메뉴 건너뛰기




Volumn 25, Issue 5, 2015, Pages 392-397

Role of CaMKII in cardiac arrhythmias

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM ION; N [2 [[N [3 (4 CHLOROPHENYL) 2 PROPENYL] N METHYLAMINO]METHYL]PHENYL] N (2 HYDROXYETHYL) 4 METHOXYBENZENESULFONAMIDE; RANOLAZINE; REACTIVE OXYGEN METABOLITE; SODIUM ION;

EID: 84930759346     PISSN: 10501738     EISSN: 18732615     Source Type: Journal    
DOI: 10.1016/j.tcm.2014.12.001     Document Type: Review
Times cited : (50)

References (62)
  • 1
    • 0028085454 scopus 로고
    • Alternative splicing introduces a nuclear localization signal that targets multifunctional CaM kinase to the nucleus
    • Srinivasan M., Edman C.F., Schulman H. Alternative splicing introduces a nuclear localization signal that targets multifunctional CaM kinase to the nucleus. J Cell Biol 1994, 126:839-852.
    • (1994) J Cell Biol , vol.126 , pp. 839-852
    • Srinivasan, M.1    Edman, C.F.2    Schulman, H.3
  • 2
    • 84856087553 scopus 로고    scopus 로고
    • Location matters: clarifying the concept of nuclear and cytosolic CaMKII subtypes
    • Mishra S., Gray C.B., Miyamoto S., Bers D.M., Brown J.H. Location matters: clarifying the concept of nuclear and cytosolic CaMKII subtypes. Circ Res 2011, 109:1354-1362.
    • (2011) Circ Res , vol.109 , pp. 1354-1362
    • Mishra, S.1    Gray, C.B.2    Miyamoto, S.3    Bers, D.M.4    Brown, J.H.5
  • 3
    • 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 2012, 110:1661-1677.
    • (2012) Circ Res , vol.110 , pp. 1661-1677
    • Swaminathan, P.D.1    Purohit, A.2    Hund, T.J.3    Anderson, M.E.4
  • 5
    • 0028306195 scopus 로고
    • Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals
    • Hanson P.I., Meyer T., Stryer L., Schulman H. Dual role of calmodulin in autophosphorylation of multifunctional CaM kinase may underlie decoding of calcium signals. Neuron 1994, 12:943-956.
    • (1994) Neuron , vol.12 , pp. 943-956
    • Hanson, P.I.1    Meyer, T.2    Stryer, L.3    Schulman, H.4
  • 6
    • 42949085382 scopus 로고    scopus 로고
    • A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation
    • Erickson J.R., Joiner M.L., Guan X., Kutschke W., Yang J., Oddis C.V., et al. A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. Cell 2008, 133:462-474.
    • (2008) Cell , vol.133 , pp. 462-474
    • Erickson, J.R.1    Joiner, M.L.2    Guan, X.3    Kutschke, W.4    Yang, J.5    Oddis, C.V.6
  • 7
    • 84885863770 scopus 로고    scopus 로고
    • Diabetic hyperglycaemia activates CaMKII and arrhythmias by O-linked glycosylation
    • Erickson J.R., Pereira L., Wang L., Han G., Ferguson A., Dao K., et al. Diabetic hyperglycaemia activates CaMKII and arrhythmias by O-linked glycosylation. Nature 2013, 502:372-376.
    • (2013) Nature , vol.502 , pp. 372-376
    • Erickson, J.R.1    Pereira, L.2    Wang, L.3    Han, G.4    Ferguson, A.5    Dao, K.6
  • 8
    • 70349754717 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent kinase II regulation of cardiac ion channels
    • Bers D.M., Grandi E. Calcium/calmodulin-dependent kinase II regulation of cardiac ion channels. J Cardiovasc Pharmacol 2009, 54:180-187.
    • (2009) J Cardiovasc Pharmacol , vol.54 , pp. 180-187
    • Bers, D.M.1    Grandi, E.2
  • 10
    • 84904723563 scopus 로고    scopus 로고
    • 2+ current facilitation is CaMKII-dependent and has arrhythmogenic consequences
    • 2+ current facilitation is CaMKII-dependent and has arrhythmogenic consequences. Front Pharmacol 2014, 5:144.
