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Volumn 538, Issue , 2004, Pages 31-41

Myosin-binding protein C (MyBP-C) in cardiac muscle and contractility

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN; MYOSIN BINDING PROTEIN C;

EID: 1842527103     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper
Times cited : (15)

References (33)
  • 3
    • 0017234893 scopus 로고
    • The location of C-protein in rabbit skeletal muscle
    • Lond
    • Craig, R., and Offer, G. 1976. The location of C-protein in rabbit skeletal muscle. Proc. R. Soc. (Lond) 192: 451-461
    • (1976) Proc. R. Soc. , vol.192 , pp. 451-461
    • Craig, R.1    Offer, G.2
  • 4
    • 0023993251 scopus 로고
    • Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from the myosin of vertebrate skeletal muscle
    • Davies, J. 1988. Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from the myosin of vertebrate skeletal muscle. J. Musc. Res. Cell Motil. 9: 174-183
    • (1988) J. Musc. Res. Cell Motil. , vol.9 , pp. 174-183
    • Davies, J.1
  • 5
    • 0033607481 scopus 로고    scopus 로고
    • COOH-tenninal truncated cardiac myosin binding protein C mutants resulting from familial hypertrophic cardiomyopathy mutations exhibit altered expression and/or incorporation into fetal rat cardiomyocytes
    • Flavigny J, Souchet M, Sebillon P, Berrebi-Bertrand I, Hainque B, Mallet A, Bril A, Schwartz K, And Carrier L. 1999. COOH-tenninal truncated cardiac myosin binding protein C mutants resulting from familial hypertrophic cardiomyopathy mutations exhibit altered expression and/or incorporation into fetal rat cardiomyocytes. J. Mol. Biol. 294: 443-456.
    • (1999) J. Mol. Biol. , vol.294 , pp. 443-456
    • Flavigny, J.1    Souchet, M.2    Sebillon, P.3    Berrebi-Bertrand, I.4    Hainque, B.5    Mallet, A.6    Bril, A.7    Schwartz, K.8    Carrier, L.9
  • 6
    • 0029029027 scopus 로고
    • Phosphorylation switches specific for the cardiac isoforms of myosin binding protein C: A modulator of cardiac contraction
    • Gautel, M., Zuffardi, O., Freiberg, A., and Labeit, S. 1995. Phosphorylation switches specific for the cardiac isoforms 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    Freiberg, A.3    Labeit, S.4
  • 7
    • 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 Sc. 109: 101-111.
    • (1996) J. Cell Sc. , vol.109 , pp. 101-111
    • Gilbert, R.1    Kelly, M.G.2    Mikawa, T.3    Fischman, D.A.4
  • 8
    • 0033605334 scopus 로고    scopus 로고
    • Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin binding protein-C
    • Gruen, M., and Gautel, M., 1999 Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin binding protein-C., J. Mol. Biol. 286, 933-949.
    • (1999) J. Mol. Biol. , vol.286 , pp. 933-949
    • Gruen, M.1    Gautel, M.2
  • 9
    • 0032772719 scopus 로고    scopus 로고
    • cAPK-phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin-S2 in an on-off fashion
    • Gruen, M., Prinz, H., and Gautel, M. 1999 cAPK-phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin-S2 in an on-off fashion. FEBS Letters. 453(3):254-9.
    • (1999) FEBS Letters. , vol.453 , Issue.3 , pp. 254-259
    • Gruen, M.1    Prinz, H.2    Gautel, M.3
  • 11
    • 0021713707 scopus 로고
    • Phosphorylation of purified cardiac muscle protein by purified cAMP-dependent and endogenous Ca-calmodulin-dependent protein kinases
    • Hartzell, C., and Glass, D. 1984. Phosphorylation of purified cardiac muscle protein by purified cAMP-dependent and endogenous Ca-calmodulin- dependent protein kinases. J. Biol. Chem 259: 15587-15596.
