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Volumn , Issue , 2010, Pages 57-72

Myocardium and development

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EID: 84882837989     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-7020-3064-2.00004-7     Document Type: Chapter
Times cited : (4)

References (122)
  • 1
    • 0015369714 scopus 로고
    • The intrinsic physiologic properties of the developing heart
    • Friedman W.F. The intrinsic physiologic properties of the developing heart. Prog Cardiovasc Dis 1972, 15:87-111.
    • (1972) Prog Cardiovasc Dis , vol.15 , pp. 87-111
    • Friedman, W.F.1
  • 2
    • 0023200290 scopus 로고
    • Developmental changes in the ultrastructure and sarcomere shortening of the isolated rabbit ventricular myocyte
    • Nassar R., Reedy M.C., Anderson P.A. Developmental changes in the ultrastructure and sarcomere shortening of the isolated rabbit ventricular myocyte. Circ Res 1987, 61:465-483.
    • (1987) Circ Res , vol.61 , pp. 465-483
    • Nassar, R.1    Reedy, M.C.2    Anderson, P.A.3
  • 3
    • 0018220385 scopus 로고
    • Normal and hypertrophic growth of the rat heart: Changes in cell dimensions and number
    • Korecky B., Rakusan K. Normal and hypertrophic growth of the rat heart: Changes in cell dimensions and number. Am J Physiol 1978, 234:H123-H128.
    • (1978) Am J Physiol , vol.234
    • Korecky, B.1    Rakusan, K.2
  • 4
    • 0018848130 scopus 로고
    • Morphometric study of early postnatal development in the left and right ventricular myocardium of the rat: I. Hypertrophy, hyperplasia, and binucleation of myocytes
    • Anversa P., Olivetti G., Loud A.V. Morphometric study of early postnatal development in the left and right ventricular myocardium of the rat: I. Hypertrophy, hyperplasia, and binucleation of myocytes. Circ Res 1980, 46:495-502.
    • (1980) Circ Res , vol.46 , pp. 495-502
    • Anversa, P.1    Olivetti, G.2    Loud, A.V.3
  • 5
    • 0030219688 scopus 로고    scopus 로고
    • Rapid transition of cardiac myocytes from hyperplasia to hypertrophy during postnatal development
    • Li F., Wang X., Capasso J.M., Gerdes A.M. Rapid transition of cardiac myocytes from hyperplasia to hypertrophy during postnatal development. J Mol Cell Cardiol 1996, 28:1737-1746.
    • (1996) J Mol Cell Cardiol , vol.28 , pp. 1737-1746
    • Li, F.1    Wang, X.2    Capasso, J.M.3    Gerdes, A.M.4
  • 6
    • 0037348215 scopus 로고    scopus 로고
    • Effect of increased pressure loading on heart growth in neonatal rats
    • Sedmera D., Thompson R.P., Kolar F. Effect of increased pressure loading on heart growth in neonatal rats. J Mol Cell Cardiol 2003, 35:301-309.
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 301-309
    • Sedmera, D.1    Thompson, R.P.2    Kolar, F.3
  • 7
    • 33847609314 scopus 로고    scopus 로고
    • Concise review: Stem cells, myocardial regeneration, and methodological artifacts
    • Anversa P., Leri A., Rota M., et al. Concise review: Stem cells, myocardial regeneration, and methodological artifacts. Stem Cells 2007, 25:589-601.
    • (2007) Stem Cells , vol.25 , pp. 589-601
    • Anversa, P.1    Leri, A.2    Rota, M.3
  • 8
    • 30944432553 scopus 로고    scopus 로고
    • Cell-based cardiac repair: Reflections at the 10-year point
    • Murry C.E., Field L.J., Menasche P. Cell-based cardiac repair: Reflections at the 10-year point. Circulation 2005, 112:3174-3183.
    • (2005) Circulation , vol.112 , pp. 3174-3183
    • Murry, C.E.1    Field, L.J.2    Menasche, P.3
  • 9
    • 20844447692 scopus 로고    scopus 로고
    • Myocardial regeneration by activation of multipotent cardiac stem cells in ischemic heart failure
    • Urbanek K., Torella D., Sheikh F., et al. Myocardial regeneration by activation of multipotent cardiac stem cells in ischemic heart failure. Proc Natl Acad Sci U S A 2005, 102:8692-8697.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 8692-8697
    • Urbanek, K.1    Torella, D.2    Sheikh, F.3
  • 10
    • 0034976441 scopus 로고    scopus 로고
    • Adult-derived stem cells from the liver become myocytes in the heart in vivo
    • Malouf N.N., Coleman W.B., Grisham J.W., et al. Adult-derived stem cells from the liver become myocytes in the heart in vivo. Am J Pathol 2001, 158:1929-1935.
    • (2001) Am J Pathol , vol.158 , pp. 1929-1935
    • Malouf, N.N.1    Coleman, W.B.2    Grisham, J.W.3
  • 11
    • 34247211563 scopus 로고    scopus 로고
    • Mechanisms controlling the acquisition of a cardiac phenotype by liver stem cells
    • Muller-Borer B.J., Cascio W.E., Esch G.L., et al. Mechanisms controlling the acquisition of a cardiac phenotype by liver stem cells. Proc Natl Acad U S A Sci 2007, 104:3877-3882.
    • (2007) Proc Natl Acad U S A Sci , vol.104 , pp. 3877-3882
    • Muller-Borer, B.J.1    Cascio, W.E.2    Esch, G.L.3
  • 12
    • 0023713203 scopus 로고
    • Protooncogene induction and reprogramming of cardiac gene expression produced by pressure overload
    • Izumo S., Nadal-Ginard B., Mahdavi V. Protooncogene induction and reprogramming of cardiac gene expression produced by pressure overload. Proc Natl Acad Sci U S A 1988, 85:339-343.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 339-343
    • Izumo, S.1    Nadal-Ginard, B.2    Mahdavi, V.3
  • 13
    • 0023923723 scopus 로고
    • Expression of cellular oncogenes in the myocardium during the developmental stage and pressure-overloaded hypertrophy of the rat heart
    • Komuro I., Kurabayashi M., Takaku F., Yazaki Y. Expression of cellular oncogenes in the myocardium during the developmental stage and pressure-overloaded hypertrophy of the rat heart. Circ Res 1988, 62:1075-1079.
    • (1988) Circ Res , vol.62 , pp. 1075-1079
    • Komuro, I.1    Kurabayashi, M.2    Takaku, F.3    Yazaki, Y.4
  • 14
    • 0012627221 scopus 로고    scopus 로고
    • Effect of intrauterine creation of pulmonary stenosis and atresia on ventricular hypertrophy in the foetal lamb, haemodynamic, morphometric and ultrastructural study
    • Toussaint M., Bical O., Balliz P., Neveux J.Y. Effect of intrauterine creation of pulmonary stenosis and atresia on ventricular hypertrophy in the foetal lamb, haemodynamic, morphometric and ultrastructural study. Eur Heart J 1998, 19:654.
