria and decreases myocardial injury during ischemia and reperfusion. Am J Physiol Cell Physiol (2007) 292:C137–47.10.1152/ajpcell.00270.200616971498
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. C137-C147
    • Chen, Q.1    Camara, A.K.2    Stowe, D.F.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 125
    • 29244441132 scopus 로고    scopus 로고
    • Blockade of electron transport before cardiac ischemia with the reversible inhibitor amobarbital protects rat heart mitochondria
    • 16174799
    • Chen Q, Hoppel CL, Lesnefsky EJ. Blockade of electron transport before cardiac ischemia with the reversible inhibitor amobarbital protects rat heart mitochondria. J Pharmacol Exp Ther (2006) 316:200–7.10.1124/jpet.105.09170216174799
    • (2006) J Pharmacol Exp Ther , vol.316 , pp. 200-207
    • Chen, Q.1    Hoppel, C.L.2    Lesnefsky, E.J.3
  • 126
    • 84892880554 scopus 로고    scopus 로고
    • The breathing heart – mitochondrial respiratory chain dysfunction in cardiac disease
    • 24377708
    • Schwarz K, Siddiqi N, Singh S, Neil CJ, Dawson DK, Frenneaux MP. The breathing heart – mitochondrial respiratory chain dysfunction in cardiac disease. Int J Cardiol (2014) 171:134–43.10.1016/j.ijcard.2013.12.01424377708
    • (2014) Int J Cardiol , vol.171 , pp. 134-143
    • Schwarz, K.1    Siddiqi, N.2    Singh, S.3    Neil, C.J.4    Dawson, D.K.5    Frenneaux, M.P.6
  • 127
    • 84883562084 scopus 로고    scopus 로고
    • Cardiac metabolism in heart failure: implications beyond ATP production
    • 23989714
    • Doenst T, Nguyen TD, Abel ED. Cardiac metabolism in heart failure: implications beyond ATP production. Circ Res (2013) 113:709–24.10.1161/CIRCRESAHA.113.30037623989714
    • (2013) Circ Res , vol.113 , pp. 709-724
    • Doenst, T.1    Nguyen, T.D.2    Abel, E.D.3
  • 128
    • 84872676487 scopus 로고    scopus 로고
    • Mitochondria in cardiac hypertrophy and heart failure
    • Rosca MG, Tandler B, Hoppel CL. Mitochondria in cardiac hypertrophy and heart failure. J Mol Cell Cardiol (2013) 55:31–41.10.1016/j.yjmcc.2012.09.002
    • (2013) J Mol Cell Cardiol , vol.55 , pp. 31-41
    • Rosca, M.G.1    Tandler, B.2    Hoppel, C.L.3
  • 129
    • 84885331404 scopus 로고    scopus 로고
    • Alterations in mitochondrial function in cardiac hypertrophy and heart failure
    • 22968404
    • Osterholt M, Nguyen TD, Schwarzer M, Doenst T. Alterations in mitochondrial function in cardiac hypertrophy and heart failure. Heart Fail Rev (2013) 18:645–56.10.1007/s10741-012-9346-722968404
    • (2013) Heart Fail Rev , vol.18 , pp. 645-656
    • Osterholt, M.1    Nguyen, T.D.2    Schwarzer, M.3    Doenst, T.4
  • 130
    • 0033385980 scopus 로고    scopus 로고
    • Progress on the mitochondrial permeability transition pore: regulation by complex I and ubiquinone analogs
    • 10665524
    • Fontaine E, Bernardi P. Progress on the mitochondrial permeability transition pore: regulation by complex I and ubiquinone analogs. J Bioenerg Biomembr (1999) 31:335–45.10.1023/A:100547580235010665524
    • (1999) J Bioenerg Biomembr , vol.31 , pp. 335-345
    • Fontaine, E.1    Bernardi, P.2
  • 131
  • 133
    • 84881348520 scopus 로고    scopus 로고
    • Mitochondrial complex I deficiency increases protein acetylation and accelerates heart failure
    • 23931755
