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Volumn 174, Issue 1, 2011, Pages 44-51

Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin

Author keywords

Cardiac myosin binding protein C; CMyBP C; Electron microscopy; F actin

Indexed keywords

ACTIN; F ACTIN; MYOSIN BINDING PROTEIN C;

EID: 79952454934     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.12.003     Document Type: Article
Times cited : (72)

References (63)
  • 1
    • 55149084783 scopus 로고    scopus 로고
    • Myosin binding protein C positioned to play a key role in regulation of muscle contraction: structure and interactions of domain C1
    • Ababou A., Rostkova E., Mistry S., Le Masurier C., Gautel M., Pfuhl M. Myosin binding protein C positioned to play a key role in regulation of muscle contraction: structure and interactions of domain C1. J. Mol. Biol. 2008, 384:615-630.
    • (2008) J. Mol. Biol. , vol.384 , pp. 615-630
    • Ababou, A.1    Rostkova, E.2    Mistry, S.3    Le Masurier, C.4    Gautel, M.5    Pfuhl, M.6
  • 2
    • 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., Mikawa T. Skeletal muscle-specific myosin binding protein-H is expressed in Purkinje fibers of the cardiac conduction system. Circ. Res. 1997, 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
  • 3
    • 78650342501 scopus 로고    scopus 로고
    • The N-terminal region of twitchen binds thick and thin contractile filaments: redundant mechanisms of catch force maintenance
    • Butler T.M., Mooers S.U., Narayan S.R., Siegman M.J. The N-terminal region of twitchen binds thick and thin contractile filaments: redundant mechanisms of catch force maintenance. J. Biol Chem 2010, 285(52):40654-40665.
    • (2010) J. Biol Chem , vol.285 , Issue.52 , pp. 40654-40665
    • Butler, T.M.1    Mooers, S.U.2    Narayan, S.R.3    Siegman, M.J.4
  • 5
    • 33847032217 scopus 로고    scopus 로고
    • Radial displacement of myosin cross-bridges in mouse myocardium due to abalation of myosin binding protein-C
    • Colson B.A., Bekyarova T., Fitzsimons D.P., Irving T.C., Moss R.L. Radial displacement of myosin cross-bridges in mouse myocardium due to abalation of myosin binding protein-C. J. Mol. Biol. 2007, 367:36-41.
    • (2007) J. Mol. Biol. , vol.367 , pp. 36-41
    • Colson, B.A.1    Bekyarova, T.2    Fitzsimons, D.P.3    Irving, T.C.4    Moss, R.L.5
  • 6
    • 0025246301 scopus 로고
    • Isolation and characterization of a cDNA clone encoding avian skeletal C-protein: an intracellular member of the immunoglobulin superfamily
    • Einheber S., Fischman D. Isolation and characterization of a cDNA clone encoding avian skeletal C-protein: an intracellular member of the immunoglobulin superfamily. Proc. Natl. Acad. Sci. 1990, 87:2157-2161.
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 2157-2161
    • Einheber, S.1    Fischman, D.2
  • 7
    • 70349466537 scopus 로고    scopus 로고
    • Phosphorylation and the N-terminal extension of the regulatory light chain help orient and align the myosin heads in Drosophila flight muscle
    • Farman G.P., Miller M.S., Reedy M.C., Soto-Adames F.N., Vigoreaux J.O., Maughan D.W., Irving T.C. Phosphorylation and the N-terminal extension of the regulatory light chain help orient and align the myosin heads in Drosophila flight muscle. J. Struct. Biol. 2009, 168:240-249.