    • (1998) Eur Heart J , vol.19 , pp. 654
    • Toussaint, M.1    Bical, O.2    Balliz, P.3    Neveux, J.Y.4
  • 15
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • Bers D.M. Cardiac excitation-contraction coupling. Nature 2002, 415:198-205.
    • (2002) Nature , vol.415 , pp. 198-205
    • Bers, D.M.1
  • 16
    • 3242692393 scopus 로고    scopus 로고
    • Macromolecular complexes regulating cardiac ryanodine receptor function
    • Bers D.M. Macromolecular complexes regulating cardiac ryanodine receptor function. J Mol Cell Cardiol 2004, 37:417-429.
    • (2004) J Mol Cell Cardiol , vol.37 , pp. 417-429
    • Bers, D.M.1
  • 17
    • 31044434071 scopus 로고    scopus 로고
    • The L-type calcium channel in the heart: The beat goes on
    • Bodi I., Mikala G., Koch S.E., et al. The L-type calcium channel in the heart: The beat goes on. J Clin Invest 2005, 115:3306-3317.
    • (2005) J Clin Invest , vol.115 , pp. 3306-3317
    • Bodi, I.1    Mikala, G.2    Koch, S.E.3
  • 18
    • 0035793925 scopus 로고    scopus 로고
    • Identification of the t-type calcium channel (Ca(v)3.1d) in developing mouse heart
    • Cribbs L.L., Martin B.L., Schroder E.A., et al. Identification of the t-type calcium channel (Ca(v)3.1d) in developing mouse heart. Circ Res 2001, 88:403-407.
    • (2001) Circ Res , vol.88 , pp. 403-407
    • Cribbs, L.L.1    Martin, B.L.2    Schroder, E.A.3
  • 19
    • 0025740968 scopus 로고
    • L- and T-type calcium channels in acutely isolated neonatal and adult cardiac myocytes
    • Wetzel G.T., Chen F., Klitzner T.S. L- and T-type calcium channels in acutely isolated neonatal and adult cardiac myocytes. Pediatr Res 1991, 30:89-94.
    • (1991) Pediatr Res , vol.30 , pp. 89-94
    • Wetzel, G.T.1    Chen, F.2    Klitzner, T.S.3
  • 20
    • 0023583248 scopus 로고
    • Sodium-calcium exchange in heart: Membrane currents and changes in [Ca2+]i
    • Barcenas-Ruiz L., Beuckelmann D.J., Wier W.G. Sodium-calcium exchange in heart: Membrane currents and changes in [Ca2+]i. Science 1987, 238:1720-1722.
    • (1987) Science , vol.238 , pp. 1720-1722
    • Barcenas-Ruiz, L.1    Beuckelmann, D.J.2    Wier, W.G.3
  • 21
    • 0029842873 scopus 로고    scopus 로고
    • Formation of junctions involved in excitation-contraction coupling in skeletal and cardiac muscle
    • Flucher B.E., Franzini-Armstrong C. Formation of junctions involved in excitation-contraction coupling in skeletal and cardiac muscle. Proc Natl Acad Sci U S A 1996, 93:8101-8106.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8101-8106
    • Flucher, B.E.1    Franzini-Armstrong, C.2
  • 23
    • 33845324519 scopus 로고    scopus 로고
    • Junctin is a prominent regulator of contractility in cardiomyocytes
    • Fan G.C., Yuan Q., Zhao W., et al. Junctin is a prominent regulator of contractility in cardiomyocytes. Biochem Biophys Res Commun 2007, 352:617-622.
    • (2007) Biochem Biophys Res Commun , vol.352 , pp. 617-622
    • Fan, G.C.1    Yuan, Q.2    Zhao, W.3
  • 24
    • 0036788917 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels
    • Fill M., Copello J.A. Ryanodine receptor calcium release channels. Physiol Rev 2002, 82:893-922.
    • (2002) Physiol Rev , vol.82 , pp. 893-922
    • Fill, M.1    Copello, J.A.2
  • 25
    • 0029029280 scopus 로고
    • Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes
    • Bassani J.W., Yuan W., Bers D.M., Fractional S.R. Ca release is regulated by trigger Ca and SR Ca content in cardiac myocytes. Am J Physiol 1995, 268:C1313-C1319.
    • (1995) Am J Physiol , vol.268
    • Bassani, J.W.1    Yuan, W.2    Bers, D.M.3    Fractional, S.R.4
  • 26
    • 0035827585 scopus 로고    scopus 로고
    • Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor)
    • Balshaw D.M., Xu L., Yamaguchi N., et al. Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor). J Biol Chem 2001, 276:20144-20153.
    • (2001) J Biol Chem , vol.276 , pp. 20144-20153
    • Balshaw, D.M.1    Xu, L.2    Yamaguchi, N.3
  • 27
    • 1942423621 scopus 로고    scopus 로고
    • The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium
    • Gyorke I., Hester N., Jones L.R., Gyorke S. The role of calsequestrin, triadin, and junctin in conferring cardiac ryanodine receptor responsiveness to luminal calcium. Biophys J 2004, 86:2121-2128.
    • (2004) Biophys J , vol.86 , pp. 2121-2128
    • Gyorke, I.1    Hester, N.2    Jones, L.R.3    Gyorke, S.4
  • 28
    • 0034306015 scopus 로고    scopus 로고
    • Exogenous Ca2+-ATPase isoform effects on Ca2+ transients of embryonic chicken and neonatal rat cardiac myocytes
    • Cavagna M., O'Donnell J.M., Sumbilla C., et al. Exogenous Ca2+-ATPase isoform effects on Ca2+ transients of embryonic chicken and neonatal rat cardiac myocytes. J Physiol 2000, 528(pt 1):53-63.
    • (2000) J Physiol , vol.528 , Issue.PART 1 , pp. 53-63
    • Cavagna, M.1    O'Donnell, J.M.2    Sumbilla, C.3
  • 29
    • 0026567125 scopus 로고
    • Molecular mechanism of regulation of Ca2+ pump ATPase by phospholamban in cardiac sarcoplasmic reticulum: Effects of synthetic phospholamban peptides on Ca2+ pump ATPase
    • Sasaki T., Inui M., Kimura Y., et al. Molecular mechanism of regulation of Ca2+ pump ATPase by phospholamban in cardiac sarcoplasmic reticulum: Effects of synthetic phospholamban peptides on Ca2+ pump ATPase. J Biol Chem 1992, 267:1674-1679.
    • (1992) J Biol Chem , vol.267 , pp. 1674-1679
    • Sasaki, T.1    Inui, M.2    Kimura, Y.3
  • 30
    • 33747587851 scopus 로고    scopus 로고
    • Development and cardiac contractility: Cardiac troponin T isoforms and cytosolic calcium in rabbit
    • McCall S.J., Nassar R., Malouf N.N., et al. Development and cardiac contractility: Cardiac troponin T isoforms and cytosolic calcium in rabbit. Pediatr Res 2006, 60:276-281.
