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Volumn 5, Issue , 2014, Pages

Integrin-linked kinase mediates force transduction in cardiomyocytes by modulating SERCA2a/PLN function

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); INTEGRIN LINKED KINASE; PHOSPHOLAMBAN; PLECKSTRIN; REGULATOR PROTEIN; SARCOPLASMIC ENDOPLASMIC RETICULUM CALCIUM ATPASE ISOFORM 2A; UNCLASSIFIED DRUG; CALCIUM BINDING PROTEIN; INTEGRIN-LINKED KINASE; PROTEIN SERINE THREONINE KINASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 84923374863     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5533     Document Type: Article
Times cited : (40)

References (69)
  • 2
    • 84873855851 scopus 로고    scopus 로고
    • Genetic mutations and mechanisms in dilated cardiomyopathy
    • McNally, E. M., Golbus, J. R. & Puckelwartz, M. J. Genetic mutations and mechanisms in dilated cardiomyopathy. J. Clin. Invest. 123, 19-26 (2013).
    • (2013) J. Clin. Invest. , vol.123 , pp. 19-26
    • McNally, E.M.1    Golbus, J.R.2    Puckelwartz, M.J.3
  • 3
    • 84873880957 scopus 로고    scopus 로고
    • Calcium cycling proteins and heart failure: Mechanisms and therapeutics
    • Marks, A. R. Calcium cycling proteins and heart failure: mechanisms and therapeutics. J. Clin. Invest. 123, 46-52 (2013).
    • (2013) J. Clin. Invest. , vol.123 , pp. 46-52
    • Marks, A.R.1
  • 4
    • 78650889008 scopus 로고    scopus 로고
    • Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump
    • Glaves, J. P., Trieber, C. A., Ceholski, D. K., Stokes, D. L. & Young, H. S. Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump. J. Mol. Biol. 405, 707-723 (2010).
    • (2010) J. Mol. Biol. , vol.405 , pp. 707-723
    • Glaves, J.P.1    Trieber, C.A.2    Ceholski, D.K.3    Stokes, D.L.4    Young, H.S.5
  • 5
    • 84862286538 scopus 로고    scopus 로고
    • Modulation of cardiac contractility by the phospholamban/SERCA2a regulatome
    • Kranias, E. G. & Hajjar, R. J. Modulation of cardiac contractility by the phospholamban/SERCA2a regulatome. Circ. Res. 110, 1646-1660 (2012).
    • (2012) Circ. Res. , vol.110 , pp. 1646-1660
    • Kranias, E.G.1    Hajjar, R.J.2
  • 6
    • 0030888810 scopus 로고    scopus 로고
    • Increased expression of cardiac phosphatases in patients with end-stage heart failure
    • Neumann, J. et al. Increased expression of cardiac phosphatases in patients with end-stage heart failure. J. Mol. Cell Cardiol. 29, 265-272 (1997).
    • (1997) J. Mol. Cell Cardiol. , vol.29 , pp. 265-272
    • Neumann, J.1
  • 7
    • 79961032369 scopus 로고    scopus 로고
    • Calcium upregulation by percutaneous administration of gene therapy in cardiac disease (CUPID): A phase 2 trial of intracoronary gene therapy of sarcoplasmic reticulum Ca2+-ATPase in patients with advanced heart failure
    • Jessup, M. et al. Calcium upregulation by percutaneous administration of gene therapy in cardiac disease (CUPID): a phase 2 trial of intracoronary gene therapy of sarcoplasmic reticulum Ca2+-ATPase in patients with advanced heart failure. Circulation 124, 304-313 (2011).
    • (2011) Circulation , vol.124 , pp. 304-313
    • Jessup, M.1
  • 8
    • 84862010808 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum and calcium cycling targeting by gene therapy
    • Hulot, J. S., Senyei, G. & Hajjar, R. J. Sarcoplasmic reticulum and calcium cycling targeting by gene therapy. Gene Ther. 19, 596-599 (2012).