    • (2009) J. Struct. Biol. , vol.168 , pp. 240-249
    • Farman, G.P.1    Miller, M.S.2    Reedy, M.C.3    Soto-Adames, F.N.4    Vigoreaux, J.O.5    Maughan, D.W.6    Irving, T.C.7
  • 8
    • 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., Gautel M. A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur. J. Biochem. 1996, 235:317-323.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 9
    • 0042206432 scopus 로고    scopus 로고
    • Twitchin from molluscan catch muscle: primary structure and relationship between site-specific phosphorylation and mechanical function
    • Funabara D., Watabe S., Mooers S.U., Narayan S., Dudas C., Hartshone D.J., Siegman M.J., Butler T.M. Twitchin from molluscan catch muscle: primary structure and relationship between site-specific phosphorylation and mechanical function. J. Biol. Chem. 2003, 278:29308-29316.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29308-29316
    • Funabara, D.1    Watabe, S.2    Mooers, S.U.3    Narayan, S.4    Dudas, C.5    Hartshone, D.J.6    Siegman, M.J.7    Butler, T.M.8
  • 10
  • 11
    • 0026776004 scopus 로고
    • Mammalian skeletal muscle C-protein: purification from bovine muscle, binding to titin and the characterization of a full length cDNA
    • Furst D.O., Vinkemeyer U., Weber K. Mammalian skeletal muscle C-protein: purification from bovine muscle, binding to titin and the characterization of a full length cDNA. J. Cell Sci. 1992, 102:769-778.
    • (1992) J. Cell Sci. , vol.102 , pp. 769-778
    • Furst, D.O.1    Vinkemeyer, U.2    Weber, K.3
  • 12
    • 0023957833 scopus 로고
    • Phosphorylation of C-protein, troponin I, and phospholamban in isolated rabbit hearts
    • Garvey J.L., Kranias E.G., Solaro R.J. Phosphorylation of C-protein, troponin I, and phospholamban in isolated rabbit hearts. Biochem. J. 1988, 249:709-714.
    • (1988) Biochem. J. , vol.249 , pp. 709-714
    • Garvey, J.L.1    Kranias, E.G.2    Solaro, R.J.3
  • 13
    • 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., Labeit S. Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?. EMBO J. 1995, 14:1952-1960.
    • (1995) EMBO J. , vol.14 , pp. 1952-1960
    • Gautel, M.1    Zuffardi, O.2    Freiburg, A.3    Labeit, S.4
  • 14
    • 0033605334 scopus 로고    scopus 로고
    • Mutations in beta (â)-Myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C
    • Gruen M., Gautel M. Mutations in beta (â)-Myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C. J. Mol. Biol. 1999, 286:933-949.
    • (1999) J. Mol. Biol. , vol.286 , pp. 933-949
    • Gruen, M.1    Gautel, M.2
  • 16
    • 7244245537 scopus 로고    scopus 로고
    • Binding of myosin binding protein-C to myosin subfragment S2 affects contractility independent of a tether mechanism
    • Harris S.P., Rostkova E., Gautel M., Moss R.L. Binding of myosin binding protein-C to myosin subfragment S2 affects contractility independent of a tether mechanism. Circ. Res. 2004, 95:930-936.
    • (2004) Circ. Res. , vol.95 , pp. 930-936
    • Harris, S.P.1    Rostkova, E.2    Gautel, M.3    Moss, R.L.4
  • 17
    • 0022358078 scopus 로고
    • Effects of phosphorylated and unphosphorylated C-protein on cardiac actomyosin ATPase
    • Hartzell H.C. Effects of phosphorylated and unphosphorylated C-protein on cardiac actomyosin ATPase. J. Mol. Biol. 1985, 186:185-195.
    • (1985) J. Mol. Biol. , vol.186 , pp. 185-195
    • Hartzell, H.C.1
  • 18
    • 0021713707 scopus 로고
    • 2+-calmodulin-dependent protein kinases
    • 2+-calmodulin-dependent protein kinases. J. Biol. Chem. 1984, 259:15587-15596.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15587-15596
    • Hartzell, H.C.1    Glass, D.B.2
  • 19
    • 0020074903 scopus 로고
    • Effects of cholinergic and adrenergic agonists on phosphorylation of a 165,000-dalton myofibrillar protein in intact cardiac muscle
    • Hartzell H.C., Titus L. Effects of cholinergic and adrenergic agonists on phosphorylation of a 165,000-dalton myofibrillar protein in intact cardiac muscle. J. Biol. Chem. 1982, 257:2111-2120.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2111-2120
    • Hartzell, H.C.1    Titus, L.2
  • 20
    • 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. 1991, 97:1141-1163.
    • (1991) J. Gen. Physiol. , vol.97 , pp. 1141-1163
    • Hofmann, P.A.1    Hartzell, H.C.2    Moss, R.L.3
  • 21
    • 0025075839 scopus 로고
    • Atomic model of the actin filament
    • Holmes K.C., Popp D., Gebhard W., Kabsch W. Atomic model of the actin filament. Nature 1990, 347(6288):44-49.