    • (2006) Pediatr Res , vol.60 , pp. 276-281
    • McCall, S.J.1    Nassar, R.2    Malouf, N.N.3
  • 31
    • 0033520122 scopus 로고    scopus 로고
    • Subcellular [Ca2+]i gradients during excitation-contraction coupling in newborn rabbit ventricular myocytes
    • Haddock P.S., Coetzee W.A., Cho E., et al. Subcellular [Ca2+]i gradients during excitation-contraction coupling in newborn rabbit ventricular myocytes. Circ Res 1999, 85:415-427.
    • (1999) Circ Res , vol.85 , pp. 415-427
    • Haddock, P.S.1    Coetzee, W.A.2    Cho, E.3
  • 32
    • 0026453799 scopus 로고
    • Sarcolemmal Na(+)-Ca2+ exchange activity and exchanger immunoreactivity in developing rabbit hearts
    • Artman M. Sarcolemmal Na(+)-Ca2+ exchange activity and exchanger immunoreactivity in developing rabbit hearts. Am J Physiol 1992, 263:H1506-H1513.
    • (1992) Am J Physiol , vol.263
    • Artman, M.1
  • 33
    • 0028898260 scopus 로고
    • Na+/Ca2+ exchange current density in cardiac myocytes from rabbits and guinea pigs during postnatal development
    • Artman M., Ichikawa H., Avkiran M., Coetzee W.A. Na+/Ca2+ exchange current density in cardiac myocytes from rabbits and guinea pigs during postnatal development. Am J Physiol 1995, 268:H1714-1722.
    • (1995) Am J Physiol , vol.268
    • Artman, M.1    Ichikawa, H.2    Avkiran, M.3    Coetzee, W.A.4
  • 34
    • 0019452135 scopus 로고
    • Perinatal growth of the rabbit cardiac cell: Possible implications for the mechanism of relaxation
    • Hoerter J., Mazet F., Vassort G. Perinatal growth of the rabbit cardiac cell: Possible implications for the mechanism of relaxation. J Mol Cell Cardiol 1981, 13:725-740.
    • (1981) J Mol Cell Cardiol , vol.13 , pp. 725-740
    • Hoerter, J.1    Mazet, F.2    Vassort, G.3
  • 35
    • 0034097194 scopus 로고    scopus 로고
    • Molecular cloning of junctin from human and developing rabbit heart
    • Wetzel G.T., Ding S., Chen F. Molecular cloning of junctin from human and developing rabbit heart. Mol Genet Metab 2000, 69:252-258.
    • (2000) Mol Genet Metab , vol.69 , pp. 252-258
    • Wetzel, G.T.1    Ding, S.2    Chen, F.3
  • 36
    • 0015980796 scopus 로고
    • Studies on mechanism of inhibition of cardiac muscle contractile tension by ryanodine: Mechanical response
    • Penefsky Z.J. Studies on mechanism of inhibition of cardiac muscle contractile tension by ryanodine: Mechanical response. Pflugers Arch 1974, 347:173-184.
    • (1974) Pflugers Arch , vol.347 , pp. 173-184
    • Penefsky, Z.J.1
  • 37
    • 0023627173 scopus 로고
    • Development of myocardial contractile system in the fetal rabbit
    • Nakanishi T., Okuda H., Kamata K., et al. Development of myocardial contractile system in the fetal rabbit. Pediatr Res 1987, 22:201-207.
    • (1987) Pediatr Res , vol.22 , pp. 201-207
    • Nakanishi, T.1    Okuda, H.2    Kamata, K.3
  • 38
    • 0021488448 scopus 로고
    • Developmental changes in cardiac contractility in fetal and postnatal sheep: in vitro and in vivo
    • Anderson P.A., Glick K.L., Manring A., Crenshaw C. Developmental changes in cardiac contractility in fetal and postnatal sheep: in vitro and in vivo. Am J Physiol 1984, 247:H371-H379.
    • (1984) Am J Physiol , vol.247
    • Anderson, P.A.1    Glick, K.L.2    Manring, A.3    Crenshaw, C.4
  • 39
    • 0030934046 scopus 로고    scopus 로고
    • Contribution of the sodium-calcium exchanger to contractions in immature rabbit ventricular myocytes
    • Chin T.K., Christiansen G.A., Caldwell J.G., Thorburn J. Contribution of the sodium-calcium exchanger to contractions in immature rabbit ventricular myocytes. Pediatr Res 1997, 41:480-485.
    • (1997) Pediatr Res , vol.41 , pp. 480-485
    • Chin, T.K.1    Christiansen, G.A.2    Caldwell, J.G.3    Thorburn, J.4
  • 40
    • 0034724436 scopus 로고    scopus 로고
    • KB-R7943 block of Ca(2+) influx via Na(+)/Ca(2+) exchange does not alter twitches or glycoside inotropy but prevents Ca(2+) overload in rat ventricular myocytes
    • Satoh H., Ginsburg K.S., Qing K., et al. KB-R7943 block of Ca(2+) influx via Na(+)/Ca(2+) exchange does not alter twitches or glycoside inotropy but prevents Ca(2+) overload in rat ventricular myocytes. Circulation 2000, 101:1441-1446.
    • (2000) Circulation , vol.101 , pp. 1441-1446
    • Satoh, H.1    Ginsburg, K.S.2    Qing, K.3
  • 41
    • 33748447906 scopus 로고    scopus 로고
    • The inotropic effect of cardioactive glycosides in ventricular myocytes requires Na+-Ca2+ exchanger function
    • Altamirano J., Li Y., DeSantiago J., et al. The inotropic effect of cardioactive glycosides in ventricular myocytes requires Na+-Ca2+ exchanger function. J Physiol 2006, 575:845-854.
    • (2006) J Physiol , vol.575 , pp. 845-854
    • Altamirano, J.1    Li, Y.2    DeSantiago, J.3
  • 42
    • 33845575639 scopus 로고    scopus 로고
    • Differential distribution and regulation of mouse cardiac Na+/K+-ATPase alpha1 and alpha2 subunits in T-tubule and surface sarcolemmal membranes
    • Berry R.G., Despa S., Fuller W., et al. Differential distribution and regulation of mouse cardiac Na+/K+-ATPase alpha1 and alpha2 subunits in T-tubule and surface sarcolemmal membranes. Cardiovasc Res 2007, 73:92-100.