    • Karamanlidis G, Lee CF, Garcia-Menendez L, Kolwicz SC, Jr Suthammarak W, Gong G, et al. Mitochondrial complex I deficiency increases protein acetylation and accelerates heart failure. Cell Metab (2013) 18:239–50.10.1016/j.cmet.2013.07.00223931755
    • (2013) Cell Metab , vol.18 , pp. 239-250
    • Karamanlidis, G.1    Lee, C.F.2    Garcia-Menendez, L.3    Kolwicz, S.C.4    Suthammarak, W.5    Gong, G.6
  • 134
    • 77449120223 scopus 로고    scopus 로고
    • Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway
    • 19940131
    • Pillai VB, Sundaresan NR, Kim G, Gupta M, Rajamohan SB, Pillai JB, et al. Exogenous NAD blocks cardiac hypertrophic response via activation of the SIRT3-LKB1-AMP-activated kinase pathway. J Biol Chem (2010) 285:3133–44.10.1074/jbc.M109.07727119940131
    • (2010) J Biol Chem , vol.285 , pp. 3133-3144
    • Pillai, V.B.1    Sundaresan, N.R.2    Kim, G.3    Gupta, M.4    Rajamohan, S.B.5    Pillai, J.B.6
  • 135
    • 55749084738 scopus 로고    scopus 로고
    • A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
    • 18794531
    • Ahn BH, Kim HS, Song S, Lee IH, Liu J, Vassilopoulos A, et al. A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc Natl Acad Sci U S A (2008) 105:14447–52.10.1073/pnas.080379010518794531
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 14447-14452
    • Ahn, B.H.1    Kim, H.S.2    Song, S.3    Lee, I.H.4    Liu, J.5    Vassilopoulos, A.6
  • 136
    • 50149103440 scopus 로고    scopus 로고
    • Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
    • 18680753
    • Schlicker C, Gertz M, Papatheodorou P, Kachholz B, Becker CF, Steegborn C. Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. J Mol Biol (2008) 382:790–801.10.1016/j.jmb.2008.07.04818680753
    • (2008) J Mol Biol , vol.382 , pp. 790-801
    • Schlicker, C.1    Gertz, M.2    Papatheodorou, P.3    Kachholz, B.4    Becker, C.F.5    Steegborn, C.6
  • 137
    • 79957979314 scopus 로고    scopus 로고
    • Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
    • 21566644
    • Chen Y, Zhang J, Lin Y, Lei Q, Guan KL, Zhao S, et al. Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS. EMBO Rep (2011) 12:534–41.10.1038/embor.2011.6521566644
    • (2011) EMBO Rep , vol.12 , pp. 534-541
    • Chen, Y.1    Zhang, J.2    Lin, Y.3    Lei, Q.4    Guan, K.L.5    Zhao, S.6
  • 138
    • 84859951790 scopus 로고    scopus 로고
    • SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status
    • 22416140
    • Yu W, Dittenhafer-Reed KE, Denu JM. SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status. J Biol Chem (2012) 287:14078–86.10.1074/jbc.M112.35520622416140
    • (2012) J Biol Chem , vol.287 , pp. 14078-14086
    • Yu, W.1    Dittenhafer-Reed, K.E.2    Denu, J.M.3
  • 139
    • 84929011194 scopus 로고    scopus 로고
    • High-fat diet induces cardiac remodelling and dysfunction: assessment of the role played by SIRT3 loss
    • 25782072
    • Zeng H, Vaka VR, He X, Booz GW, Chen JX. High-fat diet induces cardiac remodelling and dysfunction: assessment of the role played by SIRT3 loss. J Cell Mol Med (2015) 19:1847–56.10.1111/jcmm.1255625782072
    • (2015) J Cell Mol Med , vol.19 , pp. 1847-1856
    • Zeng, H.1    Vaka, V.R.2    He, X.3    Booz, G.W.4    Chen, J.X.5
  • 140
    • 79952266729 scopus 로고    scopus 로고
    • Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy
    • 21212461