    • (1990) Nature , vol.347 , Issue.6288 , pp. 44-49
    • Holmes, K.C.1    Popp, D.2    Gebhard, W.3    Kabsch, W.4
  • 22
    • 0019216704 scopus 로고
    • Phosphorylation of a myofibrillar protein of Mr 150,000 in perfused rat heart, and the tentative identification of this as C-protein
    • Jeacocke S., England P. Phosphorylation of a myofibrillar protein of Mr 150,000 in perfused rat heart, and the tentative identification of this as C-protein. FEBS Lett. 1980, 122:129-132.
    • (1980) FEBS Lett. , vol.122 , pp. 129-132
    • Jeacocke, S.1    England, P.2
  • 23
    • 40849123741 scopus 로고    scopus 로고
    • Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C
    • Jefferies C.M., Whitten A.E., Harris S.P., Trewhella J. Small-angle X-ray scattering reveals the N-terminal domain organization of cardiac myosin binding protein C. J. Mol. Biol. 2008, 377:1186-1199.
    • (2008) J. Mol. Biol. , vol.377 , pp. 1186-1199
    • Jefferies, C.M.1    Whitten, A.E.2    Harris, S.P.3    Trewhella, J.4
  • 24
    • 77950653440 scopus 로고    scopus 로고
    • Identification of novel protein kinase A phosphorylation sites in the M-domain of human and murine cardiac myosin binding protein-C using mass spectrometry analysis
    • Jia W., Shaffer J.F., Harris S.P., Leary J.A. Identification of novel protein kinase A phosphorylation sites in the M-domain of human and murine cardiac myosin binding protein-C using mass spectrometry analysis. J. Proteome Res. 2010, 9:1843-1853.
    • (2010) J. Proteome Res. , vol.9 , pp. 1843-1853
    • Jia, W.1    Shaffer, J.F.2    Harris, S.P.3    Leary, J.A.4
  • 25
    • 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., Kato N. 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. 1994, 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
  • 26
    • 0036197173 scopus 로고    scopus 로고
    • Mammalian cardiac muscle thick filaments: their periodicity and interactions with actin
    • Kensler R.W. Mammalian cardiac muscle thick filaments: their periodicity and interactions with actin. Biophys. J. 2002, 82:1497-1508.
    • (2002) Biophys. J. , vol.82 , pp. 1497-1508
    • Kensler, R.W.1
  • 27
    • 13844264469 scopus 로고    scopus 로고
    • The mammalian cardiac muscle thick filament: crossbridge arrangement
    • Kensler R.W. The mammalian cardiac muscle thick filament: crossbridge arrangement. J. Struct. Biol. 2005, 149:303-312.
    • (2005) J. Struct. Biol. , vol.149 , pp. 303-312
    • Kensler, R.W.1
  • 28
    • 13844292743 scopus 로고    scopus 로고
    • The mammalian cardiac muscle thick filament: backbone contributions to meridional reflections
    • Kensler R.W. The mammalian cardiac muscle thick filament: backbone contributions to meridional reflections. J. Struct. Biol. 2005, 149:313-324.
    • (2005) J. Struct. Biol. , vol.149 , pp. 313-324
    • Kensler, R.W.1
  • 29
    • 41449090449 scopus 로고    scopus 로고
    • The structure of isolated myosin thick filaments from cMyBP-C knockout mice
    • Kensler R.W., Harris S.P. The structure of isolated myosin thick filaments from cMyBP-C knockout mice. Biophys. J. 2008, 94:1707-1718.
    • (2008) Biophys. J. , vol.94 , pp. 1707-1718
    • Kensler, R.W.1    Harris, S.P.2
  • 30
    • 79952441051 scopus 로고    scopus 로고
    • Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin
    • (abstract)
    • Kensler R.W., Shaffer J.F., Harris S.P. Binding of the N-terminal fragment C0-C2 of cardiac MyBP-C to cardiac F-actin. Biophys. J. 2010, 98:554a. (abstract).