    • (2007) Cardiovasc Res , vol.73 , pp. 92-100
    • Berry, R.G.1    Despa, S.2    Fuller, W.3
  • 43
    • 0023513142 scopus 로고
    • Rat cardiac ventricle has two Na+, K+-ATPases with different affinities for ouabain: Developmental changes in immunologically different catalytic subunits
    • Sweadner K.J., Farshi S.K. Rat cardiac ventricle has two Na+, K+-ATPases with different affinities for ouabain: Developmental changes in immunologically different catalytic subunits. Proc Natl Acad Sci U S A 1987, 84:8404-8407.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 8404-8407
    • Sweadner, K.J.1    Farshi, S.K.2
  • 44
    • 0023677853 scopus 로고
    • Tissue-specific and developmental regulation of rat Na, K-ATPase catalytic alpha isoform and beta subunit mRNAs
    • Orlowski J., Lingrel J.B. Tissue-specific and developmental regulation of rat Na, K-ATPase catalytic alpha isoform and beta subunit mRNAs. J Biol Chem 1988, 263:10436-10442.
    • (1988) J Biol Chem , vol.263 , pp. 10436-10442
    • Orlowski, J.1    Lingrel, J.B.2
  • 45
    • 0018324421 scopus 로고
    • Effect of digoxin on left ventricular contractility in newborns and infants estimated by echocardiography
    • Hofstetter R., Lang D., von Bernuth G. Effect of digoxin on left ventricular contractility in newborns and infants estimated by echocardiography. Eur J Cardiol 1979, 9:1-11.
    • (1979) Eur J Cardiol , vol.9 , pp. 1-11
    • Hofstetter, R.1    Lang, D.2    von Bernuth, G.3
  • 46
    • 0018348153 scopus 로고
    • Dosage of digoxin in premature infants
    • Pinsky W.W., Jacobsen J.R., Gillette P.C., et al. Dosage of digoxin in premature infants. J Pediatr 1979, 94:639-642.
    • (1979) J Pediatr , vol.94 , pp. 639-642
    • Pinsky, W.W.1    Jacobsen, J.R.2    Gillette, P.C.3
  • 47
    • 85012414651 scopus 로고
    • Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle
    • Huxley H.E. Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J Mol Biol 1963, 7:281-308.
    • (1963) J Mol Biol , vol.7 , pp. 281-308
    • Huxley, H.E.1
  • 48
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I., Holden H.M., Whittaker M., et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science 1993, 261:58-65.
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1    Holden, H.M.2    Whittaker, M.3
  • 49
    • 0023161167 scopus 로고
    • Mechanical and structural approaches to correlation of cross-bridge action in muscle with actomyosin ATPase in solution
    • Brenner B. Mechanical and structural approaches to correlation of cross-bridge action in muscle with actomyosin ATPase in solution. Annu Rev Physiol 1987, 49:655-672.
    • (1987) Annu Rev Physiol , vol.49 , pp. 655-672
    • Brenner, B.1
  • 50
    • 0026646783 scopus 로고
    • Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle
    • Metzger J.M., Moss R.L. Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle. Biophys J 1992, 63:460-468.
    • (1992) Biophys J , vol.63 , pp. 460-468
    • Metzger, J.M.1    Moss, R.L.2
  • 52
    • 0027300234 scopus 로고
    • Myosin light chain phosphorylation in vertebrate striated muscle: Regulation and function
    • Sweeney H.L., Bowman B.F., Stull J.T. Myosin light chain phosphorylation in vertebrate striated muscle: Regulation and function. Am J Physiol 1993, 264:C1085-C1095.
    • (1993) Am J Physiol , vol.264
    • Sweeney, H.L.1    Bowman, B.F.2    Stull, J.T.3
  • 53
    • 24344470264 scopus 로고    scopus 로고
    • The M-band: An elastic web that crosslinks thick filaments in the center of the sarcomere
    • Agarkova I., Perriard J.C. The M-band: An elastic web that crosslinks thick filaments in the center of the sarcomere. Trends Cell Biol 2005, 15:477-485.
    • (2005) Trends Cell Biol , vol.15 , pp. 477-485
    • Agarkova, I.1    Perriard, J.C.2
  • 54
    • 0028586108 scopus 로고
    • M-band structure, M-bridge interactions and contraction speed in vertebrate cardiac muscles
    • Pask H.T., Jones K.L., Luther P.K., Squire J.M. M-band structure, M-bridge interactions and contraction speed in vertebrate cardiac muscles. J Muscle Res Cell Motil 1994, 15:633-645.
    • (1994) J Muscle Res Cell Motil , vol.15 , pp. 633-645
    • Pask, H.T.1    Jones, K.L.2    Luther, P.K.3    Squire, J.M.4
  • 55
    • 0025816649 scopus 로고
    • Regulation of skeletal muscle stiffness and elasticity by titin isoforms: A test of the segmental extension model of resting tension
    • Wang K., McCarter R., Wright J., et al. Regulation of skeletal muscle stiffness and elasticity by titin isoforms: A test of the segmental extension model of resting tension. Proc Natl Acad Sci U S A 1991, 88:7101-7105.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 7101-7105
    • Wang, K.1    McCarter, R.2    Wright, J.3
  • 56
    • 0033972217 scopus 로고    scopus 로고
    • Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2
    • Kunst G., Kress K.R., Gruen M., et al. Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2. Circ Res 2000, 86:51-58.
    • (2000) Circ Res , vol.86 , pp. 51-58
    • Kunst, G.1    Kress, K.R.2    Gruen, M.3
  • 57
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon A.M., Homsher E., Regnier M. Regulation of contraction in striated muscle. Physiol Rev 2000, 80:853-924.
    • (2000) Physiol Rev , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 58
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop D.F., Geeves M.A. Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament. Biophys J 1993, 65:693-701.
    • (1993) Biophys J , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 59
    • 0037119477 scopus 로고    scopus 로고
    • A modulatory role for the troponin T tail domain in thin filament regulation
    • Maytum R., Geeves M.A., Lehrer S.S. A modulatory role for the troponin T tail domain in thin filament regulation. J Biol Chem 2002, 277:29774-29780.
    • (2002) J Biol Chem , vol.277 , pp. 29774-29780
    • Maytum, R.1    Geeves, M.A.2    Lehrer, S.S.3
  • 60
    • 0037008682 scopus 로고    scopus 로고
    • The troponin tail domain promotes a conformational state of the thin filament that suppresses myosin activity
    • Tobacman L.S., Nihli M., Butters C., et al. The troponin tail domain promotes a conformational state of the thin filament that suppresses myosin activity. J Biol Chem 2002, 277:27636-27642.
    • (2002) J Biol Chem , vol.277 , pp. 27636-27642
    • Tobacman, L.S.1    Nihli, M.2    Butters, C.3
  • 62
    • 0037059456 scopus 로고    scopus 로고
    • Myofilament calcium sensitivity in skinned rat cardiac trabeculae: Role of interfilament spacing
    • Konhilas J.P., Irving T.C., de Tombe P.P. Myofilament calcium sensitivity in skinned rat cardiac trabeculae: Role of interfilament spacing. Circ Res 2002, 90:59-65.
