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Volumn 296, Issue 1, 2009, Pages

Expression of active p21-activated kinase-1 induces Ca2+ flux modification with altered regulatory protein phosphorylation in cardiac myocytes

Author keywords

Cardiac relaxation; Phosphatase; Sarcoplasmic reticulum

Indexed keywords

BETA GALACTOSIDASE; CAFFEINE; CALCIUM ION; ISOPRENALINE; P21 ACTIVATED KINASE 1; PHOSPHOLAMBAN; SERINE; THREONINE; TROPONIN I;

EID: 58349095764     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00012.2008     Document Type: Article
Times cited : (34)

References (67)
  • 1
    • 0029029280 scopus 로고
    • Fractional SR Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes
    • Bassani JW, Yuan W, Bers DM. Fractional SR Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes. Am J Physiol Cell Physiol 268: C1313-C1319, 1995.
    • (1995) Am J Physiol Cell Physiol , vol.268
    • Bassani, J.W.1    Yuan, W.2    Bers, D.M.3
  • 4
    • 0032478605 scopus 로고    scopus 로고
    • A GTPase-independent mechanism of p21-activated kinase activation. Regulation by sphingosine and other biologically active lipids
    • Bokoch GM, Reilly AM, Daniels RH, King CC, Olivera A, Spiegel S, Knaus UG. A GTPase-independent mechanism of p21-activated kinase activation. Regulation by sphingosine and other biologically active lipids. J Biol Chem 273: 8137-8144, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 8137-8144
    • Bokoch, G.M.1    Reilly, A.M.2    Daniels, R.H.3    King, C.C.4    Olivera, A.5    Spiegel, S.6    Knaus, U.G.7
  • 5
    • 0028170950 scopus 로고
    • i during excitation-contraction coupling in cardiac myocytes
    • i during excitation-contraction coupling in cardiac myocytes. Biophys J 67: 1942-1956, 1994.
    • (1994) Biophys J , vol.67 , pp. 1942-1956
    • Cannell, M.B.1    Cheng, H.2    Lederer, W.J.3
  • 6
    • 0029005888 scopus 로고
    • The control of calcium release in heart muscle
    • Cannell MB, Cheng H, Lederer WJ. The control of calcium release in heart muscle. Science 268: 1045-1049, 1995.
    • (1995) Science , vol.268 , pp. 1045-1049
    • Cannell, M.B.1    Cheng, H.2    Lederer, W.J.3
  • 7
    • 0026786471 scopus 로고
    • Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation
    • Chen J, Martin BL, Brautigan DL. Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation. Science 257: 1261-1264, 1992.
    • (1992) Science , vol.257 , pp. 1261-1264
    • Chen, J.1    Martin, B.L.2    Brautigan, D.L.3
  • 9
    • 0027426069 scopus 로고
    • Calcium sparks: Elementary events underlying excitation-contraction coupling in heart muscle
    • Cheng H, Lederer WJ, Cannell MB. Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle. Science 262: 740-744, 1993.
    • (1993) Science , vol.262 , pp. 740-744
    • Cheng, H.1    Lederer, W.J.2    Cannell, M.B.3
  • 10
    • 0033037673 scopus 로고    scopus 로고
    • Amplitude distribution of calcium sparks in confocal images: Theory and studies with an automatic detection method
    • Cheng H, Song LS, Shirokova N, Gonzalez A, Lakatta EG, Rios E, Stern MD. Amplitude distribution of calcium sparks in confocal images: theory and studies with an automatic detection method. Biophys J 76: 606-617, 1999.
    • (1999) Biophys J , vol.76 , pp. 606-617
    • Cheng, H.1    Song, L.S.2    Shirokova, N.3    Gonzalez, A.4    Lakatta, E.G.5    Rios, E.6    Stern, M.D.7
  • 11
    • 51649101651 scopus 로고    scopus 로고
    • A simulation study on the activation of cardiac CaMKIIδ-isoform and its regulation by phosphatases
    • Chiba H, Schneider N, Matsuoka S, Noma A. A simulation study on the activation of cardiac CaMKIIδ-isoform and its regulation by phosphatases. Biophys J 95: 2139-2149, 2008.
    • (2008) Biophys J , vol.95 , pp. 2139-2149
    • Chiba, H.1    Schneider, N.2    Matsuoka, S.3    Noma, A.4
  • 12
    • 0033199655 scopus 로고    scopus 로고
    • p21-activated protein kinase: A crucial component of morphological signaling?