    • (2012) Gene Ther. , vol.19 , pp. 596-599
    • Hulot, J.S.1    Senyei, G.2    Hajjar, R.J.3
  • 9
    • 79953172201 scopus 로고    scopus 로고
    • Cardiac Z-disc signaling network
    • Frank, D. & Frey, N. Cardiac Z-disc signaling network. J. Biol. Chem. 286, 9897-9904 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 9897-9904
    • Frank, D.1    Frey, N.2
  • 10
    • 79961131888 scopus 로고    scopus 로고
    • PINCH proteins regulate cardiac contractility by modulating integrin-linked kinase-protein kinase B signaling
    • Meder, B. et al. PINCH proteins regulate cardiac contractility by modulating integrin-linked kinase-protein kinase B signaling. Mol. Cell Biol. 31, 3424-3435 (2011).
    • (2011) Mol. Cell Biol. , vol.31 , pp. 3424-3435
    • Meder, B.1
  • 11
    • 33748250034 scopus 로고    scopus 로고
    • Integrin-linked kinase, a novel component of the cardiac mechanical stretch sensor, controls contractility in the zebrafish heart
    • Bendig, G. et al. Integrin-linked kinase, a novel component of the cardiac mechanical stretch sensor, controls contractility in the zebrafish heart. Genes Dev. 20, 2361-2372 (2006).
    • (2006) Genes Dev. , vol.20 , pp. 2361-2372
    • Bendig, G.1
  • 12
    • 34249660635 scopus 로고    scopus 로고
    • Integrin-linked kinase at the heart of cardiac contractility, repair, and disease
    • Hannigan, G. E., Coles, J. G. & Dedhar, S. Integrin-linked kinase at the heart of cardiac contractility, repair, and disease. Circ. Res. 100, 1408-1414 (2007).
    • (2007) Circ. Res. , vol.100 , pp. 1408-1414
    • Hannigan, G.E.1    Coles, J.G.2    Dedhar, S.3
  • 13
    • 34548407064 scopus 로고    scopus 로고
    • Laminin-alpha4 and integrin-linked kinase mutations cause human cardiomyopathy via simultaneous defects in cardiomyocytes and endothelial cells
    • Knoll, R. et al. Laminin-alpha4 and integrin-linked kinase mutations cause human cardiomyopathy via simultaneous defects in cardiomyocytes and endothelial cells. Circulation 116, 515-525 (2007).
    • (2007) Circulation , vol.116 , pp. 515-525
    • Knoll, R.1
  • 14
    • 33748278519 scopus 로고    scopus 로고
    • Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure
    • White, D. E. et al. Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure. Genes Dev. 20, 2355-2360 (2006).
    • (2006) Genes Dev. , vol.20 , pp. 2355-2360
    • White, D.E.1
  • 15
    • 33751226584 scopus 로고    scopus 로고
    • Integrin-linked kinase expression is elevated in human cardiac hypertrophy and induces hypertrophy in transgenic mice
    • Lu, H. et al. Integrin-linked kinase expression is elevated in human cardiac hypertrophy and induces hypertrophy in transgenic mice. Circulation 114, 2271-2279 (2006).
    • (2006) Circulation , vol.114 , pp. 2271-2279
    • Lu, H.1
  • 16
    • 80051499864 scopus 로고    scopus 로고
    • The structure and function of cardiac t-tubules in health and disease
    • Ibrahim, M., Gorelik, J., Yacoub, M. H. & Terracciano, C. M. The structure and function of cardiac t-tubules in health and disease. Proc. Biol. Sci. 278, 2714-2723 (2011).
    • (2011) Proc. Biol. Sci. , vol.278 , pp. 2714-2723
    • Ibrahim, M.1    Gorelik, J.2    Yacoub, M.H.3    Terracciano, C.M.4
  • 17
    • 84907187465 scopus 로고    scopus 로고
    • Patient-specific induced pluripotent stem cells as a model for familial dilated cardiomyopathy
    • Sun, N. et al. Patient-specific induced pluripotent stem cells as a model for familial dilated cardiomyopathy. Sci. Transl. Med. 4, 130ra147 (2012).