    • (2002) Circ Res , vol.90 , pp. 59-65
    • Konhilas, J.P.1    Irving, T.C.2    de Tombe, P.P.3
  • 63
    • 0028135302 scopus 로고
    • Tension production and thin-filament protein isoforms in developing rat myocardium
    • Reiser P.J., Westfall M.V., Schiaffino S., Solaro R.J. Tension production and thin-filament protein isoforms in developing rat myocardium. Am J Physiol 1994, 267:H1589-H1596.
    • (1994) Am J Physiol , vol.267
    • Reiser, P.J.1    Westfall, M.V.2    Schiaffino, S.3    Solaro, R.J.4
  • 64
    • 0017885455 scopus 로고
    • Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiace and skeletal muscles
    • Fabiato A., Fabiato F. Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiace and skeletal muscles. J Physiol 1978, 276:233-255.
    • (1978) J Physiol , vol.276 , pp. 233-255
    • Fabiato, A.1    Fabiato, F.2
  • 65
    • 0022546253 scopus 로고
    • Differential effects of pH on calcium activation of myofilaments of adult and perinatal dog hearts: Evidence for developmental differences in thin filament regulation
    • Solaro R.J., Kumar P., Blanchard E.M., Martin A.F. Differential effects of pH on calcium activation of myofilaments of adult and perinatal dog hearts: Evidence for developmental differences in thin filament regulation. Circ Res 1986, 58:721-729.
    • (1986) Circ Res , vol.58 , pp. 721-729
    • Solaro, R.J.1    Kumar, P.2    Blanchard, E.M.3    Martin, A.F.4
  • 66
    • 0023705863 scopus 로고
    • Effects of acidosis on ventricular muscle from adult and neonatal rats
    • Solaro R.J., Lee J.A., Kentish J.C., Allen D.G. Effects of acidosis on ventricular muscle from adult and neonatal rats. Circ Res 1988, 63:779-787.
    • (1988) Circ Res , vol.63 , pp. 779-787
    • Solaro, R.J.1    Lee, J.A.2    Kentish, J.C.3    Allen, D.G.4
  • 67
    • 32244445605 scopus 로고    scopus 로고
    • Histidine button engineered into cardiac troponin I protects the ischemic and failing heart
    • Day S.M., Westfall M.V., Fomicheva E.V., et al. Histidine button engineered into cardiac troponin I protects the ischemic and failing heart. Nat Med 2006, 12:181-189.
    • (2006) Nat Med , vol.12 , pp. 181-189
    • Day, S.M.1    Westfall, M.V.2    Fomicheva, E.V.3
  • 68
    • 0025935299 scopus 로고
    • Troponin I isoform expression in human heart
    • Hunkeler N.M., Kullman J., Murphy A.M. Troponin I isoform expression in human heart. Circ Res 1991, 69:1409-1414.
    • (1991) Circ Res , vol.69 , pp. 1409-1414
    • Hunkeler, N.M.1    Kullman, J.2    Murphy, A.M.3
  • 69
    • 0030773407 scopus 로고    scopus 로고
    • Troponin I phosphorylation in the normal and failing adult human heart
    • Bodor G.S., Oakeley A.E., Allen P.D., et al. Troponin I phosphorylation in the normal and failing adult human heart. Circulation 1997, 96:1495-1500.
    • (1997) Circulation , vol.96 , pp. 1495-1500
    • Bodor, G.S.1    Oakeley, A.E.2    Allen, P.D.3
  • 70
    • 0033563035 scopus 로고    scopus 로고
    • Impaired cardiomyocyte relaxation and diastolic function in transgenic mice expressing slow skeletal troponin I in the heart
    • Fentzke R.C., Buck S.H., Patel J.R., et al. Impaired cardiomyocyte relaxation and diastolic function in transgenic mice expressing slow skeletal troponin I in the heart. J Physiol 1999, 517:143-157.
    • (1999) J Physiol , vol.517 , pp. 143-157
    • Fentzke, R.C.1    Buck, S.H.2    Patel, J.R.3
  • 71
    • 0033841530 scopus 로고    scopus 로고
    • Attenuation of length dependence of calcium activation in myofilaments of transgenic mouse hearts expressing slow skeletal troponin I
    • Arteaga G.M., Palmiter K.A., Leiden J.M., Solaro R.J. Attenuation of length dependence of calcium activation in myofilaments of transgenic mouse hearts expressing slow skeletal troponin I. J Physiol 2000, 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
  • 72
    • 0029146873 scopus 로고
    • The unique amino-terminal peptide of cardiac troponin I regulates myofibrillar activity only when it is phosphorylated
    • Wattanapermpool J., Guo X., Solaro R.J. The unique amino-terminal peptide of cardiac troponin I regulates myofibrillar activity only when it is phosphorylated. J Mol Cell Cardiol 1995, 27:1383-1391.
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 1383-1391
    • Wattanapermpool, J.1    Guo, X.2    Solaro, R.J.3
  • 73
    • 0028943382 scopus 로고
    • Molecular basis of human cardiac troponin T isoforms expressed in the developing, adult, and failing heart
    • Anderson P.A., Greig A., Mark T.M., et al. Molecular basis of human cardiac troponin T isoforms expressed in the developing, adult, and failing heart. Circ Res 1995, 76:681-686.
    • (1995) Circ Res , vol.76 , pp. 681-686
    • Anderson, P.A.1    Greig, A.2    Mark, T.M.3
  • 74
    • 0037144508 scopus 로고    scopus 로고
    • Cardiac troponin T isoforms affect the Ca2+ sensitivity and inhibition of force development: Insights into the role of troponin T isoforms in the heart
    • Gomes A.V., Guzman G., Zhao J., Potter J.D. Cardiac troponin T isoforms affect the Ca2+ sensitivity and inhibition of force development: Insights into the role of troponin T isoforms in the heart. J Biol Chem 2002, 277:35341-35349.
    • (2002) J Biol Chem , vol.277 , pp. 35341-35349
    • Gomes, A.V.1    Guzman, G.2    Zhao, J.3    Potter, J.D.4
  • 75
    • 9644281066 scopus 로고    scopus 로고
    • 2+ sensitivity of force development in the presence of slow skeletal troponin I: Insights into the role of troponin T isoforms in the fetal heart
    • 2+ sensitivity of force development in the presence of slow skeletal troponin I: Insights into the role of troponin T isoforms in the fetal heart. J Biol Chem 2004, 279:49579-49587.
    • (2004) J Biol Chem , vol.279 , pp. 49579-49587
    • Gomes, A.V.1    Venkatraman, G.2    Davis, J.P.3
  • 76
    • 0027285642 scopus 로고
    • Developmental analysis of tropomyosin gene expression in embryonic stem cells and mouse embryos
    • Muthuchamy M., Pajak L., Howles P., et al. Developmental analysis of tropomyosin gene expression in embryonic stem cells and mouse embryos. Mol Cell Biol 1993, 13:3311-3323.
