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Volumn 22, Issue 1, 1997, Pages 139-146

Molecular mechanisms of myofibril assembly in heart

Author keywords

Confocal microscopy; Epitope tagging; Green fluorescent protein; M band; Myomesin; Thick filament assembly

Indexed keywords

GREEN FLUORESCENT PROTEIN; MESSENGER RNA; MYOMESIN; MYOSIN LIGHT CHAIN;

EID: 0030905646     PISSN: 03867196     EISSN: None     Source Type: Journal    
DOI: 10.1247/csf.22.139     Document Type: Conference Paper
Times cited : (34)

References (27)
  • 2
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • CHALFIE, M., TU, Y., EUSKIRCHEN, G., WARD, W.W., and PRASHER, D.C. 1994. Green fluorescent protein as a marker for gene expression. Science, 263: 802-805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 3
    • 0021749672 scopus 로고
    • The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes
    • DLUGOSZ, A.A., ANTIN, P.B., NACHMIAS, V.T., and HOLTZER, H. 1984. The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes. J. Cell Biol., 99: 2268-2278.
    • (1984) J. Cell Biol. , vol.99 , pp. 2268-2278
    • Dlugosz, A.A.1    Antin, P.B.2    Nachmias, V.T.3    Holtzer, H.4
  • 4
    • 0019395642 scopus 로고
    • The Mr 165,000 M-protein myomesin: A specific protein of coss-striated muscle
    • EPPENBERGER, H.M., PERRIARD, J.-C., ROSENBERG, U.B., and STREHLER, E.E. 1981. The Mr 165,000 M-protein myomesin: A specific protein of coss-striated muscle. J. Cell Biol., 89: 185-193.
    • (1981) J. Cell Biol. , vol.89 , pp. 185-193
    • Eppenberger, H.M.1    Perriard, J.-C.2    Rosenberg, U.B.3    Strehler, E.E.4
  • 5
    • 0027246620 scopus 로고
    • Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts
    • GAUTEL, M., LEONARD, K., and LABEIT, S. 1993. Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts. EMBO-J., 12: 3827-3834.
    • (1993) EMBO-J. , vol.12 , pp. 3827-3834
    • Gautel, M.1    Leonard, K.2    Labeit, S.3
  • 6
    • 0030030825 scopus 로고    scopus 로고
    • The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle
    • GILBERT, R., KELLY, M.G., MIKAWA, T., and FISCHMAM, D.A. 1996. The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle. J. Cell Sci., 109: 101-111.
    • (1996) J. Cell Sci. , vol.109 , pp. 101-111
    • Gilbert, R.1    Kelly, M.G.2    Mikawa, T.3    Fischmam, D.A.4
  • 7
    • 0022344532 scopus 로고
    • Myomesin and M-protein: Expression of two M-band proteins in pectoral muscle and heart during development
    • GROVE, B., GROVE, B.K., CERNY, L., PERRIARD, J.-C., and EPPENBERGER, H.M. 1985. Myomesin and M-protein: Expression of two M-band proteins in pectoral muscle and heart during development. J. Cell Biol., 101: 1413-1421.
    • (1985) J. Cell Biol. , vol.101 , pp. 1413-1421
    • Grove, B.1    Grove, B.K.2    Cerny, L.3    Perriard, J.-C.4    Eppenberger, H.M.5
  • 10
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion molecules surface receptors belong to a new structural set which is close to that containing variable domains
    • HARPAZ, Y. and CHOTHIA, C. 1994. Many of the immunoglobulin superfamily domains in cell adhesion molecules surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol., 238: 528-539.
    • (1994) J. Mol. Biol. , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 11
    • 0029919189 scopus 로고    scopus 로고
    • Genomic organization of M line titin and its tissue-specific expression in two distinct isoforms
    • KOLMERER, B., OLIVIERI, N., WITT, C.C., HERRMANN, B.G., and LABEIT, S. 1996. Genomic organization of M line titin and its tissue-specific expression in two distinct isoforms. J. Mol. Biol., 256: 556-563.
    • (1996) J. Mol. Biol. , vol.256 , pp. 556-563
    • Kolmerer, B.1    Olivieri, N.2    Witt, C.C.3    Herrmann, B.G.4    Labeit, S.5
  • 12
    • 0029837673 scopus 로고    scopus 로고