    • (2014) Front Pharmacol , vol.5 , pp. 144
    • Bers, D.M.1    Morotti, S.2
  • 11
    • 84897111408 scopus 로고    scopus 로고
    • Ryanodine receptor- mediated calcium leak drives progressive development of an atrial fibrillation substrate in a transgenic mouse model
    • Li N., Chiang D.Y., Wang S., Wang Q., Sun L., Voigt N., et al. Ryanodine receptor- mediated calcium leak drives progressive development of an atrial fibrillation substrate in a transgenic mouse model. Circulation 2014, 129:1276-1285.
    • (2014) Circulation , vol.129 , pp. 1276-1285
    • Li, N.1    Chiang, D.Y.2    Wang, S.3    Wang, Q.4    Sun, L.5    Voigt, N.6
  • 14
    • 84872736412 scopus 로고    scopus 로고
    • Regulation of cardiac ATP-sensitive potassium channel surface expression by calcium/calmodulin-dependent protein kinase II
    • Sierra A., Zhu Z., Sapay N., Sharotri V., Kline C.F., Luczak E.D., et al. Regulation of cardiac ATP-sensitive potassium channel surface expression by calcium/calmodulin-dependent protein kinase II. J Biol Chem 2013, 288:1568-1581.
    • (2013) J Biol Chem , vol.288 , pp. 1568-1581
    • Sierra, A.1    Zhu, Z.2    Sapay, N.3    Sharotri, V.4    Kline, C.F.5    Luczak, E.D.6
  • 15
    • 77956528473 scopus 로고    scopus 로고
    • Ankyrin-B regulates Kir6.2 membrane expression and function in heart
    • Li J., Kline C.F., Hund T.J., Anderson M.E., Mohler P.J. Ankyrin-B regulates Kir6.2 membrane expression and function in heart. J Biol Chem 2010, 285:28723-28730.
    • (2010) J Biol Chem , vol.285 , pp. 28723-28730
    • Li, J.1    Kline, C.F.2    Hund, T.J.3    Anderson, M.E.4    Mohler, P.J.5
  • 16
    • 77954518589 scopus 로고    scopus 로고
    • Cardiomyocytes with disrupted CFTR function require CaMKII and Ca(2+)-activated Cl(-) channel activity to maintain contraction rate
    • Sellers Z.M., De Arcangelis V., Xiang Y., Best P.M. Cardiomyocytes with disrupted CFTR function require CaMKII and Ca(2+)-activated Cl(-) channel activity to maintain contraction rate. J Physiol 2010, 588:2417-2429.
    • (2010) J Physiol , vol.588 , pp. 2417-2429
    • Sellers, Z.M.1    De Arcangelis, V.2    Xiang, Y.3    Best, P.M.4
  • 18
    • 64249148329 scopus 로고    scopus 로고
    • Sticky fingers: CaMKII finds a home on another ion channel
    • Anderson M.E. Sticky fingers: CaMKII finds a home on another ion channel. Circ Res 2009, 104:712-714.
    • (2009) Circ Res , vol.104 , pp. 712-714
    • Anderson, M.E.1
  • 20
    • 77950419553 scopus 로고    scopus 로고
    • CaV1.2 beta-subunit coordinates CaMKII-triggered cardiomyocyte death and afterdepolarizations
    • Koval O.M., Guan X., Wu Y., Joiner M.L., Gao Z., Chen B., et al. CaV1.2 beta-subunit coordinates CaMKII-triggered cardiomyocyte death and afterdepolarizations. Proc Natl Acad Sci U S A 2010, 107:4996-5000.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 4996-5000
    • Koval, O.M.1    Guan, X.2    Wu, Y.3    Joiner, M.L.4    Gao, Z.5    Chen, B.6
  • 21
    • 77957838101 scopus 로고    scopus 로고
    • A betaIV spectrin/CaMKII signaling complex is essential for membrane excitability in mice
    • Hund T.J., Koval O.M., Li J., Wright P.J., Qian L., Snyder J.S., et al. A betaIV spectrin/CaMKII signaling complex is essential for membrane excitability in mice. J Clin Invest 2010, 120:3508-3519.
    • (2010) J Clin Invest , vol.120 , pp. 3508-3519
    • Hund, T.J.1    Koval, O.M.2    Li, J.3    Wright, P.J.4    Qian, L.5    Snyder, J.S.6
  • 22
    • 84922392783 scopus 로고    scopus 로고
    • Ankyrin-G coordinates intercalated disc signaling platform to regulate cardiac excitability in vivo
    • Makara M.A., Curran J., Little S., Musa H., Polina I., Smith S.A., et al. Ankyrin-G coordinates intercalated disc signaling platform to regulate cardiac excitability in vivo. Circ Res 2014, 115:929-938.