    • (1993) Mol Cell Biol , vol.13 , pp. 3311-3323
    • Muthuchamy, M.1    Pajak, L.2    Howles, P.3
  • 77
    • 0021610707 scopus 로고
    • Regulatory proteins of the myocardium: Atrial and ventricular tropomyosin and troponin-I in the developing and adult bovine and human heart
    • Humphreys J.E., Cummins P. Regulatory proteins of the myocardium: Atrial and ventricular tropomyosin and troponin-I in the developing and adult bovine and human heart. J Mol Cell Cardiol 1984, 16:643-657.
    • (1984) J Mol Cell Cardiol , vol.16 , pp. 643-657
    • Humphreys, J.E.1    Cummins, P.2
  • 78
    • 0029559447 scopus 로고
    • Molecular and physiological effects of overexpressing striated muscle beta-tropomyosin in the adult murine heart
    • Muthuchamy M., Grupp I.L., Grupp G., et al. Molecular and physiological effects of overexpressing striated muscle beta-tropomyosin in the adult murine heart. J Biol Chem 1995, 270:30593-30603.
    • (1995) J Biol Chem , vol.270 , pp. 30593-30603
    • Muthuchamy, M.1    Grupp, I.L.2    Grupp, G.3
  • 79
    • 0024836467 scopus 로고
    • Cellular distribution of smooth muscle actins during mammalian embryogenesis: Expression of the alpha-vascular but not the gamma-enteric isoform in differentiating striated myocytes
    • Sawtell N.M., Lessard J.L. Cellular distribution of smooth muscle actins during mammalian embryogenesis: Expression of the alpha-vascular but not the gamma-enteric isoform in differentiating striated myocytes. J Cell Biol 1989, 109:2929-2937.
    • (1989) J Cell Biol , vol.109 , pp. 2929-2937
    • Sawtell, N.M.1    Lessard, J.L.2
  • 80
    • 0026521724 scopus 로고
    • Onset of expression and regional deposition of alpha-smooth and sarcomeric actin during avian heart development
    • Sugi Y., Lough J. Onset of expression and regional deposition of alpha-smooth and sarcomeric actin during avian heart development. Dev Dyn 1992, 193:116-124.
    • (1992) Dev Dyn , vol.193 , pp. 116-124
    • Sugi, Y.1    Lough, J.2
  • 81
    • 0026355337 scopus 로고
    • A comprehensive analysis of the developmental and tissue-specific expression of the isoactin multigene family in the rat
    • McHugh K.M., Crawford K., Lessard J.L. A comprehensive analysis of the developmental and tissue-specific expression of the isoactin multigene family in the rat. Dev Biol 1991, 148:442-458.
    • (1991) Dev Biol , vol.148 , pp. 442-458
    • McHugh, K.M.1    Crawford, K.2    Lessard, J.L.3
  • 82
    • 0025848197 scopus 로고
    • Skeletal actin mRNA increases in the human heart during ontogenic development and is the major isoform of control and failing adult hearts
    • Boheler K.R., Carrier L., de la Bastie D., et al. Skeletal actin mRNA increases in the human heart during ontogenic development and is the major isoform of control and failing adult hearts. J Clin Invest 1991, 88:323-330.
    • (1991) J Clin Invest , vol.88 , pp. 323-330
    • Boheler, K.R.1    Carrier, L.2    de la Bastie, D.3
  • 83
    • 0020506125 scopus 로고
    • Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers
    • Pardo J.V., Siliciano J.D., Craig S.W. Vinculin is a component of an extensive network of myofibril-sarcolemma attachment regions in cardiac muscle fibers. J Cell Biol 1983, 97:1081-1088.
    • (1983) J Cell Biol , vol.97 , pp. 1081-1088
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 84
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti J.M., Campbell K.P. Membrane organization of the dystrophin-glycoprotein complex. Cell 1991, 66:1121-1131.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 85
    • 0026165749 scopus 로고
    • Structure and evolution of the actin crosslinking proteins
    • Dubreuil R.R. Structure and evolution of the actin crosslinking proteins. Bioessays 1991, 13:219-226.
    • (1991) Bioessays , vol.13 , pp. 219-226
    • Dubreuil, R.R.1
  • 86
    • 0035827723 scopus 로고    scopus 로고
    • Integrins and the myocardium
    • Ross R.S., Borg T.K. Integrins and the myocardium. Circ Res 2001, 88:1112-1119.
    • (2001) Circ Res , vol.88 , pp. 1112-1119
    • Ross, R.S.1    Borg, T.K.2
  • 88
    • 0024509062 scopus 로고
    • Expression of collagen adhesion proteins and their association with the cytoskeleton in cardiac myocytes
    • Terracio L., Gullberg D., Rubin K., et al. Expression of collagen adhesion proteins and their association with the cytoskeleton in cardiac myocytes. Anat Rec 1989, 223:62-71.
    • (1989) Anat Rec , vol.223 , pp. 62-71
    • Terracio, L.1    Gullberg, D.2    Rubin, K.3
  • 89
    • 0026026685 scopus 로고
    • Expression of collagen binding integrins during cardiac development and hypertrophy
    • Terracio L., Rubin K., Gullberg D., et al. Expression of collagen binding integrins during cardiac development and hypertrophy. Circ Res 1991, 68:734-744.
    • (1991) Circ Res , vol.68 , pp. 734-744
    • Terracio, L.1    Rubin, K.2    Gullberg, D.3
  • 90
  • 91
    • 0021009545 scopus 로고
    • Gamma actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites
    • Craig S.W., Pardo J.V. Gamma actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites. Cell Motil 1983, 3:449-462.
    • (1983) Cell Motil , vol.3 , pp. 449-462
    • Craig, S.W.1    Pardo, J.V.2
  • 92
    • 0029799148 scopus 로고    scopus 로고
    • Expression of intermediate filament desmin and vimentin in the human fetal heart
    • Kim H.D. Expression of intermediate filament desmin and vimentin in the human fetal heart. Anat Rec 1996, 246:271-278.
    • (1996) Anat Rec , vol.246 , pp. 271-278
    • Kim, H.D.1
  • 93
    • 33745726394 scopus 로고    scopus 로고
    • Plasticity of cardiac titin/connectin in heart development
    • Opitz C.A., Linke W.A. Plasticity of cardiac titin/connectin in heart development. J Muscle Res Cell Motil 2005, 26:333-342.
    • (2005) J Muscle Res Cell Motil , vol.26 , pp. 333-342
    • Opitz, C.A.1    Linke, W.A.2
  • 94
    • 0018831307 scopus 로고
    • Morphometric study of early postnatal development in the left and right ventricular myocardium of the rat: II. Tissue composition, capillary growth, and sarcoplasmic alterations
    • Olivetti G., Anversa P., Loud A.V. Morphometric study of early postnatal development in the left and right ventricular myocardium of the rat: II. Tissue composition, capillary growth, and sarcoplasmic alterations. Circ Res 1980, 46:503-512.
