메뉴 건너뛰기




Volumn 131, Issue 1, 2008, Pages 33-44

A broken heart: A stretch too far. An overview of mouse models with mutations in stretch-sensor components

Author keywords

Cardiomyopathy; Hypertrophy; Mouse model; Stretch

Indexed keywords

PROTEIN;

EID: 56349153013     PISSN: 01675273     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijcard.2008.06.049     Document Type: Review
Times cited : (15)

References (118)
  • 1
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction; interference microscopy of living muscle fibres
    • Huxley A.F., and Niedergerke R. Structural changes in muscle during contraction; interference microscopy of living muscle fibres. Nature 173 (1954) 971-973
    • (1954) Nature , vol.173 , pp. 971-973
    • Huxley, A.F.1    Niedergerke, R.2
  • 2
    • 33744494538 scopus 로고    scopus 로고
    • The sarcomeric Z-disc: a nodal point in signalling and disease
    • Frank D., Kuhn C., Katus H.A., and Frey N. The sarcomeric Z-disc: a nodal point in signalling and disease. J Mol Med 84 (2006) 446-468
    • (2006) J Mol Med , vol.84 , pp. 446-468
    • Frank, D.1    Kuhn, C.2    Katus, H.A.3    Frey, N.4
  • 3
    • 1242320058 scopus 로고    scopus 로고
    • At the crossroads of myocardial signaling: the role of Z-discs in intracellular signaling and cardiac function
    • Pyle W.G., and Solaro R.J. At the crossroads of myocardial signaling: the role of Z-discs in intracellular signaling and cardiac function. Circ Res 94 (2004) 296-305
    • (2004) Circ Res , vol.94 , pp. 296-305
    • Pyle, W.G.1    Solaro, R.J.2
  • 4
    • 0038190993 scopus 로고    scopus 로고
    • Costameres: the Achilles' heel of Herculean muscle
    • Ervasti J.M. Costameres: the Achilles' heel of Herculean muscle. J Biol Chem 278 (2003) 13591-13594
    • (2003) J Biol Chem , vol.278 , pp. 13591-13594
    • Ervasti, J.M.1
  • 5
    • 0026008748 scopus 로고
    • Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: correlation of thin filament length, nebulin size, and epitope profile
    • Kruger M., Wright J., and Wang K. Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: correlation of thin filament length, nebulin size, and epitope profile. J Cell Biol 115 (1991) 97-107
    • (1991) J Cell Biol , vol.115 , pp. 97-107
    • Kruger, M.1    Wright, J.2    Wang, K.3
  • 6
    • 33750061609 scopus 로고    scopus 로고
    • Cardiac titin: structure, functions and role in disease
    • LeWinter M.M., Wu Y., Labeit S., and Granzier H. Cardiac titin: structure, functions and role in disease. Clin Chim Acta 375 (2007) 1-9
    • (2007) Clin Chim Acta , vol.375 , pp. 1-9
    • LeWinter, M.M.1    Wu, Y.2    Labeit, S.3    Granzier, H.4
  • 7
    • 24944524470 scopus 로고    scopus 로고
    • Nebulin regulates the assembly and lengths of the thin filaments in striated muscle
    • McElhinny A.S., Schwach C., Valichnac M., Mount-Patrick S., and Gregorio C.C. Nebulin regulates the assembly and lengths of the thin filaments in striated muscle. J Cell Biol 170 (2005) 947-957
    • (2005) J Cell Biol , vol.170 , pp. 947-957
    • McElhinny, A.S.1    Schwach, C.2    Valichnac, M.3    Mount-Patrick, S.4    Gregorio, C.C.5
  • 8
    • 0028784365 scopus 로고
    • Nebulette: a 107 kD nebulin-like protein in cardiac muscle
    • Moncman C.L., and Wang K. Nebulette: a 107 kD nebulin-like protein in cardiac muscle. Cell Motil Cytoskeleton 32 (1995) 205-225
    • (1995) Cell Motil Cytoskeleton , vol.32 , pp. 205-225
    • Moncman, C.L.1    Wang, K.2
  • 9
    • 0032557642 scopus 로고    scopus 로고
    • Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin
    • Mues A., van der Ven P.F., Young P., Fürst D.O., and Gautel M. Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin. FEBS Lett 428 (1998) 111-114
    • (1998) FEBS Lett , vol.428 , pp. 111-114
    • Mues, A.1    van der Ven, P.F.2    Young, P.3    Fürst, D.O.4    Gautel, M.5
  • 10
    • 0031590316 scopus 로고    scopus 로고
    • Telethonin, a novel sarcomeric protein of heart and skeletal muscle
    • Valle G., Faulkner G., De Antoni A., et al. Telethonin, a novel sarcomeric protein of heart and skeletal muscle. FEBS Lett 415 (1997) 163-168
    • (1997) FEBS Lett , vol.415 , pp. 163-168
    • Valle, G.1    Faulkner, G.2    De Antoni, A.3
  • 11
    • 0032538660 scopus 로고    scopus 로고
    • The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity
    • Gregorio C.C., Trombitas K., Centner T., et al. The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity. J Cell Biol 143 (1998) 1013-1027
    • (1998) J Cell Biol , vol.143 , pp. 1013-1027
    • Gregorio, C.C.1    Trombitas, K.2    Centner, T.3
  • 12
    • 0030871066 scopus 로고    scopus 로고
    • Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression
    • Louis H.A., Pino J.D., Schmeichel K.L., Pomies P., and Beckerle M.C. Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression. J Biol Chem 272 (1997) 27484-27491
    • (1997) J Biol Chem , vol.272 , pp. 27484-27491
    • Louis, H.A.1    Pino, J.D.2    Schmeichel, K.L.3    Pomies, P.4    Beckerle, M.C.5
  • 13
    • 0034663572 scopus 로고    scopus 로고
    • Fine mapping of the alpha-actinin binding site within cysteine-rich protein
    • Harper B.D., Beckerle M.C., and Pomies P. Fine mapping of the alpha-actinin binding site within cysteine-rich protein. Biochem J 350 Pt 1 (2000) 269-274
    • (2000) Biochem J , vol.350 , Issue.PART 1 , pp. 269-274
    • Harper, B.D.1    Beckerle, M.C.2    Pomies, P.3
  • 14
    • 0034687814 scopus 로고    scopus 로고
    • Calsarcins, a novel family of sarcomeric calcineurin-binding proteins
    • Frey N., Richardson J.A., and Olson E.N. Calsarcins, a novel family of sarcomeric calcineurin-binding proteins. Proc Natl Acad Sci U S A 97 (2000) 14632-14637
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14632-14637
    • Frey, N.1    Richardson, J.A.2    Olson, E.N.3
  • 15
    • 9644281144 scopus 로고    scopus 로고
    • Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy
    • Hayashi T., Arimura T., Itoh-Satoh M., et al. Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy. J Am Coll Cardiol 44 (2004) 2192-2201