    • Hafner AV, Dai J, Gomes AP, Xiao CY, Palmeira CM, Rosenzweig A, et al. Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy. Aging (Albany NY) (2010) 2:914–23.21212461
    • (2010) Aging (Albany NY) , vol.2 , pp. 914-923
    • Hafner, A.V.1    Dai, J.2    Gomes, A.P.3    Xiao, C.Y.4    Palmeira, C.M.5    Rosenzweig, A.6
  • 141
    • 84902687763 scopus 로고    scopus 로고
    • SIRT3 deficiency exacerbates ischemia-reperfusion injury: implication for aged hearts
    • 24748594
    • Porter GA, Urciuoli WR, Brookes PS, Nadtochiy SM. SIRT3 deficiency exacerbates ischemia-reperfusion injury: implication for aged hearts. Am J Physiol Heart Circ Physiol (2014) 306:H1602–9.10.1152/ajpheart.00027.201424748594
    • (2014) Am J Physiol Heart Circ Physiol , vol.306 , pp. H1602-H1609
    • Porter, G.A.1    Urciuoli, W.R.2    Brookes, P.S.3    Nadtochiy, S.M.4
  • 142
    • 84861415338 scopus 로고    scopus 로고
    • Direct renin inhibition exerts an anti-hypertrophic effect associated with improved mitochondrial function in post-infarction heart failure in diabetic rats
    • 22613984
    • Parodi-Rullan R, Barreto-Torres G, Ruiz L, Casasnovas J, Javadov S. Direct renin inhibition exerts an anti-hypertrophic effect associated with improved mitochondrial function in post-infarction heart failure in diabetic rats. Cell Physiol Biochem (2012) 29:841–50.10.1159/00017852622613984
    • (2012) Cell Physiol Biochem , vol.29 , pp. 841-850
    • Parodi-Rullan, R.1    Barreto-Torres, G.2    Ruiz, L.3    Casasnovas, J.4    Javadov, S.5
  • 144
    • 51749113618 scopus 로고    scopus 로고
    • Cardiac mitochondria in heart failure: decrease in respirasomes and oxidative phosphorylation
    • 18710878
    • Rosca MG, Vazquez EJ, Kerner J, Parland W, Chandler MP, Stanley W, et al. Cardiac mitochondria in heart failure: decrease in respirasomes and oxidative phosphorylation. Cardiovasc Res (2008) 80:30–9.10.1093/cvr/cvn18418710878
    • (2008) Cardiovasc Res , vol.80 , pp. 30-39
    • Rosca, M.G.1    Vazquez, E.J.2    Kerner, J.3    Parland, W.4    Chandler, M.P.5    Stanley, W.6
  • 145
    • 77956586695 scopus 로고    scopus 로고
    • Mitochondria in heart failure
    • Rosca MG, Hoppel CL. Mitochondria in heart failure. Cardiovasc Res (2010) 88:40–50.10.1093/cvr/cvq240
    • (2010) Cardiovasc Res , vol.88 , pp. 40-50
    • Rosca, M.G.1    Hoppel, C.L.2
  • 146
    • 84900447983 scopus 로고    scopus 로고
    • Low abundance of the matrix arm of complex I in mitochondria predicts longevity in mice
    • 24815183
    • Miwa S, Jow H, Baty K, Johnson A, Czapiewski R, Saretzki G, et al. Low abundance of the matrix arm of complex I in mitochondria predicts longevity in mice. Nat Commun (2014) 5:3837.10.1038/ncomms483724815183
    • (2014) Nat Commun , vol.5 , pp. 3837
    • Miwa, S.1    Jow, H.2    Baty, K.3    Johnson, A.4    Czapiewski, R.5    Saretzki, G.6
  • 147
    • 84940722200 scopus 로고    scopus 로고
    • Cell death disguised: the mitochondrial permeability transition pore as the c-subunit of the F1FO ATP synthase
    • 25956324
    • Jonas EA, Porter GA, Jr Beutner G, Mnatsakanyan N, Alavian KN. Cell death disguised: the mitochondrial permeability transition pore as the c-subunit of the F1FO ATP synthase. Pharmacol Res (2015) 99:382–92.10.1016/j.phrs.2015.04.01325956324
    • (2015) Pharmacol Res , vol.99 , pp. 382-392
    • Jonas, E.A.1    Porter, G.A.2    Beutner, G.3    Mnatsakanyan, N.4    Alavian, K.N.5