    • (2014) Circ Res , vol.115 , pp. 929-938
    • Makara, M.A.1    Curran, J.2    Little, S.3    Musa, H.4    Polina, I.5    Smith, S.A.6
  • 23
    • 64249158777 scopus 로고    scopus 로고
    • Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes
    • El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H., et al. Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes. Circ Res 2009, 104:758-769.
    • (2009) Circ Res , vol.104 , pp. 758-769
    • El-Haou, S.1    Balse, E.2    Neyroud, N.3    Dilanian, G.4    Gavillet, B.5    Abriel, H.6
  • 24
    • 0038643573 scopus 로고    scopus 로고
    • The deltaC isoform of CaMKII is activated in cardiac hypertrophy and induces dilated cardiomyopathy and heart failure
    • Zhang T., Maier L.S., Dalton N.D., Miyamoto S., Ross J., Bers D.M., et al. The deltaC isoform of CaMKII is activated in cardiac hypertrophy and induces dilated cardiomyopathy and heart failure. Circ Res 2003, 92:912-919.
    • (2003) Circ Res , vol.92 , pp. 912-919
    • Zhang, T.1    Maier, L.S.2    Dalton, N.D.3    Miyamoto, S.4    Ross, J.5    Bers, D.M.6
  • 25
    • 60549085044 scopus 로고    scopus 로고
    • The delta isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload
    • Backs J., Backs T., Neef S., Kreusser M.M., Lehmann L.H., Patrick D.M., et al. The delta isoform of CaM kinase II is required for pathological cardiac hypertrophy and remodeling after pressure overload. Proc Natl Acad Sci U S A 2009, 106:2342-2347.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2342-2347
    • Backs, J.1    Backs, T.2    Neef, S.3    Kreusser, M.M.4    Lehmann, L.H.5    Patrick, D.M.6
  • 26
    • 66449097490 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent kinase II in the transition from pressure overload- induced cardiac hypertrophy to heart failure in mice
    • 2+/calmodulin-dependent kinase II in the transition from pressure overload- induced cardiac hypertrophy to heart failure in mice. J Clin Invest 2009, 119:1230-1240.
    • (2009) J Clin Invest , vol.119 , pp. 1230-1240
    • Ling, H.1    Zhang, T.2    Pereira, L.3    Means, C.K.4    Cheng, H.5    Gu, Y.6
  • 27
    • 84897952396 scopus 로고    scopus 로고
    • CaMKII in sinoatrial node physiology and dysfunction
    • Wu Y., Anderson M.E. CaMKII in sinoatrial node physiology and dysfunction. Front Pharmacol 2014, 5:48.
    • (2014) Front Pharmacol , vol.5 , pp. 48
    • Wu, Y.1    Anderson, M.E.2
  • 28
    • 84905050495 scopus 로고    scopus 로고
    • Arrhythmias, elicited by catecholamines and serotonin, vanish in human chronic atrial fibrillation
    • Christ T., Rozmaritsa N., Engel A., Berk E., Knaut M., Metzner K., et al. Arrhythmias, elicited by catecholamines and serotonin, vanish in human chronic atrial fibrillation. Proc Natl Acad Sci U S A 2014, 111:11193-11198.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 11193-11198
    • Christ, T.1    Rozmaritsa, N.2    Engel, A.3    Berk, E.4    Knaut, M.5    Metzner, K.6
  • 29
    • 84901014984 scopus 로고    scopus 로고
    • Numerical Modeling Calcium and CaMKII Effects in the SA Node
    • Yaniv Y., Maltsev V.A. Numerical Modeling Calcium and CaMKII Effects in the SA Node. Front Pharmacol 2014, 5:58.
    • (2014) Front Pharmacol , vol.5 , pp. 58
    • Yaniv, Y.1    Maltsev, V.A.2
  • 30
    • 84902346655 scopus 로고    scopus 로고
    • Metabolic memory of ss-cells controls insulin secretion and is mediated by CaMKII
    • Santos G.J., Ferreira S.M., Ortis F., Rezende L.F., Li C., Naji A., et al. Metabolic memory of ss-cells controls insulin secretion and is mediated by CaMKII. Mol Metab 2014, 3:484-489.
