메뉴 건너뛰기




Volumn 112, Issue 1, 1999, Pages 69-79

Identification of the A-band localization domain of myosin binding proteins C and H (MyBP-C, MyBP-H) in skeletal muscle

Author keywords

A band; C protein; Development; Familial hypertrophic cardiomyopathy; H protein; Muscle protein; Sarcomere; Thick filament; Titin

Indexed keywords

CONNECTIN; MYOSIN;

EID: 0032945827     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (74)

References (54)
  • 1
    • 0030936282 scopus 로고    scopus 로고
    • Skeletal muscle-specific myosin binding protein-H is expressed in Purkinje fibers of the cardiac conduction system
    • Alyonycheva, T., Cohen-Gould, L., Siewert, C., Fischman, D. A. and Mikawa, T. (1997a). Skeletal muscle-specific myosin binding protein-H is expressed in Purkinje fibers of the cardiac conduction system. Circ. Res. 80, 665-672.
    • (1997) Circ. Res. , vol.80 , pp. 665-672
    • Alyonycheva, T.1    Cohen-Gould, L.2    Siewert, C.3    Fischman, D.A.4    Mikawa, T.5
  • 2
    • 0030861651 scopus 로고    scopus 로고
    • Isoform-specitic interaction of the myosin-binding proteins (MyBPs) with skeletal and cardiac myosin is a property of the C-terminal immunoglobulin domain
    • Alyonycheva, T. N., Mikawa, T., Reinach, F. C. and Fischman, D. A. (1997b). Isoform-specitic interaction of the myosin-binding proteins (MyBPs) with skeletal and cardiac myosin is a property of the C-terminal immunoglobulin domain. J. Biol. Chem. 272, 20866-20872.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20866-20872
    • Alyonycheva, T.N.1    Mikawa, T.2    Reinach, F.C.3    Fischman, D.A.4
  • 3
    • 0022384881 scopus 로고
    • Novel thick filament protein of chicken pectoralis muscle: The 86 kd protein. II. Purification and characterization
    • Bahler, M., Eppenberger, H. M. and Wallimann, T. (1985a). Novel thick filament protein of chicken pectoralis muscle: the 86 kd protein. II. Purification and characterization. J. Mol. Biol. 186, 381-391.
    • (1985) J. Mol. Biol. , vol.186 , pp. 381-391
    • Bahler, M.1    Eppenberger, H.M.2    Wallimann, T.3
  • 4
    • 0022380096 scopus 로고
    • Novel thick filament protein of chicken pectoralis muscle: The 86 kd protein. II. Distribution and localization
    • Bahler, M., Eppenberger, H. M. and Wallimann, T. (1985b). Novel thick filament protein of chicken pectoralis muscle: the 86 kd protein. II. Distribution and localization. J. Mol. Biol. 186, 393-401.
    • (1985) J. Mol. Biol. , vol.186 , pp. 393-401
    • Bahler, M.1    Eppenberger, H.M.2    Wallimann, T.3
  • 5
    • 0022899276 scopus 로고
    • The ultrastructural location of C-protein. X-protein and H-protein in rabbit muscle
    • Bennett, P., Craig, R., Starr, R. and Offer, G. (1986). The ultrastructural location of C-protein. X-protein and H-protein in rabbit muscle. J. Musc. Res. Cell Motil. 7, 550-567.
    • (1986) J. Musc. Res. Cell Motil. , vol.7 , pp. 550-567
    • Bennett, P.1    Craig, R.2    Starr, R.3    Offer, G.4
  • 8
    • 0017234893 scopus 로고
    • The location of C-prolein in rabbit skeletal muscle
    • Craig, R. and Offer, G. (1976). The location of C-prolein in rabbit skeletal muscle. Proc. Roy. Soc. Lond. B, 192, 451-461.
    • (1976) Proc. Roy. Soc. Lond. B , vol.192 , pp. 451-461
    • Craig, R.1    Offer, G.2
  • 9
    • 0023993251 scopus 로고
    • Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from myosin of vertebrate skeletal muscle
    • Davis, J. S. (1988). Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from myosin of vertebrate skeletal muscle. J. Musc. Res. Cell Motil. 9, 174-183.
    • (1988) J. Musc. Res. Cell Motil. , vol.9 , pp. 174-183
    • Davis, J.S.1
  • 10
    • 0021259458 scopus 로고
    • Localization of C-protein isoforms in chicken skeletal muscle: Ultrastructural detection using monoclonal antibodies
    • Dennis, J. E., Shimizu. T., Reinach, F. C. and Fischman, D. A. (1984) Localization of C-protein isoforms in chicken skeletal muscle: ultrastructural detection using monoclonal antibodies. J. Cell Biol. 98, 1514-1522.