    • The intracompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of developmental expression as determined by double epitope-tagging competition
    • KOMIYAMA, M., SOLDATI, T., VON ARX, P., and PERRIARD, J.-C. 1996. The intracompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of developmental expression as determined by double epitope-tagging competition. J. Cell Sci., 109: 2689-2099.
    • (1996) J. Cell Sci. , vol.109 , pp. 2689-12099
    • Komiyama, M.1    Soldati, T.2    Von Arx, P.3    Perriard, J.-C.4
  • 13
    • 0029155974 scopus 로고
    • Equilibration exchange of fluorescently labelled molecules in skinned skeletal muscle fibers observed by confocal microscopy
    • KRAFT, T., MESSERLI, M., RUTISHAUSER, B., PERRIARD, J.-C., WALLIMANN, T., and BRENNER, B. 1995. Equilibration exchange of fluorescently labelled molecules in skinned skeletal muscle fibers observed by confocal microscopy. Biophysical J., 69: 1246-1258.
    • (1995) Biophysical J. , vol.69 , pp. 1246-1258
    • Kraft, T.1    Messerli, M.2    Rutishauser, B.3    Perriard, J.-C.4    Wallimann, T.5    Brenner, B.6
  • 14
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • LABEIT, S. and KOLMERER, B. 1995. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science, 270: 236.
    • (1995) Science , vol.270 , pp. 236
    • Labeit, S.1    Kolmerer, B.2
  • 15
    • 0028101984 scopus 로고
    • Sequential appearance of muscle-specific proteins in myoblasts as a function of time after cell division: Evidence for a conserved myoblast differentiation program in skeletal muscle
    • LIN, Z.X., LU, M.H., SCHULTHEISS, T., CHOI, J., HOLTZER, S., DILULLO, C., FISCHMAN, D.A., and HOLTZER, H. 1994. Sequential appearance of muscle-specific proteins in myoblasts as a function of time after cell division: Evidence for a conserved myoblast differentiation program in skeletal muscle. Cell Motil Cytoskeleton, 29: 1-19.
    • (1994) Cell Motil Cytoskeleton , vol.29 , pp. 1-19
    • Lin, Z.X.1    Lu, M.H.2    Schultheiss, T.3    Choi, J.4    Holtzer, S.5    Dilullo, C.6    Fischman, D.A.7    Holtzer, H.8
  • 17
    • 0024440423 scopus 로고
    • Visualization of the polarity of isolated titin molecules: A sinle globular head on a long thin rod as the M-band anchoring domain?
    • NAVE, R., FÜRST, D.O., and WEBER, K. 1989. Visualization of the polarity of isolated titin molecules: A sinle globular head on a long thin rod as the M-band anchoring domain? J. Cell Biol., 109: 2177-2187.
    • (1989) J. Cell Biol. , vol.109 , pp. 2177-2187
    • Nave, R.1    Fürst, D.O.2    Weber, K.3
  • 18
    • 0029836627 scopus 로고    scopus 로고
    • The structure of the sarcomeric M band: Localization of defined domains of myomesin, M-protein the 250-kD carboxy-terminal region of titin by immunoelectron microscopy
    • OBERMANN, W.M.J., GAUTEL, M., STEINER, F., VAN DER VEEN, P.F.M., WEBER, K., and FÜRST, D.O. 1996. The structure of the sarcomeric M band: Localization of defined domains of myomesin, M-protein the 250-kD carboxy-terminal region of titin by immunoelectron microscopy. J. Cell Biol., 134: 1441-1453.
    • (1996) J. Cell Biol. , vol.134 , pp. 1441-1453
    • Obermann, W.M.J.1    Gautel, M.2    Steiner, F.3    Van Der Veen, P.F.M.4    Weber, K.5    Fürst, D.O.6
  • 19
    • 0027515217 scopus 로고
    • The major myosin-binding domain of skeletal muscle MyBP-C (C-protein) resides in the COOH-terminal, Immunoglobulin C2 Motif
    • OKAGAKI, T., WEBER, F.E., FISCHMAM, D.A., VAUGHAN, K.T., MIKAWA, T., and REINACH, F.C. 1993. The major myosin-binding domain of skeletal muscle MyBP-C (C-protein) resides in the COOH-terminal, Immunoglobulin C2 Motif. J. Cell Biol., 123: 619-626.
    • (1993) J. Cell Biol. , vol.123 , pp. 619-626
    • Okagaki, T.1    Weber, F.E.2    Fischmam, D.A.3    Vaughan, K.T.4    Mikawa, T.5    Reinach, F.C.6