    • Daniels RH, Bokoch GM. p21-activated protein kinase: a crucial component of morphological signaling? Trends Biochem Sci 24: 350-355, 1999.
    • (1999) Trends Biochem Sci , vol.24 , pp. 350-355
    • Daniels, R.H.1    Bokoch, G.M.2
  • 13
    • 0036702654 scopus 로고    scopus 로고
    • Frequency-dependent acceleration of relaxation in the heart depends on CaMKII, but not phospholamban
    • DeSantiago J, Maier LS, Bers DM. Frequency-dependent acceleration of relaxation in the heart depends on CaMKII, but not phospholamban. J Mol Cell Cardiol 34: 975-984, 2002.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 975-984
    • DeSantiago, J.1    Maier, L.S.2    Bers, D.M.3
  • 14
    • 0030016356 scopus 로고    scopus 로고
    • Dynamic modulation of excitation-contraction coupling by protein phosphatases in rat ventricular myocytes
    • duBell W, Lederer W, Rogers T. Dynamic modulation of excitation-contraction coupling by protein phosphatases in rat ventricular myocytes. J Physiol 493: 793-800, 1996.
    • (1996) J Physiol , vol.493 , pp. 793-800
    • duBell, W.1    Lederer, W.2    Rogers, T.3
  • 16
    • 0023957833 scopus 로고
    • Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts
    • Garvey JL, Kranias EG, Solaro RJ. Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts. Biochem J 249: 709-714, 1988.
    • (1988) Biochem J , vol.249 , pp. 709-714
    • Garvey, J.L.1    Kranias, E.G.2    Solaro, R.J.3
  • 17
    • 21644448038 scopus 로고    scopus 로고
    • A B56 regulatory subunit of protein phosphatase 2A localizes to nuclear speckles in cardiomyocytes
    • Gigena MS, Ito A, Nojima H, Rogers TB. A B56 regulatory subunit of protein phosphatase 2A localizes to nuclear speckles in cardiomyocytes. Am J Physiol Heart Circ Physiol 289: H285-H294, 2005.
    • (2005) Am J Physiol Heart Circ Physiol , vol.289
    • Gigena, M.S.1    Ito, A.2    Nojima, H.3    Rogers, T.B.4
  • 22
    • 0029781650 scopus 로고    scopus 로고
    • Calcium gradients during excitation-contraction coupling in cat atrial myocytes
    • Hüser J, Lipsius SL, Blatter LA. Calcium gradients during excitation-contraction coupling in cat atrial myocytes. J Physiol 494: 641-651, 1996.
    • (1996) J Physiol , vol.494 , pp. 641-651
    • Hüser, J.1    Lipsius, S.L.2    Blatter, L.A.3
  • 23
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens V, Goris J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem J 353: 417-439, 2001.
    • (2001) Biochem J , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 24
    • 0034623827 scopus 로고    scopus 로고
    • Regulation of cardiac L-type calcium channels by protein kinase A and protein kinase C
    • Kamp TJ, Hell JW. Regulation of cardiac L-type calcium channels by protein kinase A and protein kinase C. Circ Res 87: 1095-1102, 2000.
    • (2000) Circ Res , vol.87 , pp. 1095-1102
    • Kamp, T.J.1    Hell, J.W.2
  • 25
    • 34248364400 scopus 로고    scopus 로고
    • Regulation of L-type calcium channel and delayed rectifier potassium channel activity by p21-activated kinase-1 in guinea pig sinoatrial node pacemaker cells
    • Ke Y, Lei M, Collins TP, Rakovic S, Mattick PA, Yamasaki M, Brodie MS, Terrar DA, Solaro RJ. Regulation of L-type calcium channel and delayed rectifier potassium channel activity by p21-activated kinase-1 in guinea pig sinoatrial node pacemaker cells. Circ Res 100: 1317-1327, 2007.
    • (2007) Circ Res , vol.100 , pp. 1317-1327
    • Ke, Y.1    Lei, M.2    Collins, T.P.3    Rakovic, S.4    Mattick, P.A.5    Yamasaki, M.6    Brodie, M.S.7    Terrar, D.A.8    Solaro, R.J.9
  • 26
    • 1042279545 scopus 로고    scopus 로고
    • Intracellular localization and functional effects of p21-activated kinase-1 (Pak1) in cardiac myocytes
    • Ke Y, Wang L, Pyle WG, de Tombe PP, Solaro RJ. Intracellular localization and functional effects of p21-activated kinase-1 (Pak1) in cardiac myocytes. Circ Res 94: 194-200, 2004.