    • (1984) J. Cell Biol. , vol.98 , pp. 1514-1522
    • Dennis, J.E.1    Shimizu, T.2    Reinach, F.C.3    Fischman, D.A.4
  • 11
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for c-myc proto oncogene product
    • Evan, G. I., Lewis, G. K., Ramsay, G. and Bishop, J. M. (1985). Isolation of monoclonal antibodies specific for c-myc proto oncogene product. Mol. Cell. Biol. 5, 3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 12
    • 0025246301 scopus 로고
    • Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: An intrucellulur member of the immunoglobulin superfamily
    • Einheber, S. and Fischman, D. A. (1990). Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: an intrucellulur member of the immunoglobulin superfamily. Proc. Nat. Acad. Sci. USA 87, 2157-2161.
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 2157-2161
    • Einheber, S.1    Fischman, D.A.2
  • 13
    • 0030052266 scopus 로고    scopus 로고
    • A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • Freiburg, A. and Gautel, M. (1996). A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur. J. Biochem. 235, 317-323.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 14
    • 0026776004 scopus 로고
    • Mammalian skeletal muscle C-protein: Purification from bovine muscle, binding to titin and the characterization of a full-length human cDNA
    • Fürst, D. O., Vinkemeier, U. and Weber, K. (1992). Mammalian skeletal muscle C-protein: purification from bovine muscle, binding to titin and the characterization of a full-length human cDNA. J. Cell Sci. 102, 769-778.
    • (1992) J. Cell Sci. , vol.102 , pp. 769-778
    • Fürst, D.O.1    Vinkemeier, U.2    Weber, K.3
  • 15
    • 0029029027 scopus 로고
    • Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: A modulator of cardiac contraction?
    • Gautel, M., Zuffardi, O., Freiburg, A. and Labeit, S. (1995). Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction? EMBO J. 14, 1952-1960.
    • (1995) EMBO J. , vol.14 , pp. 1952-1960
    • Gautel, M.1    Zuffardi, O.2    Freiburg, A.3    Labeit, S.4
  • 16
    • 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 Fischman, 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    Fischman, D.A.4
  • 18
    • 0020074903 scopus 로고
    • Effects of cholinergic and adrenergic agonists on phosphorslation of a 165.000-dalton myofibrillar protein in intact cardiac muscle
    • Hartzell, H. C. and Titus, L. (1982). Effects of cholinergic and adrenergic agonists on phosphorslation of a 165.000-dalton myofibrillar protein in intact cardiac muscle J. Biol. Chem. 257, 2111-2120.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2111-2120
    • Hartzell, H.C.1    Titus, L.2
  • 19
    • 0021241235 scopus 로고
    • Phosphorylation of C-protein in intact amphibian cardiac muscle Correlation between 32P incorporation and twitch relaxation
    • Hartzell, H. C. (1984). Phosphorylation of C-protein in intact amphibian cardiac muscle Correlation between 32P incorporation and twitch relaxation. J. Gen. Physiol. 3, 563-588.
    • (1984) J. Gen. Physiol. , vol.3 , pp. 563-588
    • Hartzell, H.C.1
  • 20
    • 0022358078 scopus 로고
    • Effects of phosphorylated and unphosphorylated C-protein on cardiac actomyosin ATPase
    • Hartzell, H. (1985). Effects of phosphorylated and unphosphorylated C-protein on cardiac actomyosin ATPase. J. Mol. Biol. 186, 185-195.
    • (1985) J. Mol. Biol. , vol.186 , pp. 185-195
    • Hartzell, H.1
  • 22
    • 0026360178 scopus 로고
    • 2+ sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers
    • 2+ sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers. J. Gen. Physiol. 97, 1141-1163.
    • (1991) J. Gen. Physiol. , vol.97 , pp. 1141-1163
    • Hofmann, P.A.1    Hartzell, H.C.2    Moss, R.L.3
  • 23
    • 0028094767 scopus 로고
    • Autoimmune myocarditis induced in mice by cardiac C-protein. Cloning of complementary DNA encoding murine cardiac C-protein and partial characterization of the antigenic peptides
    • Kasahara, H., Itoh, M., Sugiyama, T., Kido, N., Hayashi, H., Saito, H., Tsukita, S. and Kato, N. (1994). Autoimmune myocarditis induced in mice by cardiac C-protein. Cloning of complementary DNA encoding murine cardiac C-protein and partial characterization of the antigenic peptides. J. Clin. Invest. 94, 1026-1036.