  • 148
    • 0038771142 scopus 로고    scopus 로고
    • The nuclear encoded subunits of complex I from bovine heart mitochondria
    • 12837546
    • Hirst J, Carroll J, Fearnley IM, Shannon RJ, Walker JE. The nuclear encoded subunits of complex I from bovine heart mitochondria. Biochim Biophys Acta (2003) 1604:135–50.10.1016/S0005-2728(03)00059-812837546
    • (2003) Biochim Biophys Acta , vol.1604 , pp. 135-150
    • Hirst, J.1    Carroll, J.2    Fearnley, I.M.3    Shannon, R.J.4    Walker, J.E.5
  • 149
    • 0038160473 scopus 로고    scopus 로고
    • Analysis of the subunit composition of complex I from bovine heart mitochondria
    • 12644575
    • Carroll J, Fearnley IM, Shannon RJ, Hirst J, Walker JE. Analysis of the subunit composition of complex I from bovine heart mitochondria. Mol Cell Proteomics (2003) 2:117–26.10.1074/mcp.M300014-MCP20012644575
    • (2003) Mol Cell Proteomics , vol.2 , pp. 117-126
    • Carroll, J.1    Fearnley, I.M.2    Shannon, R.J.3    Hirst, J.4    Walker, J.E.5
  • 150
    • 84915761829 scopus 로고    scopus 로고
    • Architecture of mammalian respiratory complex I
    • 25209663
    • Vinothkumar KR, Zhu J, Hirst J. Architecture of mammalian respiratory complex I. Nature (2014) 515:80–4.10.1038/nature1368625209663
    • (2014) Nature , vol.515 , pp. 80-84
    • Vinothkumar, K.R.1    Zhu, J.2    Hirst, J.3
  • 151
    • 85079112769 scopus 로고    scopus 로고
    • Institute of Molecular and Cell Biology, Agency for Science, Technology and Research, Singapore, Ph.D
    • Lu H. The Study of GRIM-19 Function in Mitochondria. Ph.D., Institute of Molecular and Cell Biology, Agency for Science, Technology and Research, Singapore (2007).
    • (2007) The Study of GRIM-19 Function in Mitochondria
    • Lu, H.1
  • 152
    • 84897352802 scopus 로고    scopus 로고
    • ND3, ND1 and 39kDa subunits are more exposed in the de-active form of bovine mitochondrial complex I
    • 24560811
    • Babot M, Labarbuta P, Birch A, Kee S, Fuszard M, Botting CH, et al. ND3, ND1 and 39kDa subunits are more exposed in the de-active form of bovine mitochondrial complex I. Biochim Biophys Acta (2014) 1837:929–39.10.1016/j.bbabio.2014.02.01324560811
    • (2014) Biochim Biophys Acta , vol.1837 , pp. 929-939
    • Babot, M.1    Labarbuta, P.2    Birch, A.3    Kee, S.4    Fuszard, M.5    Botting, C.H.6
  • 153
    • 78149471573 scopus 로고    scopus 로고
    • Quinone binding and reduction by respiratory complex I
    • 20493164
    • Tocilescu MA, Zickermann V, Zwicker K, Brandt U. Quinone binding and reduction by respiratory complex I. Biochim Biophys Acta (2010) 1797:1883–90.10.1016/j.bbabio.2010.05.00920493164
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1883-1890
    • Tocilescu, M.A.1    Zickermann, V.2    Zwicker, K.3    Brandt, U.4
  • 154
    • 84874352529 scopus 로고    scopus 로고
    • Crystal structure of the entire respiratory complex I
    • 23417064
    • Baradaran R, Berrisford JM, Minhas GS, Sazanov LA. Crystal structure of the entire respiratory complex I. Nature (2013) 494:443–8.10.1038/nature1187123417064
    • (2013) Nature , vol.494 , pp. 443-448
    • Baradaran, R.1    Berrisford, J.M.2    Minhas, G.S.3    Sazanov, L.A.4
  • 155
    • 77952979824 scopus 로고    scopus 로고
    • The architecture of respiratory complex I
    • 20505720