    • (2004) Circ Res , vol.94 , pp. 194-200
    • Ke, Y.1    Wang, L.2    Pyle, W.G.3    de Tombe, P.P.4    Solaro, R.J.5
  • 27
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle
    • Kentish JC, McCloskey DT, Layland J, Palmer S, Leiden JM, Martin AF, Solaro RJ. Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle. Circ Res 88: 1059-1065, 2001.
    • (2001) Circ Res , vol.88 , pp. 1059-1065
    • Kentish, J.C.1    McCloskey, D.T.2    Layland, J.3    Palmer, S.4    Leiden, J.M.5    Martin, A.F.6    Solaro, R.J.7
  • 29
    • 0020477578 scopus 로고
    • Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart
    • Kranias EG, Solaro RJ. Phosphorylation of troponin I and phospholamban during catecholamine stimulation of rabbit heart. Nature 298: 182-184, 1982.
    • (1982) Nature , vol.298 , pp. 182-184
    • Kranias, E.G.1    Solaro, R.J.2
  • 30
    • 0023736065 scopus 로고
    • Purification and characterization of phospholamban phosphatase from cardiac muscle
    • Kranias EG, Steenaart NA, Di Salvo J. Purification and characterization of phospholamban phosphatase from cardiac muscle. J Biol Chem 263: 15681-15687, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 15681-15687
    • Kranias, E.G.1    Steenaart, N.A.2    Di Salvo, J.3
  • 32
  • 33
    • 0036783558 scopus 로고    scopus 로고
    • 1 receptor-mediated protein phosphatase 2a activation in the heart
    • 1 receptor-mediated protein phosphatase 2a activation in the heart. Am J Physiol Heart Circ Physiol 283: H1314-H1321, 2002.
    • (2002) Am J Physiol Heart Circ Physiol , vol.283
    • Liu, Q.1    Hofmann, P.A.2
  • 34
    • 0029080486 scopus 로고
    • Modulation of cardiac ryanodine receptors of swine and rabbit by a phosphorylation- dephosphorylation mechanism
    • Lokuta AJ, Rogers TB, Lederer WJ, Valdivia HH. Modulation of cardiac ryanodine receptors of swine and rabbit by a phosphorylation- dephosphorylation mechanism. J Physiol 487: 609-622, 1995.
    • (1995) J Physiol , vol.487 , pp. 609-622
    • Lokuta, A.J.1    Rogers, T.B.2    Lederer, W.J.3    Valdivia, H.H.4
  • 35
    • 0029038461 scopus 로고
    • Local calcium transients triggered by single L-type calcium channel currents in cardiac cells
    • Lopez-Lopez JR, Shacklock PS, Balke CW, Wier WG. Local calcium transients triggered by single L-type calcium channel currents in cardiac cells. Science 268: 1042-1045, 1995.
    • (1995) Science , vol.268 , pp. 1042-1045
    • Lopez-Lopez, J.R.1    Shacklock, P.S.2    Balke, C.W.3    Wier, W.G.4
  • 39
    • 42549130368 scopus 로고    scopus 로고
    • Adrenergic regulation of cardiac contractility does not involve phosphorylation of the cardiac ryanodine receptor at serine 2808
    • MacDonnell SM, Garcia-Rivas G, Scherman JA, Kubo H, Chen X, Valdivia H, Houser SR. Adrenergic regulation of cardiac contractility does not involve phosphorylation of the cardiac ryanodine receptor at serine 2808. Circ Res 102: e65-e72, 2008.
    • (2008) Circ Res , vol.102
    • MacDonnell, S.M.1    Garcia-Rivas, G.2    Scherman, J.A.3    Kubo, H.4    Chen, X.5    Valdivia, H.6    Houser, S.R.7
  • 40
    • 0026016543 scopus 로고
    • Identification of the major protein phosphatases in mammalian cardiac muscle which dephosphorylate phospholamban
    • MacDougall LK, Jones LR, Cohen P. Identification of the major protein phosphatases in mammalian cardiac muscle which dephosphorylate phospholamban. Eur J Biochem 196: 725-734, 1991.
    • (1991) Eur J Biochem , vol.196 , pp. 725-734
    • MacDougall, L.K.1    Jones, L.R.2    Cohen, P.3
  • 41
    • 0036702526 scopus 로고    scopus 로고
    • Calcium, calmodulin, and calcium-calmodulin kinase II: Heartbeat to heartbeat and beyond
    • Maier LS, Bers DM. Calcium, calmodulin, and calcium-calmodulin kinase II: heartbeat to heartbeat and beyond. J Mol Cell Cardiol 34: 919-939, 2002.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 919-939
    • Maier, L.S.1    Bers, D.M.2
  • 42
    • 0031036626 scopus 로고    scopus 로고
    • Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes
    • Manser E, Huang HY, Loo TH, Chen XQ, Dong JM, Leung T, Lim L. Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes. Mol Cell Biol 17: 1129-1143, 1997.