    • (2004) J Am Coll Cardiol , vol.44 , pp. 2192-2201
    • Hayashi, T.1    Arimura, T.2    Itoh-Satoh, M.3
  • 16
    • 0035852783 scopus 로고    scopus 로고
    • Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines
    • Takada F., Vander Woude D.L., Tong H.Q., et al. Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines. Proc Natl Acad Sci U S A 98 (2001) 1595-1600
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1595-1600
    • Takada, F.1    Vander Woude, D.L.2    Tong, H.Q.3
  • 17
    • 36849043778 scopus 로고    scopus 로고
    • Interaction of BMP10 with Tcap may modulate the course of hypertensive cardiac hypertrophy
    • Nakano N., Hori H., Abe M., et al. Interaction of BMP10 with Tcap may modulate the course of hypertensive cardiac hypertrophy. Am J Physiol Heart Circ Physiol 293 6 (2007) H3396-H3403
    • (2007) Am J Physiol Heart Circ Physiol , vol.293 , Issue.6
    • Nakano, N.1    Hori, H.2    Abe, M.3
  • 18
    • 0027959864 scopus 로고
    • Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates
    • Schafer D.A., Korshunova Y.O., Schroer T.A., and Cooper J.A. Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates. J Cell Biol 127 (1994) 453-465
    • (1994) J Cell Biol , vol.127 , pp. 453-465
    • Schafer, D.A.1    Korshunova, Y.O.2    Schroer, T.A.3    Cooper, J.A.4
  • 19
    • 0033552611 scopus 로고    scopus 로고
    • Vertebrate isoforms of actin capping protein beta have distinct functions In vivo
    • Hart M.C., and Cooper J.A. Vertebrate isoforms of actin capping protein beta have distinct functions In vivo. J Cell Biol 147 (1999) 1287-1298
    • (1999) J Cell Biol , vol.147 , pp. 1287-1298
    • Hart, M.C.1    Cooper, J.A.2
  • 20
    • 0032997340 scopus 로고    scopus 로고
    • Alpha actinin-CapZ, an anchoring complex for thin filaments in Z-line
    • Papa I., Astier C., Kwiatek O., et al. Alpha actinin-CapZ, an anchoring complex for thin filaments in Z-line. J Muscle Res Cell Motil 20 (1999) 187-197
    • (1999) J Muscle Res Cell Motil , vol.20 , pp. 187-197
    • Papa, I.1    Astier, C.2    Kwiatek, O.3
  • 21
    • 0033538565 scopus 로고    scopus 로고
    • Cypher, a striated muscle-restricted PDZ and LIM domain-containing protein, binds to alpha-actinin-2 and protein kinase C
    • Zhou Q., Ruiz-Lozano P., Martone M.E., and Chen J. Cypher, a striated muscle-restricted PDZ and LIM domain-containing protein, binds to alpha-actinin-2 and protein kinase C. J Biol Chem 274 (1999) 19807-19813
    • (1999) J Biol Chem , vol.274 , pp. 19807-19813
    • Zhou, Q.1    Ruiz-Lozano, P.2    Martone, M.E.3    Chen, J.4
  • 22
    • 0030827949 scopus 로고    scopus 로고
    • Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs
    • Xia H., Winokur S.T., Kuo W.L., Altherr M.R., and Bredt D.S. Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs. J Cell Biol 139 (1997) 507-515
    • (1997) J Cell Biol , vol.139 , pp. 507-515
    • Xia, H.1    Winokur, S.T.2    Kuo, W.L.3    Altherr, M.R.4    Bredt, D.S.5
  • 23
    • 0034646678 scopus 로고    scopus 로고
    • CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4
    • Vallenius T., Luukko K., and Makela T.P. CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4. J Biol Chem 275 (2000) 11100-11105
    • (2000) J Biol Chem , vol.275 , pp. 11100-11105
    • Vallenius, T.1    Luukko, K.2    Makela, T.P.3
  • 24
    • 0030054916 scopus 로고    scopus 로고
    • Specificity of LIM domain interactions with receptor tyrosine kinases
    • Wu R., Durick K., Songyang Z., Cantley L.C., Taylor S.S., and Gill G.N. Specificity of LIM domain interactions with receptor tyrosine kinases. J Biol Chem 271 (1996) 15934-15941
    • (1996) J Biol Chem , vol.271 , pp. 15934-15941
    • Wu, R.1    Durick, K.2    Songyang, Z.3    Cantley, L.C.4    Taylor, S.S.5    Gill, G.N.6
  • 25
    • 0029962498 scopus 로고    scopus 로고
    • Protein-protein interaction of zinc finger LIM domains with protein kinase C
    • Kuroda S., Tokunaga C., Kiyohara Y., et al. Protein-protein interaction of zinc finger LIM domains with protein kinase C. J Biol Chem 271 (1996) 31029-31032
    • (1996) J Biol Chem , vol.271 , pp. 31029-31032
    • Kuroda, S.1    Tokunaga, C.2    Kiyohara, Y.3
  • 26
    • 14644414790 scopus 로고    scopus 로고
    • Protein kinase cascades in the regulation of cardiac hypertrophy
    • Dorn II G.W., and Force T. Protein kinase cascades in the regulation of cardiac hypertrophy. J Clin Invest 115 (2005) 527-537
    • (2005) J Clin Invest , vol.115 , pp. 527-537
    • Dorn II, G.W.1    Force, T.2
  • 27
    • 0035923670 scopus 로고    scopus 로고
    • S100A1: a regulator of myocardial contractility
    • Most P., Bernotat J., Ehlermann P., et al. S100A1: a regulator of myocardial contractility. Proc Natl Acad Sci U S A 98 (2001) 13889-13894
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 13889-13894
    • Most, P.1    Bernotat, J.2    Ehlermann, P.3
  • 29
    • 24944550989 scopus 로고    scopus 로고
    • The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins
    • Gontier Y., Taivainen A., Fontao L., et al. The Z-disc proteins myotilin and FATZ-1 interact with each other and are connected to the sarcolemma via muscle-specific filamins. J Cell Sci 118 (2005) 3739-3749
    • (2005) J Cell Sci , vol.118 , pp. 3739-3749
    • Gontier, Y.1    Taivainen, A.2    Fontao, L.3
  • 30
    • 33846017683 scopus 로고    scopus 로고
    • Myomaxin is a novel transcriptional target of MEF2A that encodes a Xin-related alpha-actinin-interacting protein
    • Huang H.T., Brand O.M., Mathew M., et al. Myomaxin is a novel transcriptional target of MEF2A that encodes a Xin-related alpha-actinin-interacting protein. J Biol Chem 281 (2006) 39370-39379
    • (2006) J Biol Chem , vol.281 , pp. 39370-39379
    • Huang, H.T.1    Brand, O.M.2    Mathew, M.3
  • 31
    • 28144435989 scopus 로고    scopus 로고
    • Costameres, focal adhesions, and cardiomyocyte mechanotransduction
    • Samarel A.M. Costameres, focal adhesions, and cardiomyocyte mechanotransduction. Am J Physiol Heart Circ Physiol 289 (2005) H2291-2301