    • (2012) Sci. Transl. Med. , vol.4 , pp. 130ra147
    • Sun, N.1
  • 18
    • 84871518109 scopus 로고    scopus 로고
    • Molecular basis of physiological heart growth: Fundamental concepts and new players
    • Maillet, M., van Berlo, J. H. & Molkentin, J. D. Molecular basis of physiological heart growth: fundamental concepts and new players. Nat. Rev. Mol. Cell Biol. 14, 38-48 (2012).
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 38-48
    • Maillet, M.1    Van Berlo, J.H.2    Molkentin, J.D.3
  • 19
    • 67649304830 scopus 로고    scopus 로고
    • Integrin alphavbeta3 upregulates integrin-linked kinase expression in human ovarian cancer cells via enhancement of ILK gene transcription
    • Lossner, D. et al. Integrin alphavbeta3 upregulates integrin-linked kinase expression in human ovarian cancer cells via enhancement of ILK gene transcription. J. Cell Physiol. 220, 367-375 (2009).
    • (2009) J. Cell Physiol. , vol.220 , pp. 367-375
    • Lossner, D.1
  • 20
    • 84893511592 scopus 로고    scopus 로고
    • The role of CaMKII regulation of phospholamban activity in heart disease
    • Mattiazzi, A. & Kranias, E. G. The role of CaMKII regulation of phospholamban activity in heart disease. Front. Pharmacol. 5, 5 (2014).
    • (2014) Front. Pharmacol. , vol.5 , pp. 5
    • Mattiazzi, A.1    Kranias, E.G.2
  • 21
    • 0028882650 scopus 로고
    • Unchanged protein levels of SERCA II and phospholamban but reduced Ca2 + uptake and Ca(2+ )-ATPase activity of cardiac sarcoplasmic reticulum from dilated cardiomyopathy patients compared with patients with nonfailing hearts
    • Schwinger, R. H. et al. Unchanged protein levels of SERCA II and phospholamban but reduced Ca2 + uptake and Ca(2+ )-ATPase activity of cardiac sarcoplasmic reticulum from dilated cardiomyopathy patients compared with patients with nonfailing hearts. Circulation 92, 3220-3228 (1995).
    • (1995) Circulation , vol.92 , pp. 3220-3228
    • Schwinger, R.H.1
  • 22
    • 0028100606 scopus 로고
    • Ca(2+ )-transporting ATPase, phospholamban, and calsequestrin levels in nonfailing and failing human myocardium
    • Movsesian, M. A., Karimi, M., Green, K. & Jones, L. R. Ca(2+ )-transporting ATPase, phospholamban, and calsequestrin levels in nonfailing and failing human myocardium. Circulation 90, 653-657 (1994).
    • (1994) Circulation , vol.90 , pp. 653-657
    • Movsesian, M.A.1    Karimi, M.2    Green, K.3    Jones, L.R.4
  • 23
    • 79251617426 scopus 로고    scopus 로고
    • Stem cells and their derivatives: A renaissance in cardiovascular translational research
    • Kattman, S. J., Koonce, C. H., Swanson, B. J. & Anson, B. D. Stem cells and their derivatives: a renaissance in cardiovascular translational research. J. Cardiovasc. Transl. Res. 4, 66-72 (2011).
    • (2011) J. Cardiovasc. Transl. Res. , vol.4 , pp. 66-72
    • Kattman, S.J.1    Koonce, C.H.2    Swanson, B.J.3    Anson, B.D.4
  • 24
    • 80455164810 scopus 로고    scopus 로고
    • High purity human-induced pluripotent stem cell-derived cardiomyocytes: Electrophysiological properties of action potentials and ionic currents
    • Ma, J. et al. High purity human-induced pluripotent stem cell-derived cardiomyocytes: electrophysiological properties of action potentials and ionic currents. Am. J. Physiol. Heart Circ. Physiol. 301, H2006-H2017 (2011).
    • (2011) Am. J. Physiol. Heart Circ. Physiol. , vol.301 , pp. H2006-H2017
    • Ma, J.1
  • 25
    • 68149166465 scopus 로고    scopus 로고
    • GSK-3beta, a therapeutic target for cardiomyocyte protection
    • Miura, T. & Miki, T. GSK-3beta, a therapeutic target for cardiomyocyte protection. Circ. J. 73, 1184-1192 (2009).