    • Efremov RG, Baradaran R, Sazanov LA. The architecture of respiratory complex I. Nature (2010) 465:441–5.10.1038/nature0906620505720
    • (2010) Nature , vol.465 , pp. 441-445
    • Efremov, R.G.1    Baradaran, R.2    Sazanov, L.A.3
  • 157
    • 84894165975 scopus 로고    scopus 로고
    • Cardiac mitochondria and reactive oxygen species generation
    • 24481843
    • Chen YR, Zweier JL. Cardiac mitochondria and reactive oxygen species generation. Circ Res (2014) 114:524–37.10.1161/CIRCRESAHA.114.30055924481843
    • (2014) Circ Res , vol.114 , pp. 524-537
    • Chen, Y.R.1    Zweier, J.L.2
  • 158
    • 39549102405 scopus 로고    scopus 로고
    • Ischemic defects in the electron transport chain increase the production of reactive oxygen species from isolated rat heart mitochondria
    • 18077608
    • Chen Q, Moghaddas S, Hoppel CL, Lesnefsky EJ. Ischemic defects in the electron transport chain increase the production of reactive oxygen species from isolated rat heart mitochondria. Am J Physiol Cell Physiol (2008) 294:C460–6.10.1152/ajpcell.00211.200718077608
    • (2008) Am J Physiol Cell Physiol , vol.294 , pp. C460-C466
    • Chen, Q.1    Moghaddas, S.2    Hoppel, C.L.3    Lesnefsky, E.J.4
  • 159
    • 48249132021 scopus 로고    scopus 로고
    • GRIM-19 is essential for maintenance of mitochondrial membrane potential
    • 18287540
    • Lu H, Cao X. GRIM-19 is essential for maintenance of mitochondrial membrane potential. Mol Biol Cell (2008) 19:1893–902.10.1091/mbc.E07-07-068318287540
    • (2008) Mol Biol Cell , vol.19 , pp. 1893-1902
    • Lu, H.1    Cao, X.2
  • 160
    • 4544276735 scopus 로고    scopus 로고
    • GRIM-19, a cell death regulatory protein, is essential for assembly and function of mitochondrial complex I
    • 15367666
    • Huang G, Lu H, Hao A, Ng DC, Ponniah S, Guo K, et al. GRIM-19, a cell death regulatory protein, is essential for assembly and function of mitochondrial complex I. Mol Cell Biol (2004) 24:8447–56.10.1128/MCB.24.19.8447-8456.200415367666
    • (2004) Mol Cell Biol , vol.24 , pp. 8447-8456
    • Huang, G.1    Lu, H.2    Hao, A.3    Ng, D.C.4    Ponniah, S.5    Guo, K.6
  • 161
    • 34249736347 scopus 로고    scopus 로고
    • The phosphorylation pattern of bovine heart complex I subunits
    • 17443843
    • Palmisano G, Sardanelli AM, Signorile A, Papa S, Larsen MR. The phosphorylation pattern of bovine heart complex I subunits. Proteomics (2007) 7:1575–83.10.1002/pmic.20060080117443843
    • (2007) Proteomics , vol.7 , pp. 1575-1583
    • Palmisano, G.1    Sardanelli, A.M.2    Signorile, A.3    Papa, S.4    Larsen, M.R.5
  • 162
    • 84898023373 scopus 로고    scopus 로고
    • PINK1 loss-of-function mutations affect mitochondrial complex I activity via NdufA10 ubiquinone uncoupling
    • 24652937
    • Morais VA, Haddad D, Craessaerts K, De Bock PJ, Swerts J, Vilain S, et al. PINK1 loss-of-function mutations affect mitochondrial complex I activity via NdufA10 ubiquinone uncoupling. Science (2014) 344:203–7.10.1126/science.124916124652937
    • (2014) Science , vol.344 , pp. 203-207
    • Morais, V.A.1    Haddad, D.2    Craessaerts, K.3    De Bock, P.J.4    Swerts, J.5    Vilain, S.6
  • 163
    • 84902242573 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation
    • 24561273
    • Drose S, Brandt U, Wittig I. Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation. Biochim Biophys Acta (2014) 1844:1344–54.10.1016/j.bbapap.2014.02.00624561273