    • (2005) Am J Physiol Heart Circ Physiol , vol.289
    • Samarel, A.M.1
  • 32
    • 1642263252 scopus 로고    scopus 로고
    • Restoration of resting sarcomere length after uniaxial static strain is regulated by protein kinase Cepsilon and focal adhesion kinase
    • Mansour H., de Tombe P.P., Samarel A.M., and Russell B. Restoration of resting sarcomere length after uniaxial static strain is regulated by protein kinase Cepsilon and focal adhesion kinase. Circ Res 94 (2004) 642-649
    • (2004) Circ Res , vol.94 , pp. 642-649
    • Mansour, H.1    de Tombe, P.P.2    Samarel, A.M.3    Russell, B.4
  • 33
    • 0026739841 scopus 로고
    • Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes
    • Danowski B.A., Imanaka-Yoshida K., Sanger J.M., and Sanger J.W. Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes. J Cell Biol 118 (1992) 1411-1420
    • (1992) J Cell Biol , vol.118 , pp. 1411-1420
    • Danowski, B.A.1    Imanaka-Yoshida, K.2    Sanger, J.M.3    Sanger, J.W.4
  • 34
    • 0034724943 scopus 로고    scopus 로고
    • Increased expression of cytoskeletal, linkage, and extracellular proteins in failing human myocardium
    • Heling A., Zimmermann R., Kostin S., et al. Increased expression of cytoskeletal, linkage, and extracellular proteins in failing human myocardium. Circ Res 86 (2000) 846-853
    • (2000) Circ Res , vol.86 , pp. 846-853
    • Heling, A.1    Zimmermann, R.2    Kostin, S.3
  • 35
    • 0034267888 scopus 로고    scopus 로고
    • Genetic abnormalities responsible for dilated cardiomyopathy
    • Towbin J.A., and Bowles N.E. Genetic abnormalities responsible for dilated cardiomyopathy. Curr Cardiol Rep 2 (2000) 475-480
    • (2000) Curr Cardiol Rep , vol.2 , pp. 475-480
    • Towbin, J.A.1    Bowles, N.E.2
  • 36
    • 0037112402 scopus 로고    scopus 로고
    • Dance band on the Titanic: biomechanical signaling in cardiac hypertrophy
    • Sussman M.A., McCulloch A., and Borg T.K. Dance band on the Titanic: biomechanical signaling in cardiac hypertrophy. Circ Res 91 (2002) 888-898
    • (2002) Circ Res , vol.91 , pp. 888-898
    • Sussman, M.A.1    McCulloch, A.2    Borg, T.K.3
  • 37
    • 0037040839 scopus 로고    scopus 로고
    • Cardiac myocyte-specific excision of the beta1 integrin gene results in myocardial fibrosis and cardiac failure
    • Shai S.Y., Harpf A.E., Babbitt C.J., et al. Cardiac myocyte-specific excision of the beta1 integrin gene results in myocardial fibrosis and cardiac failure. Circ Res 90 (2002) 458-464
    • (2002) Circ Res , vol.90 , pp. 458-464
    • Shai, S.Y.1    Harpf, A.E.2    Babbitt, C.J.3
  • 39
    • 0035824920 scopus 로고    scopus 로고
    • Integrin and growth factor receptor crosstalk
    • Eliceiri B.P. Integrin and growth factor receptor crosstalk. Circ Res 89 (2001) 1104-1110
    • (2001) Circ Res , vol.89 , pp. 1104-1110
    • Eliceiri, B.P.1
  • 40
    • 0034730790 scopus 로고    scopus 로고
    • Early activation of the multicomponent signaling complex associated with focal adhesion kinase induced by pressure overload in the rat heart
    • Franchini K.G., Torsoni A.S., Soares P.H., and Saad M.J. Early activation of the multicomponent signaling complex associated with focal adhesion kinase induced by pressure overload in the rat heart. Circ Res 87 (2000) 558-565
    • (2000) Circ Res , vol.87 , pp. 558-565
    • Franchini, K.G.1    Torsoni, A.S.2    Soares, P.H.3    Saad, M.J.4
  • 41
    • 0034634653 scopus 로고    scopus 로고
    • Integrin activation and focal complex formation in cardiac hypertrophy
    • Laser M., Willey C.D., Jiang W., et al. Integrin activation and focal complex formation in cardiac hypertrophy. J Biol Chem 275 (2000) 35624-35630
    • (2000) J Biol Chem , vol.275 , pp. 35624-35630
    • Laser, M.1    Willey, C.D.2    Jiang, W.3
  • 42
    • 0033609354 scopus 로고    scopus 로고
    • Pulsatile stretch activates mitogen-activated protein kinase (MAPK) family members and focal adhesion kinase (p125(FAK)) in cultured rat cardiac myocytes
    • Seko Y., Takahashi N., Tobe K., Kadowaki T., and Yazaki Y. Pulsatile stretch activates mitogen-activated protein kinase (MAPK) family members and focal adhesion kinase (p125(FAK)) in cultured rat cardiac myocytes. Biochem Biophys Res Commun 259 (1999) 8-14
    • (1999) Biochem Biophys Res Commun , vol.259 , pp. 8-14
    • Seko, Y.1    Takahashi, N.2    Tobe, K.3    Kadowaki, T.4    Yazaki, Y.5
  • 43
    • 0036084426 scopus 로고    scopus 로고
    • Load-induced focal adhesion kinase activation in the myocardium: role of stretch and contractile activity
    • Domingos P.P., Fonseca P.M., Nadruz Jr. W., and Franchini K.G. Load-induced focal adhesion kinase activation in the myocardium: role of stretch and contractile activity. Am J Physiol Heart Circ Physiol 282 (2002) H556-564
    • (2002) Am J Physiol Heart Circ Physiol , vol.282
    • Domingos, P.P.1    Fonseca, P.M.2    Nadruz Jr., W.3    Franchini, K.G.4
  • 44
    • 0042266791 scopus 로고    scopus 로고
    • Focal adhesion kinase is activated and mediates the early hypertrophic response to stretch in cardiac myocytes
    • Torsoni A.S., Constancio S.S., Nadruz Jr. W., Hanks S.K., and Franchini K.G. Focal adhesion kinase is activated and mediates the early hypertrophic response to stretch in cardiac myocytes. Circ Res 93 (2003) 140-147
    • (2003) Circ Res , vol.93 , pp. 140-147
    • Torsoni, A.S.1    Constancio, S.S.2    Nadruz Jr., W.3    Hanks, S.K.4    Franchini, K.G.5
  • 45
    • 0032879692 scopus 로고    scopus 로고
    • Melusin is a new muscle-specific interactor for beta(1) integrin cytoplasmic domain
    • Brancaccio M., Guazzone S., Menini N., et al. Melusin is a new muscle-specific interactor for beta(1) integrin cytoplasmic domain. J Biol Chem 274 (1999) 29282-29288
    • (1999) J Biol Chem , vol.274 , pp. 29282-29288
    • Brancaccio, M.1    Guazzone, S.2    Menini, N.3
  • 46
    • 0037236642 scopus 로고    scopus 로고
    • Melusin, a muscle-specific integrin beta1-interacting protein, is required to prevent cardiac failure in response to chronic pressure overload