    • (2009) Circ. J. , vol.73 , pp. 1184-1192
    • Miura, T.1    Miki, T.2
  • 26
    • 79951788087 scopus 로고    scopus 로고
    • Remote preconditioning provides potent cardioprotection via PI3K/Akt activation and is associated with nuclear accumulation of beta-catenin
    • Li, J. et al. Remote preconditioning provides potent cardioprotection via PI3K/Akt activation and is associated with nuclear accumulation of beta-catenin. Clin. Sci. (Lond) 120, 451-462 (2011).
    • (2011) Clin. Sci. (Lond) , vol.120 , pp. 451-462
    • Li, J.1
  • 27
    • 80055062698 scopus 로고    scopus 로고
    • Integrin-linked kinase: Not so 'pseudo' after all
    • Hannigan, G. E., McDonald, P. C., Walsh, M. P. & Dedhar, S. Integrin-linked kinase: not so 'pseudo' after all. Oncogene 30, 4375-4385 (2011).
    • (2011) Oncogene , vol.30 , pp. 4375-4385
    • Hannigan, G.E.1    McDonald, P.C.2    Walsh, M.P.3    Dedhar, S.4
  • 28
    • 77957859815 scopus 로고    scopus 로고
    • Integrin-linked kinase is a functional Mn2 +-dependent protein kinase that regulates glycogen synthase kinase-3beta (GSK-3beta) phosphorylation
    • Maydan, M. et al. Integrin-linked kinase is a functional Mn2 +-dependent protein kinase that regulates glycogen synthase kinase-3beta (GSK-3beta) phosphorylation. PLoS ONE 5, e12356 (2010).
    • (2010) PLoS ONE , vol.5 , pp. e12356
    • Maydan, M.1
  • 29
    • 77953638719 scopus 로고    scopus 로고
    • The oncogenic and growth-suppressive functions of the integrin-linked kinase are distinguished by JNK1 expression in human cancer cells
    • Durbin, A. D., Pasic, I., Wong, D. K., Hannigan, G. E. & Malkin, D. The oncogenic and growth-suppressive functions of the integrin-linked kinase are distinguished by JNK1 expression in human cancer cells. Cell Cycle 9, 1951-1959 (2010).
    • (2010) Cell Cycle , vol.9 , pp. 1951-1959
    • Durbin, A.D.1    Pasic, I.2    Wong, D.K.3    Hannigan, G.E.4    Malkin, D.5
  • 30
    • 0026668829 scopus 로고
    • Cardiac-specific phosphorylation site for multifunctional Ca2 +/calmodulin-dependent protein kinase is conserved in the brain ryanodine receptor
    • Witcher, D. R., Strifler, B. A. & Jones, L. R. Cardiac-specific phosphorylation site for multifunctional Ca2 +/calmodulin-dependent protein kinase is conserved in the brain ryanodine receptor. J. Biol. Chem. 267, 4963-4967 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 4963-4967
    • Witcher, D.R.1    Strifler, B.A.2    Jones, L.R.3
  • 31
    • 84859927880 scopus 로고    scopus 로고
    • Ca(2 +)/calmodulin-dependent protein kinase II (CaMKII) in the heart
    • Maier, L. S. Ca(2 +)/calmodulin-dependent protein kinase II (CaMKII) in the heart. Adv. Exp. Med. Biol. 740, 685-702 (2012).
