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Volumn 538, Issue , 2004, Pages 389-402

The special structure and function of troponin I in regulation of cardiac contraction and relaxation

Author keywords

[No Author keywords available]

Indexed keywords

TROPONIN I;

EID: 1842526994     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper
Times cited : (10)

References (73)
  • 1
    • 0028988060 scopus 로고
    • Diminished Ca sensitivity of skinned cardiac muscle contractility coincident with troponin T-band shifts in the diabetic rat
    • Akella, A.B., Ding, X.L., Chen, R., and Gulati, J., 1995, Diminished Ca sensitivity of skinned cardiac muscle contractility coincident with troponin T-band shifts in the diabetic rat. Circ. Res. 76:600-606.
    • (1995) Circ. Res. , vol.76 , pp. 600-606
    • Akella, A.B.1    Ding, X.L.2    Chen, R.3    Gulati, J.4
  • 2
    • 0022393490 scopus 로고
    • The cellular basis of the length-tension relation in cardiac muscle
    • Allen, D.G. and Kentish, J.C., 1985, The cellular basis of the length-tension relation in cardiac muscle. J. Mol. Cell Cardiol. 17:821-840.
    • (1985) J. Mol. Cell Cardiol. , vol.17 , pp. 821-840
    • Allen, D.G.1    Kentish, J.C.2
  • 3
    • 0033841530 scopus 로고    scopus 로고
    • Attenuation of length-dependent activation in myofilaments of transgenic mouse hearts expressing slow skeletal troponin I
    • London
    • Arteaga, G.M., Palmiter, K.A., Leiden, J.M., and Solaro, R.J., 2000, Attenuation of length-dependent activation in myofilaments of transgenic mouse hearts expressing slow skeletal troponin I. J. Physiol. (London) 526:541-549.
    • (2000) J. Physiol. , vol.526 , pp. 541-549
    • Arteaga, G.M.1    Palmiter, K.A.2    Leiden, J.M.3    Solaro, R.J.4
  • 5
    • 0034693150 scopus 로고    scopus 로고
    • The importance of the carboxyl-terminal domain of cardiac troponin C in Ca-sensitive muscle regulation
    • Calvert, M.J., Ward, D.G., Trayer, H.R., Trayer, I.P., 2000, The importance of the carboxyl-terminal domain of cardiac troponin C in Ca-sensitive muscle regulation. J. Biol. Chem., 275:32508-15.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32508-32515
    • Calvert, M.J.1    Ward, D.G.2    Trayer, H.R.3    Trayer, I.P.4
  • 6
    • 0033575919 scopus 로고    scopus 로고
    • An improved method for exchanging troponin subunits in detergent skinned rat cardiac fiber bundles
    • Chandra, M., Kim, J.J., Solaro, R.J., 1999, An improved method for exchanging troponin subunits in detergent skinned rat cardiac fiber bundles. Biochem. Biophys. Res. Commun. 263:219-23
    • (1999) Biochem. Biophys. Res. Commun. , vol.263 , pp. 219-223
    • Chandra, M.1    Kim, J.J.2    Solaro, R.J.3
  • 8
    • 0037144483 scopus 로고    scopus 로고
    • Single mutation (A162H) in human cardiac troponin I corrects acid pH sensitivity of Ca2+-regulated actomyosin S1 ATPase
    • Dargis, R., Pearlstone, J.R., Barrette-Ng, I., Edwards, H., Smillie, L.B., 2002, Single mutation (A162H) in human cardiac troponin I corrects acid pH sensitivity of Ca2+-regulated actomyosin S1 ATPase. J. Biol. Chem. 277:34662-5
    • (2002) J. Biol. Chem. , vol.277 , pp. 34662-34665
    • Dargis, R.1    Pearlstone, J.R.2    Barrette-Ng, I.3    Edwards, H.4    Smillie, L.B.5
  • 9
    • 0017814474 scopus 로고
    • Differential, direct effects of H+ on Ca2+ -activated force of skinned fibers from the soleus, cardiac and adductor magnus muscles of rabbits
    • Donaldson, S.K., Hermansen, L., and Bolles, L., 1978, Differential, direct effects of H+ on Ca2+ -activated force of skinned fibers from the soleus, cardiac and adductor magnus muscles of rabbits. Pflugers Arch. 376:55-65.