    • (1997) Mol Cell Biol , vol.17 , pp. 1129-1143
    • Manser, E.1    Huang, H.Y.2    Loo, T.H.3    Chen, X.Q.4    Dong, J.M.5    Leung, T.6    Lim, L.7
  • 43
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by cdc42 and Rac1
    • Manser E, Leung T, Salihuddin H, Zhao Zs, Lim L. A brain serine/threonine protein kinase activated by cdc42 and Rac1. Nature 367: 40-46, 1994.
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.4    Lim, L.5
  • 44
    • 0034973680 scopus 로고    scopus 로고
    • Ryanodine receptors/calcium release channels in heart failure and sudden cardiac death
    • Marks AR. Ryanodine receptors/calcium release channels in heart failure and sudden cardiac death. J Mol Cell Cardiol 33: 615-624, 2001.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 615-624
    • Marks, A.R.1
  • 45
    • 0036274039 scopus 로고    scopus 로고
    • Regulation of ryanodine receptors via macromolecular complexes: A novel role for leucine/isoleucine zippers
    • Marks AR, Marx SO, Reiken S. Regulation of ryanodine receptors via macromolecular complexes: a novel role for leucine/isoleucine zippers. Trends Cardiovasc Med 12: 166-170, 2002.
    • (2002) Trends Cardiovasc Med , vol.12 , pp. 166-170
    • Marks, A.R.1    Marx, S.O.2    Reiken, S.3
  • 46
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): Defective regulation in failing hearts
    • Marx SO, Reiken S, Hisamatsu Y, Jayaraman T, Burkhoff D, Rosemblit N, Marks AR. PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell 101: 365-376, 2000.
    • (2000) Cell , vol.101 , pp. 365-376
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3    Jayaraman, T.4    Burkhoff, D.5    Rosemblit, N.6    Marks, A.R.7
  • 47
    • 0023644837 scopus 로고
    • Cardiac contractile protein phosphatases. Purification of two enzyme forms and their characterization with subunit-specific antibodies
    • Mumby M, Russell K, Garrard L, Green D. Cardiac contractile protein phosphatases. Purification of two enzyme forms and their characterization with subunit-specific antibodies. J Biol Chem 262: 6257-6265, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 6257-6265
    • Mumby, M.1    Russell, K.2    Garrard, L.3    Green, D.4
  • 50
    • 12644306887 scopus 로고    scopus 로고
    • Differential regulation of cardiac actomyosin S-1 MgATPase by protein kinase C isozyme-specific phosphorylation of specific sites in cardiac troponin I and its phosphorylation site mutants
    • Noland TA Jr, Raynor RL, Jideama NM, Guo X, Kazanietz MG, Blumberg PM, Solaro RJ, Kuo JF. Differential regulation of cardiac actomyosin S-1 MgATPase by protein kinase C isozyme-specific phosphorylation of specific sites in cardiac troponin I and its phosphorylation site mutants. Biochemistry 35: 14923-14931, 1996.
    • (1996) Biochemistry , vol.35 , pp. 14923-14931
    • Noland Jr, T.A.1    Raynor, R.L.2    Jideama, N.M.3    Guo, X.4    Kazanietz, M.G.5    Blumberg, P.M.6    Solaro, R.J.7    Kuo, J.F.8
  • 51
    • 0037023633 scopus 로고    scopus 로고
    • Phosphorylation of troponin I controls cardiac twitch dynamics: Evidence from phosphorylation site mutants expressed on a troponin I-null background in mice
    • Pi Y, Kemnitz KR, Zhang D, Kranias EG, Walker JW. Phosphorylation of troponin I controls cardiac twitch dynamics: evidence from phosphorylation site mutants expressed on a troponin I-null background in mice. Circ Res 90: 649-656, 2002.
    • (2002) Circ Res , vol.90 , pp. 649-656
    • Pi, Y.1    Kemnitz, K.R.2    Zhang, D.3    Kranias, E.G.4    Walker, J.W.5
  • 54
    • 0027478567 scopus 로고
    • Characterization of mutants within the gene for the adenovirus E3 14.7-kilodalton protein which prevents cytolysis by tumor necrosis factor
    • Ranheim TS, Shisler J, Horton TM, Wold LJ, Gooding LR, Wold WS. Characterization of mutants within the gene for the adenovirus E3 14.7-kilodalton protein which prevents cytolysis by tumor necrosis factor. J Virol 67: 2159-2167, 1993.