    • (2012) Adv. Exp. Med. Biol. , vol.740 , pp. 685-702
    • Maier, L.S.1
  • 32
    • 79957552048 scopus 로고    scopus 로고
    • Biochemical, proteomic, structural, and thermodynamic characterizations of integrin-linked kinase (ILK): Cross-validation of the pseudokinase
    • Fukuda, K., Knight, J. D., Piszczek, G., Kothary, R. & Qin, J. Biochemical, proteomic, structural, and thermodynamic characterizations of integrin-linked kinase (ILK): cross-validation of the pseudokinase. J. Biol. Chem. 286, 21886-21895 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 21886-21895
    • Fukuda, K.1    Knight, J.D.2    Piszczek, G.3    Kothary, R.4    Qin, J.5
  • 33
    • 0035920145 scopus 로고    scopus 로고
    • Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: Critical roles for kinase activity and amino acids arginine 211 and serine 343
    • Persad, S. et al. Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343. J. Biol. Chem. 276, 27462-27469 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 27462-27469
    • Persad, S.1
  • 34
    • 67749122122 scopus 로고    scopus 로고
    • Targeting PI3K signalling in cancer: Opportunities, challenges and limitations
    • Engelman, J. A. Targeting PI3K signalling in cancer: opportunities, challenges and limitations. Nat. Rev. Cancer 9, 550-562 (2009).
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 550-562
    • Engelman, J.A.1
  • 35
    • 70350064314 scopus 로고    scopus 로고
    • Integrin-linked kinase is an adaptor with essential functions during mouse development
    • Lange, A. et al. Integrin-linked kinase is an adaptor with essential functions during mouse development. Nature 461, 1002-1006 (2009).
    • (2009) Nature , vol.461 , pp. 1002-1006
    • Lange, A.1
  • 36
    • 80052314927 scopus 로고    scopus 로고
    • Doxorubicin-induced cardiac dysfunction is attenuated by ciclosporin treatment in mice through improvements in mitochondrial bioenergetics
    • Marechal, X. et al. Doxorubicin-induced cardiac dysfunction is attenuated by ciclosporin treatment in mice through improvements in mitochondrial bioenergetics. Clin. Sci. (Lond) 121, 405-413 (2011).
    • (2011) Clin. Sci. (Lond) , vol.121 , pp. 405-413
    • Marechal, X.1
  • 38
    • 84870613644 scopus 로고    scopus 로고
    • Cancer therapy-induced cardiac toxicity in early breast cancer: Addressing the unresolved issues
    • Khouri, M. G. et al. Cancer therapy-induced cardiac toxicity in early breast cancer: addressing the unresolved issues. Circulation 126, 2749-2763 (2012).
    • (2012) Circulation , vol.126 , pp. 2749-2763
    • Khouri, M.G.1
  • 39
    • 0034085810 scopus 로고    scopus 로고
    • Acute doxorubicin cardiotoxicity involves cardiomyocyte apoptosis
    • Arola, O. J. et al. Acute doxorubicin cardiotoxicity involves cardiomyocyte apoptosis. Cancer Res. 60, 1789-1792 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 1789-1792
    • Arola, O.J.1
  • 40
    • 0033535974 scopus 로고    scopus 로고
    • Signaling pathways in reactive oxygen species-induced cardiomyocyte apoptosis
    • von Harsdorf, R., Li, P. F. & Dietz, R. Signaling pathways in reactive oxygen species-induced cardiomyocyte apoptosis. Circulation 99, 2934-2941 (1999).
    • (1999) Circulation , vol.99 , pp. 2934-2941
    • Von Harsdorf, R.1    Li, P.F.2    Dietz, R.3
  • 41
    • 77957283607 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum Ca2 + pumping kinetics regulates timing of local Ca2 + releases and spontaneous beating rate of rabbit sinoatrial node pacemaker cells
    • Vinogradova, T. M. et al. Sarcoplasmic reticulum Ca2 + pumping kinetics regulates timing of local Ca2 + releases and spontaneous beating rate of rabbit sinoatrial node pacemaker cells. Circ. Res. 107, 767-775 (2010).
    • (2010) Circ. Res. , vol.107 , pp. 767-775
    • Vinogradova, T.M.1
  • 42
    • 84880935755 scopus 로고    scopus 로고
    • Differential control of calcium homeostasis and vascular reactivity by Ca2 +/calmodulin-dependent kinase II
    • Prasad, A. M. et al. Differential control of calcium homeostasis and vascular reactivity by Ca2 +/calmodulin-dependent kinase II. Hypertension 62, 434-441 (2013).