    • (1978) Pflugers Arch. , vol.376 , pp. 55-65
    • Donaldson, S.K.1    Hermansen, L.2    Bolles, L.3
  • 11
    • 0030941244 scopus 로고    scopus 로고
    • Conformation of the N-terminal segment of a monocysteine mutant of Troponin I from cardiac muscle
    • Dong, W-J., Chandra, M., Xing, J., Solaro, R.J. and Cheung, H.C., 1997, Conformation of the N-terminal segment of a monocysteine mutant of Troponin I from cardiac muscle. Biochemistry. 36:6745-6753.
    • (1997) Biochemistry , vol.36 , pp. 6745-6753
    • Dong, W.-J.1    Chandra, M.2    Xing, J.3    Solaro, R.J.4    Cheung, H.C.5
  • 12
    • 0030904641 scopus 로고    scopus 로고
    • Phosphorylation-induced distance change in a cardiac muscle Troponin I mutant
    • Dong, W-J., Chandra, M., Xing, J., She, M., Solaro, R.J. and Cheung, H.C., 1997a, Phosphorylation-induced distance change in a cardiac muscle Troponin I mutant. Biochemistry. 36:6754-6761.
    • (1997) Biochemistry , vol.36 , pp. 6754-6761
    • Dong, W.-J.1    Chandra, M.2    Xing, J.3    She, M.4    Solaro, R.J.5    Cheung, H.C.6
  • 13
    • 0034559235 scopus 로고    scopus 로고
    • Structural mapping of single cysteine mutants of cardiac troponin I
    • Dong, W.J., Xing, J., Chandra, M., Solaro, R.J., Cheung, H.C., 2000, Structural mapping of single cysteine mutants of cardiac troponin I. Proteins 41:438-447.
    • (2000) Proteins , vol.41 , pp. 438-447
    • Dong, W.J.1    Xing, J.2    Chandra, M.3    Solaro, R.J.4    Cheung, H.C.5
  • 14
    • 0023848317 scopus 로고
    • Troponin I enhances acidic pH induced depression of Ca-binding to the regulatory sites in skeletal troponin C
    • El-Saleh, S. and Solaro, R.J. (1988) Troponin I enhances acidic pH induced depression of Ca-binding to the regulatory sites in skeletal troponin C. J. Biol. Chem. 263:3274-3278.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3274-3278
    • El-Saleh, S.1    Solaro, R.J.2
  • 16
    • 0343526912 scopus 로고    scopus 로고
    • Systematic mapping of regions of human cardiac troponin I involved in binding to cardiac troponin C: N- and C-terminal low affinity contributing regions
    • Ferrieres, G., Pugniere, M., Mani, J.C., Villard, S., Laprade, M., Doutre, P., Pau, B., Granier, C., 2000, Systematic mapping of regions of human cardiac troponin I involved in binding to cardiac troponin C: N-and C-terminal low affinity contributing regions. FEBS Lett 479:99-105.
    • (2000) FEBS Lett , vol.479 , pp. 99-105
    • Ferrieres, G.1    Pugniere, M.2    Mani, J.C.3    Villard, S.4    Laprade, M.5    Doutre, P.6    Pau, B.7    Granier, C.8
  • 18
    • 0032555957 scopus 로고    scopus 로고
    • Strong binding of myosin modulates length-dependent Ca2+ activation of rat ventricular myocytes
    • Fitzsimons, D.P. and Moss, R.L. (1998) Strong binding of myosin modulates length-dependent Ca2+ activation of rat ventricular myocytes. Circ. Res. 83:602-607.
    • (1998) Circ. Res. , vol.83 , pp. 602-607
    • Fitzsimons, D.P.1    Moss, R.L.2
  • 21
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A.M., Homsher, E., and Regnier, M., 2000, Regulation of contraction in striated muscle. Physio. Rev. 80:853-924.