    • Brancaccio M., Fratta L., Notte A., et al. Melusin, a muscle-specific integrin beta1-interacting protein, is required to prevent cardiac failure in response to chronic pressure overload. Nat Med 9 (2003) 68-75
    • (2003) Nat Med , vol.9 , pp. 68-75
    • Brancaccio, M.1    Fratta, L.2    Notte, A.3
  • 47
    • 0030026679 scopus 로고    scopus 로고
    • Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase
    • Hannigan G.E., Leung-Hagesteijn C., Fitz-Gibbon L., et al. Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase. Nature 379 (1996) 91-96
    • (1996) Nature , vol.379 , pp. 91-96
    • Hannigan, G.E.1    Leung-Hagesteijn, C.2    Fitz-Gibbon, L.3
  • 48
    • 34249660635 scopus 로고    scopus 로고
    • Integrin-linked kinase at the heart of cardiac contractility, repair, and disease
    • Hannigan G.E., Coles J.G., and Dedhar S. Integrin-linked kinase at the heart of cardiac contractility, repair, and disease. Circ Res 100 (2007) 1408-1414
    • (2007) Circ Res , vol.100 , pp. 1408-1414
    • Hannigan, G.E.1    Coles, J.G.2    Dedhar, S.3
  • 49
    • 33748278519 scopus 로고    scopus 로고
    • Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure
    • White D.E., Coutu P., Shi Y.F., et al. Targeted ablation of ILK from the murine heart results in dilated cardiomyopathy and spontaneous heart failure. Genes Dev 20 (2006) 2355-2360
    • (2006) Genes Dev , vol.20 , pp. 2355-2360
    • White, D.E.1    Coutu, P.2    Shi, Y.F.3
  • 50
    • 0035126590 scopus 로고    scopus 로고
    • Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily
    • Olski T.M., Noegel A.A., and Korenbaum E. Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily. J Cell Sci 114 (2001) 525-538
    • (2001) J Cell Sci , vol.114 , pp. 525-538
    • Olski, T.M.1    Noegel, A.A.2    Korenbaum, E.3
  • 51
    • 33646559605 scopus 로고    scopus 로고
    • Myospryn is a direct transcriptional target for MEF2A that encodes a striated muscle, alpha-actinin-interacting, costamere-localized protein
    • Durham J.T., Brand O.M., Arnold M., et al. Myospryn is a direct transcriptional target for MEF2A that encodes a striated muscle, alpha-actinin-interacting, costamere-localized protein. J Biol Chem 281 (2006) 6841-6849
    • (2006) J Biol Chem , vol.281 , pp. 6841-6849
    • Durham, J.T.1    Brand, O.M.2    Arnold, M.3
  • 52
    • 3142581436 scopus 로고    scopus 로고
    • The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor
    • Samson T., Smyth N., Janetzky S., et al. The LIM-only proteins FHL2 and FHL3 interact with alpha- and beta-subunits of the muscle alpha7beta1 integrin receptor. J Biol Chem 279 (2004) 28641-28652
    • (2004) J Biol Chem , vol.279 , pp. 28641-28652
    • Samson, T.1    Smyth, N.2    Janetzky, S.3
  • 53
    • 0033592754 scopus 로고    scopus 로고
    • Signaling pathways for cardiac hypertrophy and failure
    • Hunter J.J., and Chien K.R. Signaling pathways for cardiac hypertrophy and failure. N Engl J Med 341 (1999) 1276-1283
    • (1999) N Engl J Med , vol.341 , pp. 1276-1283
    • Hunter, J.J.1    Chien, K.R.2
  • 54
    • 0036213057 scopus 로고    scopus 로고
    • Mixed signals in heart failure: cancer rules
    • Hoshijima M., and Chien K.R. Mixed signals in heart failure: cancer rules. J Clin Invest 109 (2002) 849-855
    • (2002) J Clin Invest , vol.109 , pp. 849-855
    • Hoshijima, M.1    Chien, K.R.2
  • 55
    • 0030753648 scopus 로고    scopus 로고
    • Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD
    • Kong Y., Flick M.J., Kudla A.J., and Konieczny S.F. Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD. Mol Cell Biol 17 (1997) 4750-4760
    • (1997) Mol Cell Biol , vol.17 , pp. 4750-4760
    • Kong, Y.1    Flick, M.J.2    Kudla, A.J.3    Konieczny, S.F.4
  • 56
    • 0034509337 scopus 로고    scopus 로고
    • Downregulation and nuclear relocation of MLP during the progression of right ventricular hypertrophy induced by chronic pressure overload
    • Ecarnot-Laubriet A., De Luca K., Vandroux D., et al. Downregulation and nuclear relocation of MLP during the progression of right ventricular hypertrophy induced by chronic pressure overload. J Mol Cell Cardiol 32 (2000) 2385-2395
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 2385-2395
    • Ecarnot-Laubriet, A.1    De Luca, K.2    Vandroux, D.3
  • 57
    • 33846218274 scopus 로고    scopus 로고
    • Cardiac dysfunction and heart failure are associated with abnormalities in the subcellular distribution and amounts of oligomeric muscle LIM protein
    • Boateng S.Y., Belin R.J., Geenen D.L., et al. Cardiac dysfunction and heart failure are associated with abnormalities in the subcellular distribution and amounts of oligomeric muscle LIM protein. Am J Physiol Heart Circ Physiol 292 1 (2007) H259-H269
    • (2007) Am J Physiol Heart Circ Physiol , vol.292 , Issue.1
    • Boateng, S.Y.1    Belin, R.J.2    Geenen, D.L.3
  • 58
    • 0033981108 scopus 로고    scopus 로고
    • Targeted inhibition of calcineurin prevents agonist-induced cardiomyocyte hypertrophy
    • Taigen T., De Windt L.J., Lim H.W., and Molkentin J.D. Targeted inhibition of calcineurin prevents agonist-induced cardiomyocyte hypertrophy. Proc Natl Acad Sci U S A 97 (2000) 1196-1201
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1196-1201
    • Taigen, T.1    De Windt, L.J.2    Lim, H.W.3    Molkentin, J.D.4
  • 59
    • 0035814747 scopus 로고    scopus 로고
    • Differential activation of signal transduction pathways in human hearts with hypertrophy versus advanced heart failure
    • Haq S., Choukroun G., Lim H., et al. Differential activation of signal transduction pathways in human hearts with hypertrophy versus advanced heart failure. Circulation 103 (2001) 670-677
    • (2001) Circulation , vol.103 , pp. 670-677
    • Haq, S.1    Choukroun, G.2    Lim, H.3
  • 60
    • 0027491776 scopus 로고
    • The T-cell transcription factor NFATp is a substrate for calcineurin and interacts with Fos and Jun
    • Jain J., McCaffrey P.G., Miner Z., et al. The T-cell transcription factor NFATp is a substrate for calcineurin and interacts with Fos and Jun. Nature 365 (1993) 352-355