    • (1994) J. Clin. Invest. , vol.94 , pp. 1026-1036
    • Kasahara, H.1    Itoh, M.2    Sugiyama, T.3    Kido, N.4    Hayashi, H.5    Saito, H.6    Tsukita, S.7    Kato, N.8
  • 24
    • 0018674244 scopus 로고
    • Effects of C-protein on synthetic myosin filament structure
    • Koretz, J. (1979). Effects of C-protein on synthetic myosin filament structure. Biophys. J. 27, 433-446.
    • (1979) Biophys. J. , vol.27 , pp. 433-446
    • Koretz, J.1
  • 25
    • 0027283001 scopus 로고
    • Filamentous aggregates of native titin and binding of C-protein and AMP-deaminase
    • Koretz, J. F., Irving, T. C. and Wang, K. (1993). Filamentous aggregates of native titin and binding of C-protein and AMP-deaminase. Arch. Biochem. Biophys. 304, 305-309.
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 305-309
    • Koretz, J.F.1    Irving, T.C.2    Wang, K.3
  • 26
    • 0028824803 scopus 로고
    • Assembly of cardiac C-protein during myofibrillogenesis in myogenic cells in culture
    • Koshida, S., Kurasawa, M., Yasuda, M., Sato, N. and Obinata, T. (1995). Assembly of cardiac C-protein during myofibrillogenesis in myogenic cells in culture. Cell Struct. Funct. 20, 253-261.
    • (1995) Cell Struct. Funct. , vol.20 , pp. 253-261
    • Koshida, S.1    Kurasawa, M.2    Yasuda, M.3    Sato, N.4    Obinata, T.5
  • 27
    • 0027058975 scopus 로고
    • Clonal analysis of cardiac morphogenesis in the chicken embryo using a replication-defective retrovirus. III: Polyclonal origin of adjacent ventricular myocytes
    • Mikawa, T., Cohen-Gould, L. and Fischman, D. A. (1992). Clonal analysis of cardiac morphogenesis in the chicken embryo using a replication-defective retrovirus. III: Polyclonal origin of adjacent ventricular myocytes. Dev. Dynam. 195, 133-141.
    • (1992) Dev. Dynam. , vol.195 , pp. 133-141
    • Mikawa, T.1    Cohen-Gould, L.2    Fischman, D.A.3
  • 28
    • 0024311374 scopus 로고
    • Evolutionary conserved sequences of striated muscle myosin heavy chain isoforms
    • Miller, J. B., Teal, S. B. and StockDale, F. E. (1989). Evolutionary conserved sequences of striated muscle myosin heavy chain isoforms. J. Biol. Chem. 264, 13122-13130.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13122-13130
    • Miller, J.B.1    Teal, S.B.2    Stockdale, F.E.3
  • 29
    • 0016818769 scopus 로고
    • Interaction of C-protein with myosin, myosin rod and light meromyosin
    • Moos, C., Offer, G., Starr, R. and Bennett, P. (1975). Interaction of C-protein with myosin, myosin rod and light meromyosin. J. Mol. Biol. 97, 1-9.
    • (1975) J. Mol. Biol. , vol.97 , pp. 1-9
    • Moos, C.1    Offer, G.2    Starr, R.3    Bennett, P.4
  • 30
    • 0018126953 scopus 로고
    • The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment
    • Moos, C., Mason, C., Besterman, J., Feng, I. and Dubin, J. (1978). The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment. J. Mol. Biol. 124, 571-586.
    • (1978) J. Mol. Biol. , vol.124 , pp. 571-586
    • Moos, C.1    Mason, C.2    Besterman, J.3    Feng, I.4    Dubin, J.5
  • 31
    • 0016190087 scopus 로고
    • The line structure of developing unit collagenous fibrils in the chick
    • Morse, D. E. and Low, F. N. (1974). The line structure of developing unit collagenous fibrils in the chick. Am. J. Anal. 140, 237-262.
    • (1974) Am. J. Anal. , vol.140 , pp. 237-262
    • Morse, D.E.1    Low, F.N.2
  • 33
    • 0015924821 scopus 로고
    • A new protein of the thick filaments of vertebrate skeletal myofibrils. Extraction, purification and characterization
    • Offer, G., Moos, C. and Starr, R. (1973). A new protein of the thick filaments of vertebrate skeletal myofibrils. Extraction, purification and characterization. J. Mol. Biol. 74, 653-676.