    • (2000) Physio. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 22
    • 0028271419 scopus 로고
    • Effect of phosphorylation of troponin I and C protein on isometric tension and velocity of unloaded shortening in skinned single cardiac myocytes from rats
    • Hoffman, P.A. and Lange, J.H., III., 1995, Effect of phosphorylation of troponin I and C protein on isometric tension and velocity of unloaded shortening in skinned single cardiac myocytes from rats. Circ. Res. 74:718-726.
    • (1995) Circ. Res. , vol.74 , pp. 718-726
    • Hoffman, P.A.1    Lange III, J.H.2
  • 24
    • 0030715344 scopus 로고    scopus 로고
    • Protein kinase A does not alter unloaded velocity of sarcomere shortening in skinned rat cardiac trabeculae
    • Janssen, P.M.L. and deTombe, P.P., 1997, Protein kinase A does not alter unloaded velocity of sarcomere shortening in skinned rat cardiac trabeculae. Am. J. Physiol. H2415-H2422.
    • (1997) Am. J. Physiol.
    • Janssen, P.M.L.1    DeTombe, P.P.2
  • 26
    • 0034720444 scopus 로고    scopus 로고
    • Effect of troponin I phosphorylation by protein kinase A on length-dependence of tension activation in skinned cardiac muscle fibers
    • Kajiwara, H., Morimoto, S., Fukuda, N., Ohtsuki, I., Kurihara, S., 2000, Effect of troponin I phosphorylation by protein kinase A on length-dependence of tension activation in skinned cardiac muscle fibers. Biochem. Biophys. Res. Commun. 272:104-10.
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 104-110
    • Kajiwara, H.1    Morimoto, S.2    Fukuda, N.3    Ohtsuki, I.4    Kurihara, S.5
  • 27
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin I by protein kinase A accelerates relaxation and cross-bridge cycle kinetics in mouse ventricular muscle
    • Kentish, J.C., McCloskey, D.T., Layland, J., Palmer, S., Leiden, J.M., Martin, A.F., and Solaro, R.J., 2001, Phosphorylation of troponin I by protein kinase A accelerates relaxation and cross-bridge cycle kinetics in mouse ventricular muscle. Circ. Res. 88:1059-1065.
    • (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
  • 28
    • 33751293387 scopus 로고    scopus 로고
    • Length dependence of Ca(2+)-tension relationship in aequorin-injected ferret papillary muscles
    • Komukai, K. and Kurihara, S., 1997, Length dependence of Ca(2+)-tension relationship in aequorin-injected ferret papillary muscles. Am. J. Physiol. 273:H1068-H1074.
    • (1997) Am. J. Physiol. , vol.273
    • Komukai, K.1    Kurihara, S.2
  • 29
    • 0036795565 scopus 로고    scopus 로고
    • Length-dependent activation in three striated muscle types of the rat
    • Konhilas, J.P., Irving, T.C., de Tombe, P.P., 2002, Length-dependent activation in three striated muscle types of the rat. J. Physiol. 544:225-36.
    • (2002) J. Physiol. , vol.544 , pp. 225-236
    • Konhilas, J.P.1    Irving, T.C.2    De Tombe, P.P.3
  • 31
    • 0028016156 scopus 로고
    • NMR studies delineating spatial relationships within the cardiac troponin I-troponin C complex
    • Krudy, G.A., Kleerekoper, Q., Guo, X., Howarth, J.W., Solaro, R.J., Rosevear, P.R., 1994, NMR studies delineating spatial relationships within the cardiac troponin I-troponin C complex. J. Biol. Chem. 269:23731-5.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23731-23735
    • Krudy, G.A.1    Kleerekoper, Q.2    Guo, X.3    Howarth, J.W.4    Solaro, R.J.5    Rosevear, P.R.6
  • 32
    • 0028342760 scopus 로고
    • The regulatory switch of the muscle thin filament: Ca2+ or myosin heads?
    • Lehrer, S.S., 1994, The regulatory switch of the muscle thin filament: Ca2+ or myosin heads? J. Muscle Res. Cell Motil. 15:232-6.
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 232-236
    • Lehrer, S.S.1
  • 34
    • 0034964228 scopus 로고    scopus 로고
    • Localization of regions of troponin I important in deactivation of cardiac myofilaments by acidic pH
    • Li, G., Martin, A.F., and Solaro, R.J., 2001, Localization of regions of troponin I important in deactivation of cardiac myofilaments by acidic pH. J. Mol. Cell Cardiol. 33:1309-1320.