  • 20
    • 0029644479 scopus 로고
    • Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: A new member of the I set
    • PFUHL, M. and PASTORE, A. 1995. Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: A new member of the I set. Structure, 3: 391-401.
    • (1995) Structure , vol.3 , pp. 391-401
    • Pfuhl, M.1    Pastore, A.2
  • 21
    • 0027493032 scopus 로고
    • Skelemin, a cytoskeletal M-disc periphery protein, contains motifs of adhesion/recognition and intermediate filament proteins
    • PRICE, M.G. and GOMER, R.H. 1993. Skelemin, a cytoskeletal M-disc periphery protein, contains motifs of adhesion/recognition and intermediate filament proteins. J. Biol. Chem., 268: 21800-21810.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21800-21810
    • Price, M.G.1    Gomer, R.H.2
  • 22
    • 0024232653 scopus 로고
    • Terminally differentiated neonatal rat myocardial cells proliferate and maintain specific differentiated fuctions following expression of SV 40 large T antigen
    • SEN, A., PRESTON, D., HENDERSON, S.A., GERARD, R.D., and CHIEN, K.R. 1988. Terminally differentiated neonatal rat myocardial cells proliferate and maintain specific differentiated fuctions following expression of SV 40 large T antigen. J. Biol. Chem., 35: 19132-19136.
    • (1988) J. Biol. Chem. , vol.35 , pp. 19132-19136
    • Sen, A.1    Preston, D.2    Henderson, S.A.3    Gerard, R.D.4    Chien, K.R.5
  • 23
    • 0026550870 scopus 로고
    • 3-D observation of actin filaments during cardiac myofibrinogenesis in chick embryo using a confocal laser scanning microscope
    • SHIRAISHI, I., TAKAMATSU, T., MINAMIKAWA, T., and FUJITA, S. 1992. 3-D observation of actin filaments during cardiac myofibrinogenesis in chick embryo using a confocal laser scanning microscope. Anat. Embryol., 185: 401-408.
    • (1992) Anat. Embryol. , vol.185 , pp. 401-408
    • Shiraishi, I.1    Takamatsu, T.2    Minamikawa, T.3    Fujita, S.4
  • 24
    • 0025917462 scopus 로고
    • Intracompartimental Sorting of Essential Myosin Light Chains: Molecular Dissection in vivo Monitoring by Epitope Tagging
    • SOLDATI, T. and PERRIARD, J.-C. 1991. Intracompartimental Sorting of Essential Myosin Light Chains: Molecular Dissection in vivo Monitoring by Epitope Tagging. Cell, 66: 277-289.
    • (1991) Cell , vol.66 , pp. 277-289
    • Soldati, T.1    Perriard, J.-C.2
  • 25
    • 0027407773 scopus 로고
    • Molecular cloning of chicken myosin-binding protein (MyBP) H (86K protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs
    • VAUGHAN, K.T., WEBER, F.E., EINHEBER, S., and FISCHMANN, D.A. 1993. Molecular cloning of chicken myosin-binding protein (MyBP) H (86K protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs. J. Biol. Chem., 268: 3670-3676.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3670-3676
    • Vaughan, K.T.1    Weber, F.E.2    Einheber, S.3    Fischmann, D.A.4
  • 26
    • 0027374159 scopus 로고
    • The globular of titin extends into the center of the sarcomeric M-band
    • VINKEMEIER, U., OBERMANN, W., WEBER, K., FÜRST, D.O. 1993. The globular of titin extends into the center of the sarcomeric M-band. J. Cell Sci., 106: 319-330.
    • (1993) J. Cell Sci. , vol.106 , pp. 319-330
    • Vinkemeier, U.1    Obermann, W.2    Weber, K.3    Fürst, D.O.4
  • 27
    • 0029615379 scopus 로고
    • Dominant Negative Effect of Cytoplasmic Actin Isoproteins on Cardiomyocyte Cytoarchitecture and Function
    • VON ARX, P., BANTLE, S., SOLDATI, T., PERRIARD, J.-C. 1995. Dominant Negative Effect of Cytoplasmic Actin Isoproteins on Cardiomyocyte Cytoarchitecture and Function. J. Cell Biol., 131: 1759-1773.
    • (1995) J. Cell Biol. , vol.131 , pp. 1759-1773
    • Von Arx, P.1    Bantle, S.2    Soldati, T.3    Perriard, J.-C.4


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