    • (2014) Mol Metab , vol.3 , pp. 484-489
    • Santos, G.J.1    Ferreira, S.M.2    Ortis, F.3    Rezende, L.F.4    Li, C.5    Naji, A.6
  • 31
    • 84889674935 scopus 로고    scopus 로고
    • Activation of calcium/calmodulin-dependent protein kinase II in obesity mediates suppression of hepatic insulin signaling
    • Ozcan L., Cristina de Souza J., Harari A.A., Backs J., Olson E.N., Tabas I. Activation of calcium/calmodulin-dependent protein kinase II in obesity mediates suppression of hepatic insulin signaling. Cell Metab 2013, 18:803-815.
    • (2013) Cell Metab , vol.18 , pp. 803-815
    • Ozcan, L.1    Cristina de Souza, J.2    Harari, A.A.3    Backs, J.4    Olson, E.N.5    Tabas, I.6
  • 32
    • 84901377446 scopus 로고    scopus 로고
    • High-fat diet-induced mitochondrial biogenesis is regulated by mitochondrial-derived reactive oxygen species activation of CaMKII
    • Jain S.S., Paglialunga S., Vigna C., Ludzki A., Herbst E.A., Lally J.S., et al. High-fat diet-induced mitochondrial biogenesis is regulated by mitochondrial-derived reactive oxygen species activation of CaMKII. Diabetes 2014, 63:1907-1913.
    • (2014) Diabetes , vol.63 , pp. 1907-1913
    • Jain, S.S.1    Paglialunga, S.2    Vigna, C.3    Ludzki, A.4    Herbst, E.A.5    Lally, J.S.6
  • 33
    • 84870440232 scopus 로고    scopus 로고
    • CaMKII inhibition rescues pro-arrhythmic phenotypes in model of human ankyrin-B syndrome
    • DeGrande S., Nixon D., Koval O., Curran J.W., Wright P., Wang Q., et al. CaMKII inhibition rescues pro-arrhythmic phenotypes in model of human ankyrin-B syndrome. Heart Rhythm 2012, 9:2034-2041.
    • (2012) Heart Rhythm , vol.9 , pp. 2034-2041
    • DeGrande, S.1    Nixon, D.2    Koval, O.3    Curran, J.W.4    Wright, P.5    Wang, Q.6
  • 36
    • 57749181755 scopus 로고    scopus 로고
    • Proarrhythmic defects in Timothy syndrome require calmodulin kinase II
    • Thiel W.H., Chen B., Hund T.J., Koval O.M., Purohit A., Song L.S., et al. Proarrhythmic defects in Timothy syndrome require calmodulin kinase II. Circulation 2008, 118:2225-2234.
    • (2008) Circulation , vol.118 , pp. 2225-2234
    • Thiel, W.H.1    Chen, B.2    Hund, T.J.3    Koval, O.M.4    Purohit, A.5    Song, L.S.6
  • 37
    • 84895517603 scopus 로고    scopus 로고
    • CaMKII inhibitors: from research tools to therapeutic agents
    • Pellicena P., Schulman H. CaMKII inhibitors: from research tools to therapeutic agents. Front Pharmacol 2014, 5:21.
    • (2014) Front Pharmacol , vol.5 , pp. 21
    • Pellicena, P.1    Schulman, H.2
  • 38
    • 84880328248 scopus 로고    scopus 로고
    • Role of late sodium current as a potential arrhythmogenic mechanism in the progression of pressure-induced heart disease
    • Toischer K., Hartmann N., Wagner S., Fischer T.H., Herting J., Danner B.C., et al. Role of late sodium current as a potential arrhythmogenic mechanism in the progression of pressure-induced heart disease. J Mol Cell Cardiol 2013, 61:111-122.
    • (2013) J Mol Cell Cardiol , vol.61 , pp. 111-122
    • Toischer, K.1    Hartmann, N.2    Wagner, S.3    Fischer, T.H.4    Herting, J.5    Danner, B.C.6
  • 39
    • 0032898049 scopus 로고    scopus 로고
    • Repolarization abnormalities in cardiomyocytes of dogs with chronic heart failure: role of sustained inward current
    • Undrovinas A.I., Maltsev V.A., Sabbah H.N. Repolarization abnormalities in cardiomyocytes of dogs with chronic heart failure: role of sustained inward current. Cell Mol Life Sci 1999, 55:494-505.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 494-505
    • Undrovinas, A.I.1    Maltsev, V.A.2    Sabbah, H.N.3
  • 42
    • 84862001882 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II (CaMKII) regulates cardiac sodium channel NaV1.5 gating by multiple phosphorylation sites
    • 2+/calmodulin-dependent protein kinase II (CaMKII) regulates cardiac sodium channel NaV1.5 gating by multiple phosphorylation sites. J Biol Chem 2012, 287:19856-19869.