    • (2010) Biophys. J. , vol.98
    • Kensler, R.W.1    Shaffer, J.F.2    Harris, S.P.3
  • 31
    • 0142024741 scopus 로고    scopus 로고
    • Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C
    • Korte F.S., McDonald K.S., Harris S.P., Moss R.L. Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C. Circ. Res. 2003, 93:752-758.
    • (2003) Circ. Res. , vol.93 , pp. 752-758
    • Korte, F.S.1    McDonald, K.S.2    Harris, S.P.3    Moss, R.L.4
  • 33
    • 0033972217 scopus 로고    scopus 로고
    • Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2
    • Kunst G., Kress M., Gruen M., Utenweiler D., Gautel M., Fink R.H.A. Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2. Circ. Res. 2000, 86:51-58.
    • (2000) Circ. Res. , vol.86 , pp. 51-58
    • Kunst, G.1    Kress, M.2    Gruen, M.3    Utenweiler, D.4    Gautel, M.5    Fink, R.H.A.6
  • 34
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz M., Popp D., Holmes K.C. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 1993, 234:826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 35
    • 0028940312 scopus 로고
    • An atomic model of the unregulated thin filament obtained by X-ray diffraction on oriented actin-tropomyosin gels
    • Lorenz M., Poole k.J., Popp D., Rosenbaum G., Holmes K.C. An atomic model of the unregulated thin filament obtained by X-ray diffraction on oriented actin-tropomyosin gels. J. Mol. Biol. 1995, 246:108-119.
    • (1995) J. Mol. Biol. , vol.246 , pp. 108-119
    • Lorenz, M.1    Poole, K.2    Popp, D.3    Rosenbaum, G.4    Holmes, K.C.5
  • 36
    • 0034976642 scopus 로고    scopus 로고
    • The molecular genetic basis for hypertrophic cardiomyopathy
    • Marian A.J., Roberts R. The molecular genetic basis for hypertrophic cardiomyopathy. J. Mol. Cell Cardiol. 2001, 33:655-670.
    • (2001) J. Mol. Cell Cardiol. , vol.33 , pp. 655-670
    • Marian, A.J.1    Roberts, R.2
  • 37
    • 0034907680 scopus 로고    scopus 로고
    • Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin-binding protein C
    • McClellan G., Kulikovskaya I., Winegrad S. Changes in cardiac contractility related to calcium-mediated changes in phosphorylation of myosin-binding protein C. Biophys. J. 2001, 81:1083-1092.
    • (2001) Biophys. J. , vol.81 , pp. 1083-1092
    • McClellan, G.1    Kulikovskaya, I.2    Winegrad, S.3
  • 38
    • 0019723545 scopus 로고
    • Fluorescence microscope study of the binding of added C-protein to skeletal muscle myofibrils
    • Moos C. Fluorescence microscope study of the binding of added C-protein to skeletal muscle myofibrils. J. Cell Biol. 1981, 90:25-31.
    • (1981) J. Cell Biol. , vol.90 , pp. 25-31
    • Moos, C.1
  • 39
    • 0018126953 scopus 로고
    • The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1
    • Moos C., Mason C.M., Besterman J.M., Feng I.N., Dubin J.H. The binding of skeletal muscle C-protein to F-actin, and its relation to the interaction of actin with myosin subfragment-1. J. Mol. Biol. 1978, 124:571-586.
    • (1978) J. Mol. Biol. , vol.124 , pp. 571-586
    • Moos, C.1    Mason, C.M.2    Besterman, J.M.3    Feng, I.N.4    Dubin, J.H.5
  • 40
    • 0032853632 scopus 로고    scopus 로고
    • Tuning the human heart molecular motors by myosin light chains
    • Morano I. Tuning the human heart molecular motors by myosin light chains. J. Mol. Biol. 1999, 77:544-555.
    • (1999) J. Mol. Biol. , vol.77 , pp. 544-555
    • Morano, I.1
  • 41
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular- to fibrous-actin transition
    • Oda T., Iwasa M., Aihara T., Maeda Y., Narita A. The nature of the globular- to fibrous-actin transition. Nature 2009, 457:441-445.