    • (1984) J. Biol. Chem , vol.259 , pp. 15587-15596
    • Hartzell, C.1    Glass, D.2
  • 12
    • 0026360178 scopus 로고
    • Alterations in Ca sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers
    • Hofmann, PA., Hartzell, HC., and Moss, RL. 1991 Alterations in Ca 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
  • 13
    • 0018674244 scopus 로고
    • Effects of C-protein on synthetic myosin filament structure
    • Koretz, J.F. 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.F.1
  • 14
    • 0033972217 scopus 로고    scopus 로고
    • MyBP-C (C-Protein)- 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., Uttenweiler, D., Gautel, M., and Fink, R.H.A. 2000. MyBP-C (C-Protein)- a phosphorylation dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin - S2. Circ. Res 86: 51-58.
    • (2000) Circ. Res. , vol.86 , pp. 51-58
    • Kunst, G.1    Kress, K.R.2    Gruen, M.3    Uttenweiler, D.4    Gautel, M.5    Fink, R.H.A.6
  • 15
    • 0034900675 scopus 로고    scopus 로고
    • Multiple structures of thick filaments in resting cardiac muscle and their influence on cross bridge interactions
    • Levine, R.J.C., Weisberg A., Kulikovskaya, I., McClellan, G. and Winegrad, S. 2001. Multiple structures of thick filaments in resting cardiac muscle and their influence on cross bridge interactions. Biophys. J. 81: 1070-1082.
    • (2001) Biophys. J. , vol.81 , pp. 1070-1082
    • Levine, R.J.C.1    Weisberg, A.2    Kulikovskaya, I.3    McClellan, G.4    Winegrad, S.5
  • 16
    • 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., Lu, M.H., Schultheiss, T., Choi, J., Holtzer, S., DiLuulo, 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. Cytoskel. 29: 1-19.
    • (1994) Cell Motil. Cytoskel. , vol.29 , pp. 1-19
    • Lin, Z.1    Lu, M.H.2    Schultheiss, T.3    Choi, J.4    Holtzer, S.5    DiLuulo, C.6    Fischman, D.A.7    Holtzer, H.8
  • 17
    • 0018340818 scopus 로고
    • Movement of myosin heads during a heart beat
    • Matsubara, I., Yagi, N., Endoh, M. 1979 Movement of myosin heads during a heart beat. Nature 278: 474-476.
    • (1979) Nature , vol.278 , pp. 474-476
    • Matsubara, I.1    Yagi, N.2    Endoh, M.3
  • 18
    • 0028141720 scopus 로고
    • CAMP can raise or lower cardiac actomyosin ATPase activity depending on alpha adrenergic activity
    • McClellan, G., Weisberg, A., and Winegrad, S. 1994. CAMP can raise or lower cardiac actomyosin ATPase activity depending on alpha adrenergic activity. Amer. J. Physiol. 267: H431-442
    • (1994) Amer. J. Physiol. , vol.267
    • McClellan, G.1    Weisberg, A.2    Winegrad, S.3
  • 19
    • 0034907680 scopus 로고    scopus 로고
    • Structural and functional responses of the contractile proteins to changes in calcium concentration in the heart
    • McClellan, G., Kulikovskaya, I. and Winegrad, S. 2001 Structural and functional responses of the contractile proteins to changes in calcium concentration in the heart. Biophys. J. 81: 1083-1092
    • (2001) Biophys. J. , vol.81 , pp. 1083-1092
    • McClellan, G.1    Kulikovskaya, I.2    Winegrad, S.3
  • 20
    • 0037131207 scopus 로고    scopus 로고
    • Identification of novel interactions between domains of myosin binding protein C that are modulated by hypertrophic cardiomyopathy missense mutations
    • Moolman-Smook, J., Flashman, E., de Lange, W., Li, Z., Corfield, V., Redwood, C., Wathins, H. 2002. Identification of novel interactions between domains of myosin binding protein C that are modulated by hypertrophic cardiomyopathy missense mutations Circ. Res. 91: 704-711.