    • (1980) Circ Res , vol.46 , pp. 503-512
    • Olivetti, G.1    Anversa, P.2    Loud, A.V.3
  • 95
    • 0017332553 scopus 로고
    • Ultrastructural changes in rabbit heart mitochondria during the perinatal period: Neonatal transition to aerobic metabolism
    • Smith H.E., Page E. Ultrastructural changes in rabbit heart mitochondria during the perinatal period: Neonatal transition to aerobic metabolism. Dev Biol 1977, 57:109-117.
    • (1977) Dev Biol , vol.57 , pp. 109-117
    • Smith, H.E.1    Page, E.2
  • 96
    • 0018346393 scopus 로고
    • Cellular mechanisms of normal growth in the mammalian heart: II. A quantitative and qualitative comparison between the right and left ventricular myocytes in the dog from birth to five months of age
    • Legato M.J. Cellular mechanisms of normal growth in the mammalian heart: II. A quantitative and qualitative comparison between the right and left ventricular myocytes in the dog from birth to five months of age. Circ Res 1979, 44:263-279.
    • (1979) Circ Res , vol.44 , pp. 263-279
    • Legato, M.J.1
  • 97
    • 33745502336 scopus 로고    scopus 로고
    • N-terminal residues in Cx43 and Cx40 determine physiological properties of gap junction channels, but do not influence heteromeric assembly with each other or with Cx26
    • Gemel J., Lin X., Veenstra R.D., Beyer E.C. N-terminal residues in Cx43 and Cx40 determine physiological properties of gap junction channels, but do not influence heteromeric assembly with each other or with Cx26. J Cell Sci 2006, 119:2258-2268.
    • (2006) J Cell Sci , vol.119 , pp. 2258-2268
    • Gemel, J.1    Lin, X.2    Veenstra, R.D.3    Beyer, E.C.4
  • 98
    • 0035985057 scopus 로고    scopus 로고
    • Structural and functional diversity of connexin genes in the mouse and human genome
    • Willecke K., Eiberger J., Degen J., et al. Structural and functional diversity of connexin genes in the mouse and human genome. Biol Chem 2002, 383:725-737.
    • (2002) Biol Chem , vol.383 , pp. 725-737
    • Willecke, K.1    Eiberger, J.2    Degen, J.3
  • 99
    • 0021894449 scopus 로고
    • Physiology and pharmacology of gap junctions
    • Spray D.C., Bennett M.V. Physiology and pharmacology of gap junctions. Annu Rev Physiol 1985, 47:281-303.
    • (1985) Annu Rev Physiol , vol.47 , pp. 281-303
    • Spray, D.C.1    Bennett, M.V.2
  • 100
    • 27244462402 scopus 로고
    • Tyrosine phosphorylation of the gap junction protein connexin43 is required for the pp60v-src-induced inhibition of communication
    • Swenson K.I., Piwnica-Worms H., McNamee H., Paul D.L. Tyrosine phosphorylation of the gap junction protein connexin43 is required for the pp60v-src-induced inhibition of communication. Cell Regul 1990, 1:989-1002.
    • (1990) Cell Regul , vol.1 , pp. 989-1002
    • Swenson, K.I.1    Piwnica-Worms, H.2    McNamee, H.3    Paul, D.L.4
  • 101
    • 0035704411 scopus 로고    scopus 로고
    • Emerging issues of connexin channels: Biophysics fills the gap
    • Harris A.L. Emerging issues of connexin channels: Biophysics fills the gap. Q Rev Biophys 2001, 34:325-472.
    • (2001) Q Rev Biophys , vol.34 , pp. 325-472
    • Harris, A.L.1
  • 102
    • 0019502831 scopus 로고
    • Diameter of the cell-to-cell junctional membrane channels as probed with neutral molecules
    • Schwarzmann G., Wiegandt H., Rose B., et al. Diameter of the cell-to-cell junctional membrane channels as probed with neutral molecules. Science 1981, 213:551-553.
    • (1981) Science , vol.213 , pp. 551-553
    • Schwarzmann, G.1    Wiegandt, H.2    Rose, B.3
  • 103
    • 0019310233 scopus 로고
    • Ultrastructural changes during development of gap junctions in rabbit left ventricular myocardial cells
    • Shibata Y., Nakata K., Page E. Ultrastructural changes during development of gap junctions in rabbit left ventricular myocardial cells. J Ultrastruct Res 1980, 71:258-271.
    • (1980) J Ultrastruct Res , vol.71 , pp. 258-271
    • Shibata, Y.1    Nakata, K.2    Page, E.3
  • 104
    • 0018199998 scopus 로고
    • Formation and growth of gap junctions in mouse myocardium during ontogenesis: A freeze-cleave study
    • Gros D., Mocquard J.P., Challice C.E., Schrevel J. Formation and growth of gap junctions in mouse myocardium during ontogenesis: A freeze-cleave study. J Cell Sci 1978, 30:45-61.
    • (1978) J Cell Sci , vol.30 , pp. 45-61
    • Gros, D.1    Mocquard, J.P.2    Challice, C.E.3    Schrevel, J.4
  • 105
    • 0026693725 scopus 로고
    • Multiple connexins confer distinct regulatory and conductance properties of gap junctions in developing heart
    • Veenstra R.D., Wang H.Z., Westphale E.M., Beyer E.C. Multiple connexins confer distinct regulatory and conductance properties of gap junctions in developing heart. Circ Res 1992, 71:1277-1283.
    • (1992) Circ Res , vol.71 , pp. 1277-1283
    • Veenstra, R.D.1    Wang, H.Z.2    Westphale, E.M.3    Beyer, E.C.4
  • 106
    • 0025729509 scopus 로고
    • Spatial distribution of connexin43, the major cardiac gap junction protein, in the developing and adult rat heart
    • van Kempen M.J., Fromaget C., Gros D., et al. Spatial distribution of connexin43, the major cardiac gap junction protein, in the developing and adult rat heart. Circ Res 1991, 68:1638-1651.
    • (1991) Circ Res , vol.68 , pp. 1638-1651
    • van Kempen, M.J.1    Fromaget, C.2    Gros, D.3
  • 107
    • 0023463846 scopus 로고
    • Cell surface receptors for extracellular matrix molecules
    • Buck C.A., Horwitz A.F. Cell surface receptors for extracellular matrix molecules. Annu Rev Cell Biol 1987, 3:179-205.
    • (1987) Annu Rev Cell Biol , vol.3 , pp. 179-205
    • Buck, C.A.1    Horwitz, A.F.2
  • 108
    • 33845654352 scopus 로고    scopus 로고
    • Dynamic interactions between myocytes, fibroblasts, and extracellular matrix
    • Banerjee I., Yekkala K., Borg T.K., Baudino T.A. Dynamic interactions between myocytes, fibroblasts, and extracellular matrix. Ann N Y Acad Sci 2006, 1080:76-84.