    • (2014) Biochim Biophys Acta , vol.1844 , pp. 1344-1354
    • Drose, S.1    Brandt, U.2    Wittig, I.3
  • 164
    • 84884665651 scopus 로고    scopus 로고
    • Molecular mechanism and physiological role of active-deactive transition of mitochondrial complex I
    • 24059527
    • Babot M, Galkin A. Molecular mechanism and physiological role of active-deactive transition of mitochondrial complex I. Biochem Soc Trans (2013) 41:1325–30.10.1042/BST2013008824059527
    • (2013) Biochem Soc Trans , vol.41 , pp. 1325-1330
    • Babot, M.1    Galkin, A.2
  • 165
    • 84901841671 scopus 로고    scopus 로고
    • Characterisation of the active/de-active transition of mitochondrial complex I
    • 24569053
    • Babot M, Birch A, Labarbuta P, Galkin A. Characterisation of the active/de-active transition of mitochondrial complex I. Biochim Biophys Acta (2014) 1837:1083–92.10.1016/j.bbabio.2014.02.01824569053
    • (2014) Biochim Biophys Acta , vol.1837 , pp. 1083-1092
    • Babot, M.1    Birch, A.2    Labarbuta, P.3    Galkin, A.4
  • 166
    • 84875388964 scopus 로고    scopus 로고
    • Conformation-specific crosslinking of mitochondrial complex I
    • 23454639
    • Ciano M, Fuszard M, Heide H, Botting CH, Galkin A. Conformation-specific crosslinking of mitochondrial complex I. FEBS Lett (2013) 587:867–72.10.1016/j.febslet.2013.02.03923454639
    • (2013) FEBS Lett , vol.587 , pp. 867-872
    • Ciano, M.1    Fuszard, M.2    Heide, H.3    Botting, C.H.4    Galkin, A.5
  • 167
    • 38049136885 scopus 로고    scopus 로고
    • S-nitrosation of mitochondrial complex I depends on its structural conformation
    • 17956863
    • Galkin A, Moncada S. S-nitrosation of mitochondrial complex I depends on its structural conformation. J Biol Chem (2007) 282:37448–53.10.1074/jbc.M70754320017956863
    • (2007) J Biol Chem , vol.282 , pp. 37448-37453
    • Galkin, A.1    Moncada, S.2
  • 168
    • 84880253528 scopus 로고    scopus 로고
    • Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I
    • 23708290
    • Chouchani ET, Methner C, Nadtochiy SM, Logan A, Pell VR, Ding S, et al. Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I. Nat Med (2013) 19:753–9.10.1038/nm.321223708290
    • (2013) Nat Med , vol.19 , pp. 753-759
    • Chouchani, E.T.1    Methner, C.2    Nadtochiy, S.M.3    Logan, A.4    Pell, V.R.5    Ding, S.6
  • 169
    • 84884623857 scopus 로고    scopus 로고
    • Conformational change of mitochondrial complex I increases ROS sensitivity during ischemia
    • 23419200
    • Gorenkova N, Robinson E, Grieve DJ, Galkin A. Conformational change of mitochondrial complex I increases ROS sensitivity during ischemia. Antioxid Redox Signal (2013) 19:1459–68.10.1089/ars.2012.469823419200
    • (2013) Antioxid Redox Signal , vol.19 , pp. 1459-1468
    • Gorenkova, N.1    Robinson, E.2    Grieve, D.J.3    Galkin, A.4
  • 170
    • 84904468117 scopus 로고    scopus 로고
    • Prohibitin 1 modulates mitochondrial function of Stat3
    • 24975845
    • Han J, Yu C, Souza RF, Theiss AL. Prohibitin 1 modulates mitochondrial function of Stat3. Cell Signal (2014) 26:2086–95.10.1016/j.cellsig.2014.06.00624975845
    • (2014) Cell Signal , vol.26 , pp. 2086-2095
    • Han, J.1    Yu, C.2    Souza, R.F.3    Theiss, A.L.4


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