    • (2001) J. Mol. Cell Cardiol. , vol.33 , pp. 1309-1320
    • Li, G.1    Martin, A.F.2    Solaro, R.J.3
  • 35
    • 0033614841 scopus 로고    scopus 로고
    • Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C
    • Li, M.X., Spyracopoulos, L., and Sykes, B.D., 1999, Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C. Biochemistry 38:8289-98.
    • (1999) Biochemistry , vol.38 , pp. 8289-8298
    • Li, M.X.1    Spyracopoulos, L.2    Sykes, B.D.3
  • 36
    • 0024396685 scopus 로고
    • Subcellular distribution and immuno-cytochemical localization of protein kinase C in myocardium, and phosphorylation of troponin in isolated myocytes stimulated by isoproterenol or phorbol ester
    • Liu, J.D., Wood, J.G., Raynor, R.L., Wang, Y.C., Noland, T.A. Jr., Ansari, A.A. Kuo, J.F., 1989, Subcellular distribution and immuno-cytochemical localization of protein kinase C in myocardium, and phosphorylation of troponin in isolated myocytes stimulated by isoproterenol or phorbol ester. Biochem. Biophys. Res. Commun. 162:1105-10.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 1105-1110
    • Liu, J.D.1    Wood, J.G.2    Raynor, R.L.3    Wang, Y.C.4    Noland Jr., T.A.5    Ansari, A.A.6    Kuo, J.F.7
  • 38
    • 0025933590 scopus 로고
    • Identification and functional significance of troponin I isoforms in neonatal rat heart myofibrils
    • Martin, A.M., Ball, K., Gao, L., Kumar, P.K., and Solaro, R.J., 1991, Identification and functional significance of troponin I isoforms in neonatal rat heart myofibrils. Circ. Res. 69:1244-1252.
    • (1991) Circ. Res. , vol.69 , pp. 1244-1252
    • Martin, A.M.1    Ball, K.2    Gao, L.3    Kumar, P.K.4    Solaro, R.J.5
  • 39
    • 0035006418 scopus 로고    scopus 로고
    • Influence of length on force and activation-dependent changes in troponin c structure in skinned cardiac and fast skeletal muscle
    • Martyn, D.A. and Gordon, A.M., 2001, Influence of length on force and activation-dependent changes in troponin c structure in skinned cardiac and fast skeletal muscle. Biophys. J. 80:2798-808.
    • (2001) Biophys. J. , vol.80 , pp. 2798-2808
    • Martyn, D.A.1    Gordon, A.M.2
  • 40
    • 0028986544 scopus 로고
    • Length dependence of Ca2+ sensitivity of tension in mouse cardiac myocytes expressing skeletal troponin C
    • Mcdonald, K.S., Field, L.J., Parmacek, M.S., Soonpaa, M., Leiden, J.M., and Moss, R.L., 1995, Length dependence of Ca2+ sensitivity of tension in mouse cardiac myocytes expressing skeletal troponin C. J. Physiol. 483:131-139.
    • (1995) J. Physiol. , vol.483 , pp. 131-139
    • Mcdonald, K.S.1    Field, L.J.2    Parmacek, M.S.3    Soonpaa, M.4    Leiden, J.M.5    Moss, R.L.6
  • 41
    • 0034967037 scopus 로고    scopus 로고
    • Transgenic incorporation of fast skeletal troponin T into cardiac myofilaments blunts PKC-mediated depression of force
    • Montgomery, D.E., Chandra, M., Huang, Q-Q., Jin, J.-P., and Solaro, R.J., 2001, Transgenic incorporation of fast skeletal troponin T into cardiac myofilaments blunts PKC-mediated depression of force. Am. J. Physiol. (Heart) 280:H1011-H1018.