    • (1993) Nature , vol.365 , pp. 352-355
    • Jain, J.1    McCaffrey, P.G.2    Miner, Z.3
  • 61
    • 0032540267 scopus 로고    scopus 로고
    • A calcineurin-dependent transcriptional pathway for cardiac hypertrophy
    • Molkentin J.D., Lu J.R., Antos C.L., et al. A calcineurin-dependent transcriptional pathway for cardiac hypertrophy. Cell 93 (1998) 215-228
    • (1998) Cell , vol.93 , pp. 215-228
    • Molkentin, J.D.1    Lu, J.R.2    Antos, C.L.3
  • 62
    • 3242772151 scopus 로고    scopus 로고
    • Calcineurin-NFAT signaling regulates the cardiac hypertrophic response in coordination with the MAPKs
    • Molkentin J.D. Calcineurin-NFAT signaling regulates the cardiac hypertrophic response in coordination with the MAPKs. Cardiovasc Res 63 (2004) 467-475
    • (2004) Cardiovasc Res , vol.63 , pp. 467-475
    • Molkentin, J.D.1
  • 63
    • 33748323383 scopus 로고    scopus 로고
    • Regulation of cardiac hypertrophy by intracellular signalling pathways
    • Heineke J., and Molkentin J.D. Regulation of cardiac hypertrophy by intracellular signalling pathways. Nat Rev Mol Cell Biol 7 (2006) 589-600
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 589-600
    • Heineke, J.1    Molkentin, J.D.2
  • 64
    • 0035800083 scopus 로고    scopus 로고
    • Isoproterenol activates extracellular signal-regulated protein kinases in cardiomyocytes through calcineurin
    • Zou Y., Yao A., Zhu W., et al. Isoproterenol activates extracellular signal-regulated protein kinases in cardiomyocytes through calcineurin. Circulation 104 (2001) 102-108
    • (2001) Circulation , vol.104 , pp. 102-108
    • Zou, Y.1    Yao, A.2    Zhu, W.3
  • 65
    • 0035851920 scopus 로고    scopus 로고
    • Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein
    • Weins A., Schwarz K., Faul C., Barisoni L., Linke W.A., and Mundel P. Differentiation- and stress-dependent nuclear cytoplasmic redistribution of myopodin, a novel actin-bundling protein. J Cell Biol 155 (2001) 393-404
    • (2001) J Cell Biol , vol.155 , pp. 393-404
    • Weins, A.1    Schwarz, K.2    Faul, C.3    Barisoni, L.4    Linke, W.A.5    Mundel, P.6
  • 66
    • 0035897410 scopus 로고    scopus 로고
    • Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies
    • Bang M.L., Mudry R.E., McElhinny A.S., et al. Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies. J Cell Biol 153 (2001) 413-427
    • (2001) J Cell Biol , vol.153 , pp. 413-427
    • Bang, M.L.1    Mudry, R.E.2    McElhinny, A.S.3
  • 67
    • 0030931797 scopus 로고    scopus 로고
    • A novel cardiac-restricted target for doxorubicin. CARP, a nuclear modulator of gene expression in cardiac progenitor cells and cardiomyocytes
    • Jeyaseelan R., Poizat C., Baker R.K., et al. A novel cardiac-restricted target for doxorubicin. CARP, a nuclear modulator of gene expression in cardiac progenitor cells and cardiomyocytes. J Biol Chem 272 (1997) 22800-22808
    • (1997) J Biol Chem , vol.272 , pp. 22800-22808
    • Jeyaseelan, R.1    Poizat, C.2    Baker, R.K.3
  • 68
    • 0030967789 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus
    • Nix D.A., and Beckerle M.C. Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus. J Cell Biol 138 (1997) 1139-1147
    • (1997) J Cell Biol , vol.138 , pp. 1139-1147
    • Nix, D.A.1    Beckerle, M.C.2
  • 69
    • 0035860722 scopus 로고    scopus 로고
    • Targeting of zyxin to sites of actin membrane interaction and to the nucleus
    • Nix D.A., Fradelizi J., Bockholt S., et al. Targeting of zyxin to sites of actin membrane interaction and to the nucleus. J Biol Chem 276 (2001) 34759-34767
    • (2001) J Biol Chem , vol.276 , pp. 34759-34767
    • Nix, D.A.1    Fradelizi, J.2    Bockholt, S.3
  • 70
    • 0026586856 scopus 로고
    • An interaction between zyxin and alpha-actinin
    • Crawford A.W., Michelsen J.W., and Beckerle M.C. An interaction between zyxin and alpha-actinin. J Cell Biol 116 (1992) 1381-1393
    • (1992) J Cell Biol , vol.116 , pp. 1381-1393
    • Crawford, A.W.1    Michelsen, J.W.2    Beckerle, M.C.3
  • 71
    • 26444507242 scopus 로고    scopus 로고
    • Atrial natriuretic peptide promotes cardiomyocyte survival by cGMP-dependent nuclear accumulation of zyxin and Akt
    • Kato T., Muraski J., Chen Y., et al. Atrial natriuretic peptide promotes cardiomyocyte survival by cGMP-dependent nuclear accumulation of zyxin and Akt. J Clin Invest 115 (2005) 2716-2730
    • (2005) J Clin Invest , vol.115 , pp. 2716-2730
    • Kato, T.1    Muraski, J.2    Chen, Y.3
  • 72
    • 0036478897 scopus 로고    scopus 로고
    • Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy
    • Gerull B., Gramlich M., Atherton J., et al. Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy. Nat Genet 30 (2002) 201-204
    • (2002) Nat Genet , vol.30 , pp. 201-204
    • Gerull, B.1    Gramlich, M.2    Atherton, J.3
  • 73
    • 0033610050 scopus 로고    scopus 로고
    • Structural analysis of the titin gene in hypertrophic cardiomyopathy: identification of a novel disease gene
    • Satoh M., Takahashi M., Sakamoto T., Hiroe M., Marumo F., and Kimura A. Structural analysis of the titin gene in hypertrophic cardiomyopathy: identification of a novel disease gene. Biochem Biophys Res Commun 262 (1999) 411-417
    • (1999) Biochem Biophys Res Commun , vol.262 , pp. 411-417
    • Satoh, M.1    Takahashi, M.2    Sakamoto, T.3    Hiroe, M.4    Marumo, F.5    Kimura, A.6
  • 74
    • 0035707910 scopus 로고    scopus 로고
    • The muscular dystrophy with myositis (mdm) mouse mutation disrupts a skeletal muscle-specific domain of titin
    • Garvey S.M., Rajan C., Lerner A.P., Frankel W.N., and Cox G.A. The muscular dystrophy with myositis (mdm) mouse mutation disrupts a skeletal muscle-specific domain of titin. Genomics 79 (2002) 146-149
    • (2002) Genomics , vol.79 , pp. 146-149
    • Garvey, S.M.1    Rajan, C.2    Lerner, A.P.3    Frankel, W.N.4    Cox, G.A.5
  • 75
    • 2342596403 scopus 로고    scopus 로고
    • A Titin mutation defines roles for circulation in endothelial morphogenesis