    • (2012) J Biol Chem , vol.287 , pp. 19856-19869
    • Ashpole, N.M.1    Herren, A.W.2    Ginsburg, K.S.3    Brogan, J.D.4    Johnson, D.E.5    Cummins, T.R.6
  • 43
    • 84870954315 scopus 로고    scopus 로고
    • Mass spectrometry-based identification of native cardiac Nav1.5 channel alpha subunit phosphorylation sites
    • Marionneau C., Lichti C.F., Lindenbaum P., Charpentier F., Nerbonne J.M., Townsend R.R., et al. Mass spectrometry-based identification of native cardiac Nav1.5 channel alpha subunit phosphorylation sites. J Proteome Res 2012, 11:5994-6007.
    • (2012) J Proteome Res , vol.11 , pp. 5994-6007
    • Marionneau, C.1    Lichti, C.F.2    Lindenbaum, P.3    Charpentier, F.4    Nerbonne, J.M.5    Townsend, R.R.6
  • 45
    • 82455175177 scopus 로고    scopus 로고
    • Subcellular heterogeneity of sodium current properties in adult cardiac ventricular myocytes
    • Lin X., Liu N., Lu J., Zhang J., Anumonwo J.M., Isom L.L., et al. Subcellular heterogeneity of sodium current properties in adult cardiac ventricular myocytes. Heart Rhythm 2011, 8:1923-1930.
    • (2011) Heart Rhythm , vol.8 , pp. 1923-1930
    • Lin, X.1    Liu, N.2    Lu, J.3    Zhang, J.4    Anumonwo, J.M.5    Isom, L.L.6
  • 46
    • 15744405775 scopus 로고    scopus 로고
    • Nav1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Nav1.5 on the surface of cardiomyocytes
    • Mohler P.J., Rivolta I., Napolitano C., LeMaillet G., Lambert S., Priori S.G., et al. Nav1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Nav1.5 on the surface of cardiomyocytes. Proc Natl Acad Sci U S A 2004, 101:17533-17538.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17533-17538
    • Mohler, P.J.1    Rivolta, I.2    Napolitano, C.3    LeMaillet, G.4    Lambert, S.5    Priori, S.G.6
  • 47
    • 33747425933 scopus 로고    scopus 로고
    • Cardiac sodium channel Nav1.5 is regulated by a multiprotein complex composed of syntrophins and dystrophin
    • Gavillet B., Rougier J.S., Domenighetti A.A., Behar R., Boixel C., Ruchat P., et al. Cardiac sodium channel Nav1.5 is regulated by a multiprotein complex composed of syntrophins and dystrophin. Circ Res 2006, 99:407-414.
    • (2006) Circ Res , vol.99 , pp. 407-414
    • Gavillet, B.1    Rougier, J.S.2    Domenighetti, A.A.3    Behar, R.4    Boixel, C.5    Ruchat, P.6
  • 48
    • 84904053841 scopus 로고    scopus 로고
    • PDZ domain-binding motif regulates cardiomyocyte compartment-specific NaV1.5 channel expression and function
    • Shy D., Gillet L., Ogrodnik J., Albesa M., Verkerk A.O., Wolswinkel R., et al. PDZ domain-binding motif regulates cardiomyocyte compartment-specific NaV1.5 channel expression and function. Circulation 2014, 130:147-160.
    • (2014) Circulation , vol.130 , pp. 147-160
    • Shy, D.1    Gillet, L.2    Ogrodnik, J.3    Albesa, M.4    Verkerk, A.O.5    Wolswinkel, R.6
  • 49
    • 48249148221 scopus 로고    scopus 로고
    • Syntrophin mutation associated with long QT syndrome through activation of the nNOS-SCN5A macromolecular complex
    • Ueda K., Valdivia C., Medeiros-Domingo A., Tester D.J., Vatta M., Farrugia G., et al. Syntrophin mutation associated with long QT syndrome through activation of the nNOS-SCN5A macromolecular complex. Proc Natl Acad Sci U S A 2008, 105:9355-9360.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9355-9360
    • Ueda, K.1    Valdivia, C.2    Medeiros-Domingo, A.3    Tester, D.J.4    Vatta, M.5    Farrugia, G.6
  • 50
    • 84901034764 scopus 로고    scopus 로고
    • Modeling CaMKII-mediated regulation of l-type Ca(2+) channels and ryanodine receptors in the heart
    • Greenstein J.L., Foteinou P.T., Hashambhoy-Ramsay Y.L., Winslow R.L. Modeling CaMKII-mediated regulation of l-type Ca(2+) channels and ryanodine receptors in the heart. Front Pharmacol 2014, 5:60.