    • (2001) Am. J. Physiol. (Heart) , vol.280
    • Montgomery, D.E.1    Chandra, M.2    Huang, Q.-Q.3    Jin, J.-P.4    Solaro, R.J.5
  • 42
    • 0032820357 scopus 로고    scopus 로고
    • Roles of troponin isoforms in pH dependence of contraction in rabbit fast and slow skeletal and cardiac muscles
    • Morimoto, S., Harada, K., and Ohtsuki, I., 1999, Roles of troponin isoforms in pH dependence of contraction in rabbit fast and slow skeletal and cardiac muscles. J. Biochem. (Tokyo) 126:121-9.
    • (1999) J. Biochem. (Tokyo) , vol.126 , pp. 121-129
    • Morimoto, S.1    Harada, K.2    Ohtsuki, I.3
  • 43
    • 0034816767 scopus 로고    scopus 로고
    • A pH-sensitive interaction of troponin I with troponin C coupled with strongly binding cross-bridges in cardiac myofilament activation
    • Morimoto, S., Ohta, M., Goto, T., and Ohtsuki, I., 2001, A pH-sensitive interaction of troponin I with troponin C coupled with strongly binding cross-bridges in cardiac myofilament activation. Biochem. Biophys. Res. Commun. 282:811-5.
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 811-815
    • Morimoto, S.1    Ohta, M.2    Goto, T.3    Ohtsuki, I.4
  • 44
    • 0011277233 scopus 로고    scopus 로고
    • Regulation of Cardiac Contraction by Calcium
    • E. Page, H. Fozzard, R. J. Solaro, eds. Oxford University Press, New York
    • Moss, R.L. and Buck, S.H., 2001, Regulation of Cardiac Contraction by Calcium, in: Handbook of Physiology: Section 2. The Cardiovascular System. Vol I. The Heart, E. Page, H. Fozzard, R. J. Solaro, eds.) Oxford University Press, New York, pp. 420-454.
    • (2001) Handbook of Physiology: Section 2. The Cardiovascular System. Vol I. The Heart , vol.1 , pp. 420-454
    • Moss, R.L.1    Buck, S.H.2
  • 45
    • 0024399052 scopus 로고
    • Identification of sites phosphorylated in bovine cardiac troponin I and troponin T by protein kinase C and comparative substrate activity of synthetic peptides containing the phosphorylation sites
    • Noland, T.A., Jr., Raynor, R.L., and Kuo, J.F., 1989, Identification of sites phosphorylated in bovine cardiac troponin I and troponin T by protein kinase C and comparative substrate activity of synthetic peptides containing the phosphorylation sites. J. Biol. Chem. 264:20778-20785.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20778-20785
    • Noland Jr., T.A.1    Raynor, R.L.2    Kuo, J.F.3
  • 46
    • 0027508915 scopus 로고
    • 2+-stimulated MgATPase activity in reconstituted actomyosin and isolated myofibrils, and decreases actin-myosin interactions
    • 2+-stimulated MgATPase activity in reconstituted actomyosin and isolated myofibrils, and decreases actin-myosin interactions. J. Mol. Cell. Cardiol. 25:53-65.
    • (1993) J. Mol. Cell. Cardiol. , vol.25 , pp. 53-65
    • Noland Jr., T.A.1    Kuo, J.F.2
  • 47
    • 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, T.A. Jr., Raynor, R.L., Jideama, N.M., Quo, X., Kazanietz, M.G., Blumberg, P.M., Solaro, R.J., and Kuo, J.F., 1996, 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) Biochemistry , vol.35 , pp. 14923-14931
    • Noland Jr., T.A.1    Raynor, R.L.2    Jideama, N.M.3    Quo, X.4    Kazanietz, M.G.5    Blumberg, P.M.6    Solaro, R.J.7    Kuo, J.F.8
  • 49
    • 0023644924 scopus 로고
    • Calcium binding properties of troponin C in detergent skinned heart muscle fibers
    • Pan B-S. and Solaro, R.J., 1987, Calcium binding properties of troponin C in detergent skinned heart muscle fibers. J. Biol. Chem. 262:7339-7349.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7339-7349
    • Pan, B.-S.1    Solaro, R.J.2
  • 50
    • 0028858949 scopus 로고
    • A direct regulatory role for troponin T and a dual role for troponin C in the Ca2+ regulation of muscle contraction
    • Potter, J.D., Sheng, Z., Pan, B.S., Zhao, J.A., 1995, A direct regulatory role for troponin T and a dual role for troponin C in the Ca2+ regulation of muscle contraction. J. Biol. Chem. 270:2557-62.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2557-2562
    • Potter, J.D.1    Sheng, Z.2    Pan, B.S.3    Zhao, J.A.4
  • 54
    • 0025348807 scopus 로고
    • Adrenaline increases the rate of cross-bridge cycling in rat cardiac muscle
    • Saeki, Y., Shiozawa, K., Yanagisawa, K., and Shibata, T., 1990, Adrenaline increases the rate of cross-bridge cycling in rat cardiac muscle. J. Mol. Cell Cardiol. 22:453-460.