    • (2013) Hypertension , vol.62 , pp. 434-441
    • Prasad, A.M.1
  • 43
    • 84881480907 scopus 로고    scopus 로고
    • Biowire: A platform for maturation of human pluripotent stem cell-derived cardiomyocytes
    • Nunes, S. S. et al. Biowire: a platform for maturation of human pluripotent stem cell-derived cardiomyocytes. Nat. Methods 10, 781-787 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 781-787
    • Nunes, S.S.1
  • 45
    • 27144443115 scopus 로고    scopus 로고
    • Doxorubicin cardiac dysfunction: Effects on calcium regulatory proteins, sarcoplasmic reticulum, and triiodothyronine
    • Olson, R. D. et al. Doxorubicin cardiac dysfunction: effects on calcium regulatory proteins, sarcoplasmic reticulum, and triiodothyronine. Cardiovasc. Toxicol. 5, 269-283 (2005).
    • (2005) Cardiovasc. Toxicol. , vol.5 , pp. 269-283
    • Olson, R.D.1
  • 46
    • 83055173972 scopus 로고    scopus 로고
    • Impedance-based detection of beating rhythm and proarrhythmic effects of compounds on stem cell-derived cardiomyocytes
    • Jonsson, M. K., Wang, Q. D. & Becker, B. Impedance-based detection of beating rhythm and proarrhythmic effects of compounds on stem cell-derived cardiomyocytes. Assay Drug. Dev. Technol. 9, 589-599 (2011).
    • (2011) Assay Drug. Dev. Technol. , vol.9 , pp. 589-599
    • Jonsson, M.K.1    Wang, Q.D.2    Becker, B.3
  • 47
    • 82855168014 scopus 로고    scopus 로고
    • Functional cardiotoxicity profiling and screening using the xCELLigence RTCA Cardio System
    • Xi, B. et al. Functional cardiotoxicity profiling and screening using the xCELLigence RTCA Cardio System. J. Lab. Autom. 16, 415-421 (2011).
    • (2011) J. Lab. Autom. , vol.16 , pp. 415-421
    • Xi, B.1
  • 48
    • 67651006358 scopus 로고    scopus 로고
    • JNK1 determines the oncogenic or tumor-suppressive activity of the integrin-linked kinase in human rhabdomyosarcoma
    • Durbin, A. D. et al. JNK1 determines the oncogenic or tumor-suppressive activity of the integrin-linked kinase in human rhabdomyosarcoma. J. Clin. Invest. 119, 1558-1570 (2009).
    • (2009) J. Clin. Invest. , vol.119 , pp. 1558-1570
    • Durbin, A.D.1
  • 49
    • 33748061258 scopus 로고    scopus 로고
    • Tissue Doppler imaging predicts left ventricular dysfunction and mortality in a murine model of cardiac injury
    • Neilan, T. G. et al. Tissue Doppler imaging predicts left ventricular dysfunction and mortality in a murine model of cardiac injury. Eur. Heart J. 27, 1868-1875 (2006).
    • (2006) Eur. Heart J. , vol.27 , pp. 1868-1875
    • Neilan, T.G.1
  • 50
    • 79954593490 scopus 로고    scopus 로고
    • Early detection and prediction of cardiotoxicity in chemotherapy-treated patients
    • Sawaya, H. et al. Early detection and prediction of cardiotoxicity in chemotherapy-treated patients. Am. J. Cardiol. 107, 1375-1380 (2011).
    • (2011) Am. J. Cardiol. , vol.107 , pp. 1375-1380
    • Sawaya, H.1
  • 51
    • 84866164871 scopus 로고    scopus 로고
    • Assessment of echocardiography and biomarkers for the extended prediction of cardiotoxicity in patients treated with anthracyclines, taxanes, and trastuzumab
    • Sawaya, H. et al. Assessment of echocardiography and biomarkers for the extended prediction of cardiotoxicity in patients treated with anthracyclines, taxanes, and trastuzumab. Circ. Cardiovasc. Imaging 5, 596-603 (2012).