    • (1973) J. Mol. Biol. , vol.74 , pp. 653-676
    • Offer, G.1    Moos, C.2    Starr, R.3
  • 34
    • 0027515217 scopus 로고
    • The major myosin-binding domain of skeletal muscle MyBP-C (C-protein) resides in the C-terminal, immunoglobulin C2 motif
    • Okagaki, T., Weber, F. E., Fischman, 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 C-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    Fischman, D.A.3    Vaughan, K.T.4    Mikawa, T.5    Reinach, F.C.6
  • 35
    • 0020350969 scopus 로고
    • Isoforms of C-protein in adult chicken skeletal muscle: Detection with monoclonal antibodies
    • Reinach, F. C., Masaki, T., Shafiq, S., Obinata, T. and Fischman, D. A. (1982). Isoforms of C-protein in adult chicken skeletal muscle: detection with monoclonal antibodies. J. Cell Biol. 95, 78-84.
    • (1982) J. Cell Biol. , vol.95 , pp. 78-84
    • Reinach, F.C.1    Masaki, T.2    Shafiq, S.3    Obinata, T.4    Fischman, D.A.5
  • 37
    • 0030027029 scopus 로고    scopus 로고
    • Modulation of myosin filament organization by C-protein family members
    • Seiler, S. H., Fischman, D. A. and Leinwand, L. A. (1996). Modulation of myosin filament organization by C-protein family members. Mol. Biol. Cell. 7, 113-127.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 113-127
    • Seiler, S.H.1    Fischman, D.A.2    Leinwand, L.A.3
  • 38
    • 0013617971 scopus 로고
    • Nucleotide sequence 5′ of the chicken c-myc coding region: Localization of a noncoding exon that is absent from myc transcripts in most avian leukosis virus-induced lymphomas
    • Shin, C.-K., Linial, M. L., Goodenow, M. M. and Hayward, W. S. (1984). Nucleotide sequence 5′ of the chicken c-myc coding region: localization of a noncoding exon that is absent from myc transcripts in most avian leukosis virus-induced lymphomas. Proc.. Nat. Acad. Sci. USA 81, 4697-4701.
    • (1984) Proc.. Nat. Acad. Sci. USA , vol.81 , pp. 4697-4701
    • Shin, C.-K.1    Linial, M.L.2    Goodenow, M.M.3    Hayward, W.S.4
  • 39
    • 0027536473 scopus 로고
    • A survey of interactions made by the giant protein titin
    • Soteriou, A., Gamage, M. and Trinick, J. (1993). A survey of interactions made by the giant protein titin. J. Cell Sci. 104, 119-123.
    • (1993) J. Cell Sci. , vol.104 , pp. 119-123
    • Soteriou, A.1    Gamage, M.2    Trinick, J.3
  • 40
    • 0021069784 scopus 로고
    • H-protein and X-protein. Two new components of the thick filaments of vertebrate skeletal muscle
    • Starr, R. and Offer, G. (1983). H-protein and X-protein. Two new components of the thick filaments of vertebrate skeletal muscle. J. Mol. Biol. 170, 675-698.
    • (1983) J. Mol. Biol. , vol.170 , pp. 675-698
    • Starr, R.1    Offer, G.2
  • 41
    • 0022383165 scopus 로고
    • A method for the efficient blotting of strongly basic proteins from sodium dodecyl sulfate-acrylamide gels to nitrocellulose
    • Szewczyk, B. and Kozloff, L. M. (1985). A method for the efficient blotting of strongly basic proteins from sodium dodecyl sulfate-acrylamide gels to nitrocellulose. Anal. Bioehem. 150, 403-407.
    • (1985) Anal. Bioehem. , vol.150 , pp. 403-407
    • Szewczyk, B.1    Kozloff, L.M.2
  • 42
    • 0024740978 scopus 로고
    • Size and charge heterogeneity of C-protein isoforms in avian skeletal muscle. Expression of six different isotorms in chicken muscle
    • Takano-Ohmuro, H., Goldfine, S. M., Kojima, T. Obinata, T. and Fischman, D. A. (1989). Size and charge heterogeneity of C-protein isoforms in avian skeletal muscle. Expression of six different isotorms in chicken muscle. J. Musc. Res. Cell Motil. 10, 369-378.