    • (1993) J Virol , vol.67 , pp. 2159-2167
    • Ranheim, T.S.1    Shisler, J.2    Horton, T.M.3    Wold, L.J.4    Gooding, L.R.5    Wold, W.S.6
  • 56
    • 33645064302 scopus 로고    scopus 로고
    • Partial replacement of cardiac troponin I with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCε phosphorylation
    • Scruggs SB, Walker LA, Lyu T, Geenen DL, Solaro RJ, Buttrick PM, Goldspink PH. Partial replacement of cardiac troponin I with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCε phosphorylation. J Mol Cell Cardiol 40: 446-450, 2006.
    • (2006) J Mol Cell Cardiol , vol.40 , pp. 446-450
    • Scruggs, S.B.1    Walker, L.A.2    Lyu, T.3    Geenen, D.L.4    Solaro, R.J.5    Buttrick, P.M.6    Goldspink, P.H.7
  • 57
    • 0034036663 scopus 로고    scopus 로고
    • Potentiation of fractional sarcoplasmic reticulum calcium release by total and free intra-sarcoplasmic reticulum calcium concentration
    • Shannon TR, Ginsburg KS, Bers DM. Potentiation of fractional sarcoplasmic reticulum calcium release by total and free intra-sarcoplasmic reticulum calcium concentration. Biophys J 78: 334-343, 2000.
    • (2000) Biophys J , vol.78 , pp. 334-343
    • Shannon, T.R.1    Ginsburg, K.S.2    Bers, D.M.3
  • 58
    • 0022921924 scopus 로고
    • Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains
    • Simmerman H, Collins J, Theibert J, Wegener A, Jones L. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J Biol Chem 261: 13333-13341, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 13333-13341
    • Simmerman, H.1    Collins, J.2    Theibert, J.3    Wegener, A.4    Jones, L.5
  • 62
    • 0024360671 scopus 로고
    • Phospholamban phosphorylation in intact ventricles. Phosphorylation of serine 16 and threonine 17 in response to β-adrenergic stimulation
    • Wegener AD, Simmerman HK, Lindemann JP, Jones LR. Phospholamban phosphorylation in intact ventricles. Phosphorylation of serine 16 and threonine 17 in response to β-adrenergic stimulation. J Biol Chem 264: 11468-11474, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 11468-11474
    • Wegener, A.D.1    Simmerman, H.K.2    Lindemann, J.P.3    Jones, L.R.4
  • 63
    • 0033534615 scopus 로고    scopus 로고
    • Identification of kinase-phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A
    • Westphal RS, Coffee RL Jr, Marotta A, Pelech SL, Wadzinski BE. Identification of kinase-phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A. J Biol Chem 274: 687-692, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 687-692
    • Westphal, R.S.1    Coffee Jr, R.L.2    Marotta, A.3    Pelech, S.L.4    Wadzinski, B.E.5
  • 64
    • 0025772161 scopus 로고
    • Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity
    • Witcher DR, Kovacs RJ, Schulman H, Cefali DC, Jones LR. Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity. J Biol Chem 266: 11144-11152, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 11144-11152
    • Witcher, D.R.1    Kovacs, R.J.2    Schulman, H.3    Cefali, D.C.4    Jones, L.R.5
  • 66
    • 33750692762 scopus 로고    scopus 로고
    • Method for isolation of adult mouse cardiomyocytes for studies of contraction and microfluorimetry
    • Wolska BM, Solaro RJ. Method for isolation of adult mouse cardiomyocytes for studies of contraction and microfluorimetry. Am J Physiol Heart Circ Physiol 271: H1250-H1255, 1996.
    • (1996) Am J Physiol Heart Circ Physiol , vol.271
    • Wolska, B.M.1    Solaro, R.J.2
  • 67
    • 35648947326 scopus 로고    scopus 로고
    • Protein kinase Cζ: A novel regulator of both phosphorylation and de-phosphorylation of cardiac sarcomeric proteins
    • Wu SC, Solaro RJ. Protein kinase Cζ: a novel regulator of both phosphorylation and de-phosphorylation of cardiac sarcomeric proteins. J Biol Chem 282: 30691-30698, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 30691-30698
    • Wu, S.C.1    Solaro, R.J.2


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