    • (2012) Circ. Cardiovasc. Imaging , vol.5 , pp. 596-603
    • Sawaya, H.1
  • 52
    • 84861391189 scopus 로고    scopus 로고
    • Vitro model for assessing arrhythmogenic properties of drugs based on high-resolution impedance measurements
    • Nguemo, F. et al. In vitro model for assessing arrhythmogenic properties of drugs based on high-resolution impedance measurements. Cell Physiol. Biochem. 29, 819-832 (2012).
    • (2012) Cell Physiol. Biochem. , vol.29 , pp. 819-832
    • Nguemo, F.1
  • 53
    • 80052342152 scopus 로고    scopus 로고
    • SERCA2a gene transfer decreases sarcoplasmic reticulum calcium leak and reduces ventricular arrhythmias in a model of chronic heart failure
    • Lyon, A. R. et al. SERCA2a gene transfer decreases sarcoplasmic reticulum calcium leak and reduces ventricular arrhythmias in a model of chronic heart failure. Circ. Arrhythm. Electrophysiol. 4, 362-372 (2011).
    • (2011) Circ. Arrhythm. Electrophysiol. , vol.4 , pp. 362-372
    • Lyon, A.R.1
  • 55
    • 14844361721 scopus 로고    scopus 로고
    • Increased nitration of sarcoplasmic reticulum Ca2 +-ATPase in human heart failure
    • Lokuta, A. J. et al. Increased nitration of sarcoplasmic reticulum Ca2 +-ATPase in human heart failure. Circulation 111, 988-995 (2005).
    • (2005) Circulation , vol.111 , pp. 988-995
    • Lokuta, A.J.1
  • 56
    • 84862296973 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase II: Linking heart failure and arrhythmias
    • Swaminathan, P. D., Purohit, A., Hund, T. J. & Anderson, M. E. Calmodulin-dependent protein kinase II: linking heart failure and arrhythmias. Circ. Res. 110, 1661-1677 (2012).
    • (2012) Circ. Res. , vol.110 , pp. 1661-1677
    • Swaminathan, P.D.1    Purohit, A.2    Hund, T.J.3    Anderson, M.E.4
  • 57
    • 84859469380 scopus 로고    scopus 로고
    • CaMKII inhibition in heart failure, beneficial, harmful, or both
    • Cheng, J. et al. CaMKII inhibition in heart failure, beneficial, harmful, or both. Am. J. Physiol. Heart Circ. Physiol. 302, H1454-H1465 (2012).
    • (2012) Am. J. Physiol. Heart Circ. Physiol. , vol.302 , pp. H1454-H1465
    • Cheng, J.1
  • 58
    • 78549243374 scopus 로고    scopus 로고
    • Sequential alterations in Akt, GSK3beta, and calcineurin signalling in the mouse left ventricle after thoracic aortic constriction
    • Previlon, M., Pezet, M., Dachez, C., Mercadier, J. J. & Rouet-Benzineb, P. Sequential alterations in Akt, GSK3beta, and calcineurin signalling in the mouse left ventricle after thoracic aortic constriction. Can. J. Physiol. Pharmacol. 88, 1093-1101 (2010).
    • (2010) Can. J. Physiol. Pharmacol. , vol.88 , pp. 1093-1101
    • Previlon, M.1    Pezet, M.2    Dachez, C.3    Mercadier, J.J.4    Rouet-Benzineb, P.5
  • 59
    • 84857178202 scopus 로고    scopus 로고
    • Differences in MEF2 and NFAT transcriptional pathways according to human heart failure aetiology
    • Cortes, R. et al. Differences in MEF2 and NFAT transcriptional pathways according to human heart failure aetiology. PLoS ONE 7, e30915 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e30915
    • Cortes, R.1
  • 60
    • 84861785221 scopus 로고    scopus 로고
    • LNK (SH2B3) is a key regulator of integrin signaling in endothelial cells and targets alpha-parvin to control cell adhesion and migration
    • Devalliere, J. et al. LNK (SH2B3) is a key regulator of integrin signaling in endothelial cells and targets alpha-parvin to control cell adhesion and migration. FASEB J. 26, 2592-2606 (2013).