    • May S.R., Stewart N.J., Chang W., and Peterson A.S. A Titin mutation defines roles for circulation in endothelial morphogenesis. Dev Biol 270 (2004) 31-46
    • (2004) Dev Biol , vol.270 , pp. 31-46
    • May, S.R.1    Stewart, N.J.2    Chang, W.3    Peterson, A.S.4
  • 76
    • 33646798022 scopus 로고    scopus 로고
    • M line-deficient titin causes cardiac lethality through impaired maturation of the sarcomere
    • Weinert S., Bergmann N., Luo X., Erdmann B., and Gotthardt M. M line-deficient titin causes cardiac lethality through impaired maturation of the sarcomere. J Cell Biol 173 (2006) 559-570
    • (2006) J Cell Biol , vol.173 , pp. 559-570
    • Weinert, S.1    Bergmann, N.2    Luo, X.3    Erdmann, B.4    Gotthardt, M.5
  • 77
    • 0037458739 scopus 로고    scopus 로고
    • Conditional expression of mutant M-line titins results in cardiomyopathy with altered sarcomere structure
    • Gotthardt M., Hammer R.E., Hubner N., et al. Conditional expression of mutant M-line titins results in cardiomyopathy with altered sarcomere structure. J Biol Chem 278 (2003) 6059-6065
    • (2003) J Biol Chem , vol.278 , pp. 6059-6065
    • Gotthardt, M.1    Hammer, R.E.2    Hubner, N.3
  • 78
    • 33847653726 scopus 로고    scopus 로고
    • Targeted deletion of titin N2B region leads to diastolic dysfunction and cardiac atrophy
    • Radke M.H., Peng J., Wu Y., et al. Targeted deletion of titin N2B region leads to diastolic dysfunction and cardiac atrophy. Proc Natl Acad Sci U S A 104 (2007) 3444-3449
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 3444-3449
    • Radke, M.H.1    Peng, J.2    Wu, Y.3
  • 79
    • 0037184992 scopus 로고    scopus 로고
    • The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy
    • Knoll R., Hoshijima M., Hoffman H.M., et al. The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy. Cell 111 (2002) 943-955
    • (2002) Cell , vol.111 , pp. 943-955
    • Knoll, R.1    Hoshijima, M.2    Hoffman, H.M.3
  • 80
    • 0030933063 scopus 로고    scopus 로고
    • MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure
    • Arber S., Hunter J.J., Ross Jr. J., et al. MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure. Cell 88 (1997) 393-403
    • (1997) Cell , vol.88 , pp. 393-403
    • Arber, S.1    Hunter, J.J.2    Ross Jr., J.3
  • 81
    • 0142058043 scopus 로고    scopus 로고
    • Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis
    • Mohapatra B., Jimenez S., Lin J.H., et al. Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis. Mol Genet Metab 80 (2003) 207-215
    • (2003) Mol Genet Metab , vol.80 , pp. 207-215
    • Mohapatra, B.1    Jimenez, S.2    Lin, J.H.3
  • 82
    • 0035853110 scopus 로고    scopus 로고
    • Myocyte-enriched calcineurin-interacting protein, MCIP1, inhibits cardiac hypertrophy in vivo
    • Rothermel B.A., McKinsey T.A., Vega R.B., et al. Myocyte-enriched calcineurin-interacting protein, MCIP1, inhibits cardiac hypertrophy in vivo. Proc Natl Acad Sci U S A 98 (2001) 3328-3333
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 3328-3333
    • Rothermel, B.A.1    McKinsey, T.A.2    Vega, R.B.3
  • 83
    • 19944423058 scopus 로고    scopus 로고
    • Mice lacking calsarcin-1 are sensitized to calcineurin signaling and show accelerated cardiomyopathy in response to pathological biomechanical stress
    • Frey N., Barrientos T., Shelton J.M., et al. Mice lacking calsarcin-1 are sensitized to calcineurin signaling and show accelerated cardiomyopathy in response to pathological biomechanical stress. Nat Med 10 (2004) 1336-1343
    • (2004) Nat Med , vol.10 , pp. 1336-1343
    • Frey, N.1    Barrientos, T.2    Shelton, J.M.3
  • 84
    • 13344280343 scopus 로고    scopus 로고
    • T cell responses in calcineurin A alpha-deficient mice
    • Zhang B.W., Zimmer G., Chen J., et al. T cell responses in calcineurin A alpha-deficient mice. J Exp Med 183 (1996) 413-420
    • (1996) J Exp Med , vol.183 , pp. 413-420
    • Zhang, B.W.1    Zimmer, G.2    Chen, J.3
  • 85
    • 0037007016 scopus 로고    scopus 로고
    • Impaired cardiac hypertrophic response in Calcineurin Abeta -deficient mice
    • Bueno O.F., Wilkins B.J., Tymitz K.M., et al. Impaired cardiac hypertrophic response in Calcineurin Abeta -deficient mice. Proc Natl Acad Sci U S A 99 (2002) 4586-4591
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 4586-4591
    • Bueno, O.F.1    Wilkins, B.J.2    Tymitz, K.M.3
  • 86
    • 0037188943 scopus 로고    scopus 로고
    • Actin capping protein: an essential element in protein kinase signaling to the myofilaments
    • Pyle W.G., Hart M.C., Cooper J.A., Sumandea M.P., de Tombe P.P., and Solaro R.J. Actin capping protein: an essential element in protein kinase signaling to the myofilaments. Circ Res 90 (2002) 1299-1306
    • (2002) Circ Res , vol.90 , pp. 1299-1306
    • Pyle, W.G.1    Hart, M.C.2    Cooper, J.A.3    Sumandea, M.P.4    de Tombe, P.P.5    Solaro, R.J.6
  • 87
    • 33748434072 scopus 로고    scopus 로고
    • Control of cardiac myofilament activation and PKC-betaII signaling through the actin capping protein, CapZ
    • Pyle W.G., La Rotta G., de Tombe P.P., Sumandea M.P., and Solaro R.J. Control of cardiac myofilament activation and PKC-betaII signaling through the actin capping protein, CapZ. J Mol Cell Cardiol 41 (2006) 537-543
    • (2006) J Mol Cell Cardiol , vol.41 , pp. 537-543
    • Pyle, W.G.1    La Rotta, G.2    de Tombe, P.P.3    Sumandea, M.P.4    Solaro, R.J.5
  • 88
    • 0035134806 scopus 로고    scopus 로고
    • Actinin-associated LIM protein-deficient mice maintain normal development and structure of skeletal muscle
    • Jo K., Rutten B., Bunn R.C., and Bredt D.S. Actinin-associated LIM protein-deficient mice maintain normal development and structure of skeletal muscle. Mol Cell Biol 21 (2001) 1682-1687
    • (2001) Mol Cell Biol , vol.21 , pp. 1682-1687
    • Jo, K.1    Rutten, B.2    Bunn, R.C.3    Bredt, D.S.4
  • 89
    • 0035033212 scopus 로고    scopus 로고
    • Adult mice deficient in actinin-associated LIM-domain protein reveal a developmental pathway for right ventricular cardiomyopathy