    • (1990) J. Mol. Cell Cardiol. , vol.22 , pp. 453-460
    • Saeki, Y.1    Shiozawa, K.2    Yanagisawa, K.3    Shibata, T.4
  • 55
    • 0024459179 scopus 로고
    • Troponin I switching in the developing heart
    • Saggin, L., Gorza, L., Ausoni, S., and Schiaffino, S., 1989, Troponin I switching in the developing heart. J. Biol. Chem. 264:16299-302.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16299-16302
    • Saggin, L.1    Gorza, L.2    Ausoni, S.3    Schiaffino, S.4
  • 57
    • 0012681744 scopus 로고    scopus 로고
    • Role of Troponin I in the Sarcomere Length Dependence of Calcium Sensitivity in Skinned Rat Trabeculae
    • Smith, S.H., Versluis, J.P., Martin, A.F., Solaro, R.J., de Tombe, P.P., 2002, Role of Troponin I in the Sarcomere Length Dependence of Calcium Sensitivity in Skinned Rat Trabeculae Circulation 106(11):101.
    • (2002) Circulation , vol.106 , Issue.11 , pp. 101
    • Smith, S.H.1    Versluis, J.P.2    Martin, A.F.3    Solaro, R.J.4    De Tombe, P.P.5
  • 58
    • 0023705863 scopus 로고
    • Differences in the response of adult and neonatal heart muscle to acidosis
    • Solaro, R.J., Lee, J., Kentish, J., and Allen, D.A., 1988, Differences in the response of adult and neonatal heart muscle to acidosis. Circ. Res. 63:779-787.
    • (1988) Circ. Res. , vol.63 , pp. 779-787
    • Solaro, R.J.1    Lee, J.2    Kentish, J.3    Allen, D.A.4
  • 59
    • 0001259213 scopus 로고    scopus 로고
    • Modulation of cardiac myofilament activity by protein phosphorylation
    • (E. Page, H. Fozzard, R. J. Solaro, Eds.) Oxford University Press, New York
    • Solaro, R.J., 2001, Modulation of cardiac myofilament activity by protein phosphorylation. Handbook of Physiology: Section 2. The Cardiovascular System. Vol I. The Heart (E. Page, H. Fozzard, R. J. Solaro, Eds.) Oxford University Press, New York, pp 264-300.
    • (2001) Handbook of Physiology: Section 2. The Cardiovascular System. Vol I. The Heart , vol.1 , pp. 264-300
    • Solaro, R.J.1
  • 60
    • 0032494188 scopus 로고    scopus 로고
    • Troponin and tropomyosin: Proteins that switch on and tune in the activity of cardiac myofilaments
    • Solaro, R.J. and Rarick, H.M., 1998, Troponin and tropomyosin: proteins that switch on and tune in the activity of cardiac myofilaments. Circ. Res. 83:471-480.
    • (1998) Circ. Res. , vol.83 , pp. 471-480
    • Solaro, R.J.1    Rarick, H.M.2
  • 61
    • 0022546253 scopus 로고
    • 2+ activation of myofilaments of adult and perinatal dog hearts: Evidence for developmental differences in thin filament regulation
    • 2+ activation of myofilaments of adult and perinatal dog hearts: Evidence for developmental differences in thin filament regulation. Circ. Res. 58:721-729.