    • (2013) FASEB J. , vol.26 , pp. 2592-2606
    • Devalliere, J.1
  • 61
    • 84879561516 scopus 로고    scopus 로고
    • Mutations in the paxillin-binding site of integrin-linked kinase (ILK) destabilize the pseudokinase domain and cause embryonic lethality in mice
    • Moik, D. et al. Mutations in the paxillin-binding site of integrin-linked kinase (ILK) destabilize the pseudokinase domain and cause embryonic lethality in mice. J. Biol. Chem. 288, 18863-18871 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 18863-18871
    • Moik, D.1
  • 62
    • 84856759299 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates vasomotor function by preventing endothelial nitric oxide synthase uncoupling: Role in atherosclerosis
    • Herranz, B. et al. Integrin-linked kinase regulates vasomotor function by preventing endothelial nitric oxide synthase uncoupling: role in atherosclerosis. Circ. Res. 110, 439-449 (2012).
    • (2012) Circ. Res. , vol.110 , pp. 439-449
    • Herranz, B.1
  • 63
    • 80052829997 scopus 로고    scopus 로고
    • The impairment of ILK related angiogenesis involved in cardiac maladaptation after infarction
    • Xie, J. et al. The impairment of ILK related angiogenesis involved in cardiac maladaptation after infarction. PLoS ONE 6, e24115 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e24115
    • Xie, J.1
  • 64
    • 84894100320 scopus 로고    scopus 로고
    • Mutation in integrin-linked kinase (ILKR211A) and heat-shock protein 70 comprise a broadly cardioprotective complex
    • Traister, A. et al. Mutation in integrin-linked kinase (ILKR211A) and heat-shock protein 70 comprise a broadly cardioprotective complex. PLoS ONE 8, e77331 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e77331
    • Traister, A.1
  • 65
    • 18844377152 scopus 로고    scopus 로고
    • Stabilization of integrin-linked kinase by binding to Hsp90
    • Aoyagi, Y., Fujita, N. & Tsuruo, T. Stabilization of integrin-linked kinase by binding to Hsp90. Biochem. Biophys. Res. Commun. 331, 1061-1068 (2005).
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 1061-1068
    • Aoyagi, Y.1    Fujita, N.2    Tsuruo, T.3
  • 67
    • 0035354255 scopus 로고    scopus 로고
    • Use of fluorescent Ca2+ dyes with green fluorescent protein and its variants: Problems and solutions
    • Bolsover, S., Ibrahim, O., O'Luanaigh, N., Williams, H. & Cockcroft, S. Use of fluorescent Ca2+ dyes with green fluorescent protein and its variants: problems and solutions. Biochem. J. 356, 345-352 (2001).
    • (2001) Biochem. J. , vol.356 , pp. 345-352
    • Bolsover, S.1    Ibrahim, O.2    O'Luanaigh, N.3    Williams, H.4    Cockcroft, S.5
  • 68
    • 84869196685 scopus 로고    scopus 로고
    • Subtle alterations in breathing and heart rate control in the 5-HT1A receptor knockout mouse in early postnatal development
    • Barrett, K. T. et al. Subtle alterations in breathing and heart rate control in the 5-HT1A receptor knockout mouse in early postnatal development. J. Appl. Physiol. 113, 1585-1593 (2012).
    • (2012) J. Appl. Physiol. , vol.113 , pp. 1585-1593
    • Barrett, K.T.1
  • 69
    • 84868632918 scopus 로고    scopus 로고
    • Use of cardiac markers for monitoring of doxorubixin-induced cardiotoxicity in children with cancer
    • Pongprot, Y., Sittiwangkul, R., Charoenkwan, P. & Silvilairat, S. Use of cardiac markers for monitoring of doxorubixin-induced cardiotoxicity in children with cancer. J. Pediatr. Hematol. Oncol. 34, 589-595 (2012).
    • (2012) J. Pediatr. Hematol. Oncol. , vol.34 , pp. 589-595
    • Pongprot, Y.1    Sittiwangkul, R.2    Charoenkwan, P.3    Silvilairat, S.4


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