    • (2002) Circ. Res. , vol.91 , pp. 704-711
    • Moolman-Smook, J.1    Flashman, E.2    De Lange, W.3    Li, Z.4    Corfield, V.5    Redwood, C.6    Wathins, H.7
  • 21
    • 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
  • 22
    • 0027515217 scopus 로고
    • The major myosin binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 repeat
    • 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 COOH-terminal, immunoglobulin C2 repeat. 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
  • 23
    • 0028278854 scopus 로고
    • The premyofibril: Evidence for its role in myofibrillogenesis
    • Rhee, D. Sanger, J.M., and Sanger, J.W. 1994. The premyofibril: evidence for its role in myofibrillogenesis. Cell Motil. Cytoskel. 28: 1-24.
    • (1994) Cell Motil. Cytoskel. , vol.28 , pp. 1-24
    • Rhee, D.1    Sanger, J.M.2    Sanger, J.W.3
  • 24
    • 0030852878 scopus 로고    scopus 로고
    • Novel splice donor site mutation in the cardiac myosin-binding protein C gene in familail hypertrophic cardiomyopathy. Charaterization of cardiac transcript and protein
    • Rottbauer, W., Gautel, M., Zehelein, J., Labeit, S., Franz, W.M., Fischer, C., Vollrath, B., Mall, G., Dietz, R., Kubler, W., Katus, H.A. Novel splice donor site mutation in the cardiac myosin-binding protein C gene in familail hypertrophic cardiomyopathy. Charaterization of cardiac transcript and protein. J. Clin. Invest. 100: 475-482. 1997
    • (1997) J. Clin. Invest. , vol.100 , pp. 475-482
    • Rottbauer, W.1    Gautel, M.2    Zehelein, J.3    Labeit, S.4    Franz, W.M.5    Fischer, C.6    Vollrath, B.7    Mall, G.8    Dietz, R.9    Kubler, W.10    Katus, H.A.11
  • 26
    • 0025727168 scopus 로고
    • Phosphorylation of chicken cardiac C protein by calcium calmodulin-dependent protein kinase II
    • Schlender, K., and Bean, L. 1991. Phosphorylation of chicken cardiac C protein by calcium calmodulin-dependent protein kinase II. J. Biol. Chem. 266: 2811-2817
    • (1991) J. Biol. Chem. , vol.266 , pp. 2811-2817
    • Schlender, K.1    Bean, L.2
  • 28
    • 0030027029 scopus 로고    scopus 로고
    • Modulation of myosin filament organization by C protein family members
    • Seiler, S.H., Fischman, D.A., Leinwand, L.A. 1996 Modulation of myosin filament organization by C protein family members. Molec. Biol. Cell 7: 113-127.
    • (1996) Molec. Biol. Cell , vol.7 , pp. 113-127
    • Seiler, S.H.1    Fischman, D.A.2    Leinwand, L.A.3
  • 29
    • 0017826080 scopus 로고
    • The interaction of C-protein with heavy meromyosin and subfragment-2
    • Starr, R. and Offer, G. 1978 The interaction of C-protein with heavy meromyosin and subfragment-2. Biochem. J. 171: 813-816.
    • (1978) Biochem. J. , vol.171 , pp. 813-816
    • Starr, R.1    Offer, G.2
  • 31
    • 0029812703 scopus 로고    scopus 로고
    • Alteration in myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle
    • USA
    • Weisberg, A., and Winegrad, S. 1996. Alteration in myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle. Proc. Nat. Acad. Sc (USA) 93: 8999-9003.
    • (1996) Proc. Nat. Acad. Sc , vol.93 , pp. 8999-9003
    • Weisberg, A.1    Winegrad, S.2
  • 32
    • 0032514222 scopus 로고    scopus 로고
    • Relation between cross bridge structure and actomyosin ATPase activity in rat heart
    • Weisberg, A., and Winegrad, S. 1998. Relation between cross bridge structure and actomyosin ATPase activity in rat heart. Circ. Res. 1998; 83: 60-72
    • (1998) Circ. Res. 1998 , vol.83 , pp. 60-72
    • Weisberg, A.1    Winegrad, S.2
  • 33
    • 0033612182 scopus 로고    scopus 로고
    • Cardiac myosin binding protein C
    • Winegrad, S. 1999. Cardiac myosin binding protein C. Circ. Res. 84: 1117-1126.
    • (1999) Circ. Res. , vol.84 , pp. 1117-1126
    • Winegrad, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.