    • (1986) Circ. Res. , vol.58 , pp. 721-729
    • Solaro, R.J.1    Kumar, P.2    Blanchard, E.M.3    Martin, A.M.4
  • 62
    • 0141781208 scopus 로고    scopus 로고
    • Modulation of Thin Filament Activity in Long and Short Term Regulation of Cardiac Function
    • R.J. Solaro and R.L. Moss, eds., Kluwer Academic Publishers, Dordrecht, Netherlands
    • Solaro R.J., Wolska, B.M., Arteaga G., Martin A.F., Buttrick P., deTombe, P., 2002, Modulation of Thin Filament Activity in Long and Short Term Regulation of Cardiac Function, in: Molecular Control Mechanisms in Striated Muscle Contraction, R.J. Solaro and R.L. Moss, eds., Kluwer Academic Publishers, Dordrecht, Netherlands pp. 291-327.
    • (2002) Molecular Control Mechanisms in Striated Muscle Contraction , pp. 291-327
    • Solaro, R.J.1    Wolska, B.M.2    Arteaga, G.3    Martin, A.F.4    Buttrick, P.5    DeTombe, P.6
  • 63
  • 64
    • 0031777885 scopus 로고    scopus 로고
    • A new look at thin filament regulation in vertebrate skeletal muscle
    • Squire, J.M. and Morris, E.P., 1998, A new look at thin filament regulation in vertebrate skeletal muscle. FASEB J. 12:761-771.
    • (1998) FASEB J. , vol.12 , pp. 761-771
    • Squire, J.M.1    Morris, E.P.2
  • 65
    • 0028174245 scopus 로고
    • Beta-adrenergic receptor stimulation increases unloaded shortening velocity of skinned single ventricular myocytes from rats
    • Strang, K.T., Sweitzer, N.K., Greaser, M.L., and Moss, R.L., 1994, Beta-adrenergic receptor stimulation increases unloaded shortening velocity of skinned single ventricular myocytes from rats. Circ. Res. 74:542-549.
    • (1994) Circ. Res. , vol.74 , pp. 542-549
    • Strang, K.T.1    Sweitzer, N.K.2    Greaser, M.L.3    Moss, R.L.4
  • 66
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman, L.S., 1996, Thin filament-mediated regulation of cardiac contraction. Ann. Rev. Physiol. 58:447-481.
    • (1996) Ann. Rev. Physiol. , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 68
    • 0027974349 scopus 로고
    • Length, force, and Ca(2+)-troponin C affinity in cardiac and slow skeletal muscle
    • Wang, Y.P., and Fuchs, F. (1994) Length, force, and Ca(2+)-troponin C affinity in cardiac and slow skeletal muscle. Am. J. Physiol. 266:C1077-C1082.
    • (1994) Am. J. Physiol. , vol.266
    • Wang, Y.P.1    Fuchs, F.2
  • 69
    • 0036830352 scopus 로고    scopus 로고
    • Structural consequences of cardiac troponin I phosphorylation
    • Ward, D.G., Cornes, M.P., Trayer, I.P., 2002, Structural consequences of cardiac troponin I phosphorylation. J. Biol. Chem. 277:41795-41801.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41795-41801
    • Ward, D.G.1    Cornes, M.P.2    Trayer, I.P.3
  • 70
    • 0029146873 scopus 로고
    • The unique amino-terminal peptide of cardiac troponin I regulates myofibrillar ATPase activity only when it is phosphorylated
    • Wattanapermpool, J., Guo, X. and Solaro, R.J., 1995, The unique amino-terminal peptide of cardiac troponin I regulates myofibrillar ATPase activity only when it is phosphorylated. J. Mol. Cell. Cardiol. 27:1383-1391.
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 1383-1391
    • Wattanapermpool, J.1    Guo, X.2    Solaro, R.J.3
  • 71
    • 0035653571 scopus 로고    scopus 로고
    • Troponin I isoforms and chimeras: Tuning the molecular switch of cardiac contraction
    • Westfall, M.V. and Metzger, J.M., 2001. Troponin I isoforms and chimeras: tuning the molecular switch of cardiac contraction. News Physiol. Sci. 16:278-81.
    • (2001) News Physiol. Sci. , vol.16 , pp. 278-281
    • Westfall, M.V.1    Metzger, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.