    • (2014) Front Pharmacol , vol.5 , pp. 60
    • Greenstein, J.L.1    Foteinou, P.T.2    Hashambhoy-Ramsay, Y.L.3    Winslow, R.L.4
  • 51
    • 84895560919 scopus 로고    scopus 로고
    • Modeling CaMKII in cardiac physiology: from molecule to tissue
    • Onal B., Unudurthi S.D., Hund T.J. Modeling CaMKII in cardiac physiology: from molecule to tissue. Front Pharmacol 2014, 5:9.
    • (2014) Front Pharmacol , vol.5 , pp. 9
    • Onal, B.1    Unudurthi, S.D.2    Hund, T.J.3
  • 52
    • 8744246332 scopus 로고    scopus 로고
    • Rate dependence and regulation of action potential and calcium transient in a canine cardiac ventricular cell model
    • Hund T.J., Rudy Y. Rate dependence and regulation of action potential and calcium transient in a canine cardiac ventricular cell model. Circulation 2004, 110:3168-3174.
    • (2004) Circulation , vol.110 , pp. 3168-3174
    • Hund, T.J.1    Rudy, Y.2
  • 54
    • 74549157674 scopus 로고    scopus 로고
    • Oxidized calmodulin kinase II regulates conduction following myocardial infarction: a computational analysis
    • Christensen M.D., Dun W., Boyden P.A., Anderson M.E., Mohler P.J., Hund T.J. Oxidized calmodulin kinase II regulates conduction following myocardial infarction: a computational analysis. PLoS Comput Biol 2009, 5:e1000583.
    • (2009) PLoS Comput Biol , vol.5 , pp. e1000583
    • Christensen, M.D.1    Dun, W.2    Boyden, P.A.3    Anderson, M.E.4    Mohler, P.J.5    Hund, T.J.6
  • 55
    • 50449107767 scopus 로고    scopus 로고
    • Role of activated CaMKII in abnormal calcium homeostasis and INa remodeling after myocardial infarction: insights from mathematical modeling
    • Hund T.J., Decker K.F., Kanter E., Mohler P.J., Boyden P.A., Schuessler R.B., et al. Role of activated CaMKII in abnormal calcium homeostasis and INa remodeling after myocardial infarction: insights from mathematical modeling. J Mol Cell Cardiol 2008, 45:420-428.
    • (2008) J Mol Cell Cardiol , vol.45 , pp. 420-428
    • Hund, T.J.1    Decker, K.F.2    Kanter, E.3    Mohler, P.J.4    Boyden, P.A.5    Schuessler, R.B.6
  • 57
    • 70349435474 scopus 로고    scopus 로고
    • Regulation of excitation-contraction coupling in mouse cardiac myocytes: integrative analysis with mathematical modelling
    • Koivumaki J.T., Korhonen T., Takalo J., Weckstrom M., Tavi P. Regulation of excitation-contraction coupling in mouse cardiac myocytes: integrative analysis with mathematical modelling. BMC Physiol 2009, 9:16.
    • (2009) BMC Physiol , vol.9 , pp. 16
    • Koivumaki, J.T.1    Korhonen, T.2    Takalo, J.3    Weckstrom, M.4    Tavi, P.5
  • 60
    • 84874607556 scopus 로고    scopus 로고
    • Diabetes increases mortality after myocardial infarction by oxidizing CaMKII
    • Luo M., Guan X., Di L., Kutschke W., Gao Z., Yang J., et al. Diabetes increases mortality after myocardial infarction by oxidizing CaMKII. J Clin Invest 2013, 123:1262-1274.
    • (2013) J Clin Invest , vol.123 , pp. 1262-1274
    • Luo, M.1    Guan, X.2    Di, L.3    Kutschke, W.4    Gao, Z.5    Yang, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.