    • Pashmforoush M., Pomies P., Peterson K.L., et al. Adult mice deficient in actinin-associated LIM-domain protein reveal a developmental pathway for right ventricular cardiomyopathy. Nat Med 7 (2001) 591-597
    • (2001) Nat Med , vol.7 , pp. 591-597
    • Pashmforoush, M.1    Pomies, P.2    Peterson, K.L.3
  • 90
    • 84924110084 scopus 로고    scopus 로고
    • Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy
    • Zhou Q., Chu P.H., Huang C., et al. Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy. J Cell Biol 155 (2001) 605-612
    • (2001) J Cell Biol , vol.155 , pp. 605-612
    • Zhou, Q.1    Chu, P.H.2    Huang, C.3
  • 91
    • 13144260646 scopus 로고    scopus 로고
    • Mutations in ZASP define a novel form of muscular dystrophy in humans
    • Selcen D., and Engel A.G. Mutations in ZASP define a novel form of muscular dystrophy in humans. Ann Neurol 57 (2005) 269-276
    • (2005) Ann Neurol , vol.57 , pp. 269-276
    • Selcen, D.1    Engel, A.G.2
  • 92
    • 0028979153 scopus 로고
    • Deletion of beta 1 integrins in mice results in inner cell mass failure and peri-implantation lethality
    • Stephens L.E., Sutherland A.E., Klimanskaya I.V., et al. Deletion of beta 1 integrins in mice results in inner cell mass failure and peri-implantation lethality. Genes Dev 9 (1995) 1883-1895
    • (1995) Genes Dev , vol.9 , pp. 1883-1895
    • Stephens, L.E.1    Sutherland, A.E.2    Klimanskaya, I.V.3
  • 93
    • 0345103747 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation
    • Sakai T., Li S., Docheva D., et al. Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation. Genes Dev 17 (2003) 926-940
    • (2003) Genes Dev , vol.17 , pp. 926-940
    • Sakai, T.1    Li, S.2    Docheva, D.3
  • 94
    • 0033667594 scopus 로고    scopus 로고
    • Disruption of the talin gene arrests mouse development at the gastrulation stage
    • Monkley S.J., Zhou X.H., Kinston S.J., et al. Disruption of the talin gene arrests mouse development at the gastrulation stage. Dev Dyn 219 (2000) 560-574
    • (2000) Dev Dyn , vol.219 , pp. 560-574
    • Monkley, S.J.1    Zhou, X.H.2    Kinston, S.J.3
  • 95
    • 31044436891 scopus 로고    scopus 로고
    • Inactivation of focal adhesion kinase in cardiomyocytes promotes eccentric cardiac hypertrophy and fibrosis in mice
    • Peng X., Kraus M.S., Wei H., et al. Inactivation of focal adhesion kinase in cardiomyocytes promotes eccentric cardiac hypertrophy and fibrosis in mice. J Clin Invest 116 (2006) 217-227
    • (2006) J Clin Invest , vol.116 , pp. 217-227
    • Peng, X.1    Kraus, M.S.2    Wei, H.3
  • 96
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • Xu W., Baribault H., and Adamson E.D. Vinculin knockout results in heart and brain defects during embryonic development. Development 125 (1998) 327-337
    • (1998) Development , vol.125 , pp. 327-337
    • Xu, W.1    Baribault, H.2    Adamson, E.D.3
  • 97
    • 4344568148 scopus 로고    scopus 로고
    • Heterozygous inactivation of the vinculin gene predisposes to stress-induced cardiomyopathy
    • Zemljic-Harpf A.E., Ponrartana S., Avalos R.T., et al. Heterozygous inactivation of the vinculin gene predisposes to stress-induced cardiomyopathy. Am J Pathol 165 (2004) 1033-1044
    • (2004) Am J Pathol , vol.165 , pp. 1033-1044
    • Zemljic-Harpf, A.E.1    Ponrartana, S.2    Avalos, R.T.3
  • 98
    • 33747753150 scopus 로고    scopus 로고
    • Loss of FilaminC (FLNc) results in severe defects in myogenesis and myotube structure
    • Dalkilic I., Schienda J., Thompson T.G., and Kunkel L.M. Loss of FilaminC (FLNc) results in severe defects in myogenesis and myotube structure. Mol Cell Biol 26 (2006) 6522-6534
    • (2006) Mol Cell Biol , vol.26 , pp. 6522-6534
    • Dalkilic, I.1    Schienda, J.2    Thompson, T.G.3    Kunkel, L.M.4
  • 99
    • 22544478749 scopus 로고    scopus 로고
    • A mutation in the dimerization domain of filamin c causes a novel type of autosomal dominant myofibrillar myopathy
    • Vorgerd M., van der Ven P.F., Bruchertseifer V., et al. A mutation in the dimerization domain of filamin c causes a novel type of autosomal dominant myofibrillar myopathy. Am J Hum Genet 77 (2005) 297-304
    • (2005) Am J Hum Genet , vol.77 , pp. 297-304
    • Vorgerd, M.1    van der Ven, P.F.2    Bruchertseifer, V.3
  • 100
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine S.C., Latres E., Baumhueter S., et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294 (2001) 1704-1708
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3
  • 101
    • 34248371018 scopus 로고    scopus 로고
    • Loss of muscle-specific RING-finger 3 predisposes the heart to cardiac rupture after myocardial infarction
    • Fielitz J., van Rooij E., Spencer J.A., et al. Loss of muscle-specific RING-finger 3 predisposes the heart to cardiac rupture after myocardial infarction. Proc Natl Acad Sci U S A 104 (2007) 4377-4382
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 4377-4382
    • Fielitz, J.1    van Rooij, E.2    Spencer, J.A.3
  • 102
    • 33644818634 scopus 로고    scopus 로고
    • Effects of mechanosensitive ion channels on ventricular electrophysiology: experimental and theoretical models
    • Kohl P., Bollensdorff C., and Garny A. Effects of mechanosensitive ion channels on ventricular electrophysiology: experimental and theoretical models. Exp Physiol 91 (2006) 307-321
    • (2006) Exp Physiol , vol.91 , pp. 307-321
    • Kohl, P.1    Bollensdorff, C.2    Garny, A.3
  • 103
    • 0034123657 scopus 로고    scopus 로고
    • Mechanical stress-induced cardiac hypertrophy: mechanisms and signal transduction pathways
    • Ruwhof C., and van der Laarse A. Mechanical stress-induced cardiac hypertrophy: mechanisms and signal transduction pathways. Cardiovasc Res 47 (2000) 23-37
    • (2000) Cardiovasc Res , vol.47 , pp. 23-37
    • Ruwhof, C.1    van der Laarse, A.2
  • 104
    • 14344283370 scopus 로고    scopus 로고
    • Mouse model of desmin-related cardiomyopathy
    • Wang X., Osinska H., Dorn II G.W., et al. Mouse model of desmin-related cardiomyopathy. Circulation 103 (2001) 2402-2407
    • (2001) Circulation , vol.103 , pp. 2402-2407