    • (1989) J. Musc. Res. Cell Motil. , vol.10 , pp. 369-378
    • Takano-Ohmuro, H.1    Goldfine, S.M.2    Kojima, T.3    Obinata, T.4    Fischman, D.A.5
  • 43
    • 0027285758 scopus 로고
    • Human myosin-binding protein H (MyBP-H): Complete primary sequence, repeat structure, genomic organization and chromosomal localization
    • Vaughan, K. T., Weber, F. E., Reinach, F. C., Ried, T., Ward, D. and Fischman, D. A. (1993a). Human myosin-binding protein H (MyBP-H): Complete primary sequence, repeat structure, genomic organization and chromosomal localization. Genomics 16, 34-40.
    • (1993) Genomics , vol.16 , pp. 34-40
    • Vaughan, K.T.1    Weber, F.E.2    Reinach, F.C.3    Ried, T.4    Ward, D.5    Fischman, D.A.6
  • 44
    • 0027407773 scopus 로고
    • Molecular cloning of chicken myosin-hinding protein (MyBP) H (86-kDa protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglohulin C2 and fibronectin type III motifs
    • Vaughan, K. T., Weber, F. E., Einheber, S. and Fischman, D. A. (1993b). Molecular cloning of chicken myosin-hinding protein (MyBP) H (86-kDa protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglohulin 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    Fischman, D.A.4
  • 46
    • 0031952705 scopus 로고    scopus 로고
    • Genotype: Phenotype correlations in hypertrophic cardiomyopathy
    • Watkins, H. (1998). Genotype: phenotype correlations in hypertrophic cardiomyopathy. Eur. Heart J. 19, 10-12.
    • (1998) Eur. Heart J. , vol.19 , pp. 10-12
    • Watkins, H.1
  • 47
    • 0027168759 scopus 로고
    • Complete sequence of human fast-type and slow-type muscle myosin-binding-protein C (MyBP-C): Differential expression, conserved domain structure and chromosome assignment
    • Weber, F. E., Vaughan, K. T., Okagaki, T., Reinach, F. C. and Fischman, D. A. (1993). Complete sequence of human fast-type and slow-type muscle myosin-binding-protein C (MyBP-C): Differential expression, conserved domain structure and chromosome assignment. Eur. J. Biochem. 216, 661-669.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 661-669
    • Weber, F.E.1    Vaughan, K.T.2    Okagaki, T.3    Reinach, F.C.4    Fischman, D.A.5
  • 48
    • 0029812703 scopus 로고    scopus 로고
    • Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle
    • Weisberg, A. and Winegrad, S. (1996). Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle. Proc. Nat. Acad. Sci. USA 93, 8999-9003.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.93 , pp. 8999-9003
    • Weisberg, A.1    Winegrad, S.2
  • 49
    • 0032514222 scopus 로고    scopus 로고
    • Relation between crossbridge structure and actomyosin ATPase activity in rat heart
    • Weisberg, A. and Winegrad, S. (1998). Relation between crossbridge structure and actomyosin ATPase activity in rat heart. Circ. Res. 83, 60-72.
    • (1998) Circ. Res. , vol.83 , pp. 60-72
    • Weisberg, A.1    Winegrad, S.2
  • 50
    • 0020522788 scopus 로고
    • The C-proteins of rabbit red, white, and cardiac muscles
    • Yamamoto, K. and Moos, C. (1983). The C-proteins of rabbit red, white, and cardiac muscles. J. Biol. Chem. 258, 8395-8401.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8395-8401
    • Yamamoto, K.1    Moos, C.2
  • 51
    • 0021194773 scopus 로고
    • Cliaracterization of H-protein, a component of skeletal muscle myofibrils
    • Yamamoto, K. (1984). Cliaracterization of H-protein, a component of skeletal muscle myofibrils. J. Biol. Chem. 259, 7163-7168.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7163-7168
    • Yamamoto, K.1
  • 52
    • 0023029653 scopus 로고
    • The binding of skeletal muscle C-protein to regulated actin
    • Yamamoto, K. (1986). The binding of skeletal muscle C-protein to regulated actin. FEBS Lett. 208, 123-127.
    • (1986) FEBS Lett. , vol.208 , pp. 123-127
    • Yamamoto, K.1
  • 53
    • 0028808791 scopus 로고
    • Complete primary structure of chicken cardiac C-protein (MyBP-C) and its expression in developing striated muscles
    • Yasuda, M., Koshida, S., Sato, N. and Obinata, T. (1995). Complete primary structure of chicken cardiac C-protein (MyBP-C) and its expression in developing striated muscles. J. Mol. Cell. Cardiol. 27, 2275-2286.
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 2275-2286
    • Yasuda, M.1    Koshida, S.2    Sato, N.3    Obinata, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.