    • (2006) Ann N Y Acad Sci , vol.1080 , pp. 76-84
    • Banerjee, I.1    Yekkala, K.2    Borg, T.K.3    Baudino, T.A.4
  • 109
    • 1942494484 scopus 로고    scopus 로고
    • Organization of fibroblasts in the heart
    • Goldsmith E.C., Hoffman A., Morales M.O., et al. Organization of fibroblasts in the heart. Dev Dyn 2004, 230:787-794.
    • (2004) Dev Dyn , vol.230 , pp. 787-794
    • Goldsmith, E.C.1    Hoffman, A.2    Morales, M.O.3
  • 110
    • 0026726189 scopus 로고
    • Ultrastructural localization of laminin on in vivo embryonic, neonatal, and adult rat cardiac myocytes and in early rat embryos raised in whole-embryo culture
    • Price R.L., Nakagawa M., Terracio L., Borg T.K. Ultrastructural localization of laminin on in vivo embryonic, neonatal, and adult rat cardiac myocytes and in early rat embryos raised in whole-embryo culture. J Histochem Cytochem 1992, 40:1373-1381.
    • (1992) J Histochem Cytochem , vol.40 , pp. 1373-1381
    • Price, R.L.1    Nakagawa, M.2    Terracio, L.3    Borg, T.K.4
  • 111
    • 20744435789 scopus 로고    scopus 로고
    • Cross talk between cell-cell and cell-matrix adhesion signaling pathways during heart organogenesis: Implications for cardiac birth defects
    • Linask K.K., Manisastry S., Han M. Cross talk between cell-cell and cell-matrix adhesion signaling pathways during heart organogenesis: Implications for cardiac birth defects. Microsc Microanal 2005, 11:200-208.
    • (2005) Microsc Microanal , vol.11 , pp. 200-208
    • Linask, K.K.1    Manisastry, S.2    Han, M.3
  • 112
    • 0020327069 scopus 로고
    • Changes in the distribution of fibronectin and collagen during development of the neonatal rat heart
    • Borg T.K., Gay R.E., Johnson L.D. Changes in the distribution of fibronectin and collagen during development of the neonatal rat heart. Coll Relat Res 1982, 2:211-218.
    • (1982) Coll Relat Res , vol.2 , pp. 211-218
    • Borg, T.K.1    Gay, R.E.2    Johnson, L.D.3
  • 113
    • 0028296384 scopus 로고
    • The neonatal heart has a relatively high content of total collagen and type I collagen, a condition that may explain the less compliant state
    • Marijianowski M.M., van der Loos C.M., Mohrschladt M.F., Becker A.E. The neonatal heart has a relatively high content of total collagen and type I collagen, a condition that may explain the less compliant state. J Am Coll Cardiol 1994, 23:1204-1208.
    • (1994) J Am Coll Cardiol , vol.23 , pp. 1204-1208
    • Marijianowski, M.M.1    van der Loos, C.M.2    Mohrschladt, M.F.3    Becker, A.E.4
  • 114
    • 0023225627 scopus 로고
    • Neural crest cell migratory pathways in the trunk of the chick embryo
    • Loring J.F., Erickson C.A. Neural crest cell migratory pathways in the trunk of the chick embryo. Dev Biol 1987, 121:220-236.
    • (1987) Dev Biol , vol.121 , pp. 220-236
    • Loring, J.F.1    Erickson, C.A.2
  • 115
    • 0018776001 scopus 로고
    • The force-interval relationship of the left ventricle
    • Anderson P.A., Manring A., Serwer G.A., et al. The force-interval relationship of the left ventricle. Circulation 1979, 60:334-348.
    • (1979) Circulation , vol.60 , pp. 334-348
    • Anderson, P.A.1    Manring, A.2    Serwer, G.A.3
  • 116
    • 0018645221 scopus 로고
    • Age-related cardiovascular effects of catecholamines in anesthetized piglets
    • Buckley N.M., Gootman P.M., Yellin E.L., Brazeau P. Age-related cardiovascular effects of catecholamines in anesthetized piglets. Circ Res 1979, 45:282-292.
    • (1979) Circ Res , vol.45 , pp. 282-292
    • Buckley, N.M.1    Gootman, P.M.2    Yellin, E.L.3    Brazeau, P.4
  • 117
    • 0018857046 scopus 로고
    • The postnatal development of adrenoceptor responses in isolated papillary muscles from rat
    • Mackenzie E., Standen N.B. The postnatal development of adrenoceptor responses in isolated papillary muscles from rat. Pflugers Arch 1980, 383:185-187.
    • (1980) Pflugers Arch , vol.383 , pp. 185-187
    • Mackenzie, E.1    Standen, N.B.2
  • 118
    • 0019508514 scopus 로고
    • Cellular mechanisms of impaired adrenergic responsiveness in neonatal dogs
    • Rockson S.G., Homcy C.J., Quinn P., et al. Cellular mechanisms of impaired adrenergic responsiveness in neonatal dogs. J Clin Invest 1981, 67:319-327.
    • (1981) J Clin Invest , vol.67 , pp. 319-327
    • Rockson, S.G.1    Homcy, C.J.2    Quinn, P.3
  • 119
    • 0020533297 scopus 로고
    • Functional development of adrenergic uptake mechanisms in the human fetal heart
    • Saarikoski S. Functional development of adrenergic uptake mechanisms in the human fetal heart. Biol Neonate 1983, 43:158-163.
    • (1983) Biol Neonate , vol.43 , pp. 158-163
    • Saarikoski, S.1
  • 120
    • 0014865191 scopus 로고
    • Ontogenesis of peripheral adrenergic neurons in the rat: Pre- and postnatal observations
    • De Champlain J., Malmfors T., Olson L., Sachs C. Ontogenesis of peripheral adrenergic neurons in the rat: Pre- and postnatal observations. Acta Physiol Scand 1970, 80:276-288.
    • (1970) Acta Physiol Scand , vol.80 , pp. 276-288
    • De Champlain, J.1    Malmfors, T.2    Olson, L.3    Sachs, C.4
  • 121
    • 0014830495 scopus 로고
    • The early pattern of cardiac innervation in the fetal guinea pig
    • Hoar R.M., Hall J.L. The early pattern of cardiac innervation in the fetal guinea pig. Am J Anat 1970, 128:499-508.
    • (1970) Am J Anat , vol.128 , pp. 499-508
    • Hoar, R.M.1    Hall, J.L.2
  • 122
    • 0019451131 scopus 로고
    • Development of innervation to the ventricular myocardium of the rabbit
    • Papka R.E. Development of innervation to the ventricular myocardium of the rabbit. J Mol Cell Cardiol 1981, 13:217-228.
    • (1981) J Mol Cell Cardiol , vol.13 , pp. 217-228
    • Papka, R.E.1


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