    • Wang, X.1    Osinska, H.2    Dorn II, G.W.3
  • 105
    • 0036779359 scopus 로고    scopus 로고
    • Titin-cap associates with, and regulates secretion of, Myostatin
    • Nicholas G., Thomas M., Langley B., et al. Titin-cap associates with, and regulates secretion of, Myostatin. J Cell Physiol 193 (2002) 120-131
    • (2002) J Cell Physiol , vol.193 , pp. 120-131
    • Nicholas, G.1    Thomas, M.2    Langley, B.3
  • 106
    • 0031001970 scopus 로고    scopus 로고
    • Rescue of cardiac alpha-actin-deficient mice by enteric smooth muscle gamma-actin
    • Kumar A., Crawford K., Close L., et al. Rescue of cardiac alpha-actin-deficient mice by enteric smooth muscle gamma-actin. Proc Natl Acad Sci U S A 94 (1997) 4406-4411
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 4406-4411
    • Kumar, A.1    Crawford, K.2    Close, L.3
  • 107
    • 2042462926 scopus 로고    scopus 로고
    • BMP10 is essential for maintaining cardiac growth during murine cardiogenesis
    • Chen H., Shi S., Acosta L., et al. BMP10 is essential for maintaining cardiac growth during murine cardiogenesis. Development 131 (2004) 2219-2231
    • (2004) Development , vol.131 , pp. 2219-2231
    • Chen, H.1    Shi, S.2    Acosta, L.3
  • 108
    • 33748749375 scopus 로고    scopus 로고
    • Overexpression of bone morphogenetic protein 10 in myocardium disrupts cardiac postnatal hypertrophic growth
    • Chen H., Yong W., Ren S., et al. Overexpression of bone morphogenetic protein 10 in myocardium disrupts cardiac postnatal hypertrophic growth. J Biol Chem 281 37 (2006) 27481-27491
    • (2006) J Biol Chem , vol.281 , Issue.37 , pp. 27481-27491
    • Chen, H.1    Yong, W.2    Ren, S.3
  • 109
    • 0037470052 scopus 로고    scopus 로고
    • Characterization and in vivo functional analysis of splice variants of cypher
    • Huang C., Zhou Q., Liang P., et al. Characterization and in vivo functional analysis of splice variants of cypher. J Biol Chem 278 (2003) 7360-7365
    • (2003) J Biol Chem , vol.278 , pp. 7360-7365
    • Huang, C.1    Zhou, Q.2    Liang, P.3
  • 110
    • 0029120440 scopus 로고
    • Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
    • Ilic D., Furuta Y., Kanazawa S., et al. Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 377 (1995) 539-544
    • (1995) Nature , vol.377 , pp. 539-544
    • Ilic, D.1    Furuta, Y.2    Kanazawa, S.3
  • 111
    • 0035811023 scopus 로고    scopus 로고
    • Cardiac-specific LIM protein FHL2 modifies the hypertrophic response to beta-adrenergic stimulation
    • Kong Y., Shelton J.M., Rothermel B., et al. Cardiac-specific LIM protein FHL2 modifies the hypertrophic response to beta-adrenergic stimulation. Circulation 103 (2001) 2731-2738
    • (2001) Circulation , vol.103 , pp. 2731-2738
    • Kong, Y.1    Shelton, J.M.2    Rothermel, B.3
  • 112
    • 0033805096 scopus 로고    scopus 로고
    • FHL2 (SLIM3) is not essential for cardiac development and function
    • Chu P.H., Bardwell W.M., Gu Y., Ross Jr. J., and Chen J. FHL2 (SLIM3) is not essential for cardiac development and function. Mol Cell Biol 20 (2000) 7460-7462
    • (2000) Mol Cell Biol , vol.20 , pp. 7460-7462
    • Chu, P.H.1    Bardwell, W.M.2    Gu, Y.3    Ross Jr., J.4    Chen, J.5
  • 113
    • 33845801599 scopus 로고    scopus 로고
    • Targeted deletion of the muscular dystrophy gene myotilin does not perturb muscle structure or function in mice
    • Moza M., Mologni L., Trokovic R., Faulkner G., Partanen J., and Carpen O. Targeted deletion of the muscular dystrophy gene myotilin does not perturb muscle structure or function in mice. Mol Cell Biol 27 (2007) 244-252
    • (2007) Mol Cell Biol , vol.27 , pp. 244-252
    • Moza, M.1    Mologni, L.2    Trokovic, R.3    Faulkner, G.4    Partanen, J.5    Carpen, O.6
  • 114
    • 0036142219 scopus 로고    scopus 로고
    • The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling
    • Hagel M., George E.L., Kim A., et al. The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling. Mol Cell Biol 22 (2002) 901-915
    • (2002) Mol Cell Biol , vol.22 , pp. 901-915
    • Hagel, M.1    George, E.L.2    Kim, A.3
  • 115
    • 0034746792 scopus 로고    scopus 로고
    • Protein kinase Cepsilon is required for macrophage activation and defense against bacterial infection
    • Castrillo A., Pennington D.J., Otto F., Parker P.J., Owen M.J., and Bosca L. Protein kinase Cepsilon is required for macrophage activation and defense against bacterial infection. J Exp Med 194 (2001) 1231-1242
    • (2001) J Exp Med , vol.194 , pp. 1231-1242
    • Castrillo, A.1    Pennington, D.J.2    Otto, F.3    Parker, P.J.4    Owen, M.J.5    Bosca, L.6
  • 116
    • 0036023643 scopus 로고    scopus 로고
    • Targeted disruption of the protein kinase C epsilon gene abolishes the infarct size reduction that follows ischaemic preconditioning of isolated buffer-perfused mouse hearts
    • Saurin A.T., Pennington D.J., Raat N.J., Latchman D.S., Owen M.J., and Marber M.S. Targeted disruption of the protein kinase C epsilon gene abolishes the infarct size reduction that follows ischaemic preconditioning of isolated buffer-perfused mouse hearts. Cardiovasc Res 55 (2002) 672-680
    • (2002) Cardiovasc Res , vol.55 , pp. 672-680
    • Saurin, A.T.1    Pennington, D.J.2    Raat, N.J.3    Latchman, D.S.4    Owen, M.J.5    Marber, M.S.6
  • 117
    • 0036193622 scopus 로고    scopus 로고
    • Impaired cardiac contractility response to hemodynamic stress in S100A1-deficient mice
    • Du X.J., Cole T.J., Tenis N., et al. Impaired cardiac contractility response to hemodynamic stress in S100A1-deficient mice. Mol Cell Biol 22 (2002) 2821-2829
    • (2002) Mol Cell Biol , vol.22 , pp. 2821-2829
    • Du, X.J.1    Cole, T.J.2    Tenis, N.3
  • 118
    • 0037215407 scopus 로고    scopus 로고
    • Targeted disruption of the murine zyxin gene
    • Hoffman L.M., Nix D.A., Benson B., et al. Targeted disruption of the murine zyxin gene. Mol Cell Biol 23 (2003) 70-79
    • (2003) Mol Cell Biol , vol.23 , pp. 70-79
    • Hoffman, L.M.1    Nix, D.A.2    Benson, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.