    • (2009) Nature , vol.457 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maeda, Y.4    Narita, A.5
  • 42
    • 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., Fischman D.A., Vaughan K.T., Mikawa T., Reinach F.C. The major myosin-binding domain of skeletal muscle MyBP-C (C-protein) resides in the COOH-terminal immunoglobulin C2 motif. J. Cell Biol. 1993, 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
  • 43
    • 79952440381 scopus 로고    scopus 로고
    • Binding of N-terminus fragments of cardiac myosin-binding C-protein to actin
    • (abstract)
    • Orlova A., Galkin V.E., Jeffries C.M., Trewhella J., Engelman E.H. Binding of N-terminus fragments of cardiac myosin-binding C-protein to actin. Biophys. J. 2010, 98:157a. (abstract).
    • (2010) Biophys. J. , vol.98
    • Orlova, A.1    Galkin, V.E.2    Jeffries, C.M.3    Trewhella, J.4    Engelman, E.H.5
  • 48
    • 33846021648 scopus 로고    scopus 로고
    • Effects of the N-terminal domains of myosin binding protein-C in an in vitro motility assay: evidence for long-lived cross-bridges
    • Razumova M.V., Shaffer J.F., Tu A.Y., Flint G.V., Regnier M., Harris S.P. Effects of the N-terminal domains of myosin binding protein-C in an in vitro motility assay: evidence for long-lived cross-bridges. J. Biol. Chem. 2006, 281:35846-35854.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35846-35854
    • Razumova, M.V.1    Shaffer, J.F.2    Tu, A.Y.3    Flint, G.V.4    Regnier, M.5    Harris, S.P.6
  • 49
    • 59449108572 scopus 로고    scopus 로고
    • Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae
    • Razumova M.V., Bezold K.L., Tu A.Y., Regnier M., Harris S.P. Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae. J. Gen. Physiol. 2008, 132:575-585.
    • (2008) J. Gen. Physiol. , vol.132 , pp. 575-585
    • Razumova, M.V.1    Bezold, K.L.2    Tu, A.Y.3    Regnier, M.4    Harris, S.P.5
  • 50
    • 78751475039 scopus 로고    scopus 로고
    • Myosin binding protein C interactions with actin: characterization and mapping of the binding site
    • Rybakova I.N., Greaser M.L., Moss R.L. Myosin binding protein C interactions with actin: characterization and mapping of the binding site. J. Biol. Chem. 2010, 10.1074/jbc.M110.170605e.
    • (2010) J. Biol. Chem.
    • Rybakova, I.N.1    Greaser, M.L.2    Moss, R.L.3
  • 51
    • 0025727168 scopus 로고
    • Phosphorylation of chick cardiac C-protein by calcium/calmodulin-dependent protein kinase II
    • Schlender K., Bean L.J. Phosphorylation of chick cardiac C-protein by calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 1991, 266:2811-2817.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2811-2817
    • Schlender, K.1    Bean, L.J.2
  • 52
    • 0023225164 scopus 로고
    • Dephosphorylation of cardiac myofibril C-protein by protein phosphatase 1 and protein phosphatase 2A
    • Schlender K.K., Hegazy M.G., Thysseril T.J. Dephosphorylation of cardiac myofibril C-protein by protein phosphatase 1 and protein phosphatase 2A. Biochim. Biophys. Acta 1987, 928:312-319.
    • (1987) Biochim. Biophys. Acta , vol.928 , pp. 312-319
    • Schlender, K.K.1    Hegazy, M.G.2    Thysseril, T.J.3
  • 53
    • 66449110385 scopus 로고    scopus 로고
    • The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner
    • Shaffer J.F., Kensler R.W., Harris S.P. The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner. J. Biol. Chem. 2009, 284:12318-12327.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12318-12327
    • Shaffer, J.F.1    Kensler, R.W.2    Harris, S.P.3
  • 54
    • 0042093724 scopus 로고    scopus 로고
    • Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain
    • Squire J.M., Luther P.K., Knupp C. Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain. J. Mol. Biol. 2003, 331:713-724.
    • (2003) J. Mol. Biol. , vol.331 , pp. 713-724
    • Squire, J.M.1    Luther, P.K.2    Knupp, C.3
  • 55
    • 33744944759 scopus 로고    scopus 로고
    • Ablation of myosin-binding protein C accelerates force development in mouse myocardium
    • Stelzer J.E., Fitzsimons D.P., Moss R.L. Ablation of myosin-binding protein C accelerates force development in mouse myocardium. Biophys. J. 2006, 90:4119-4127.
    • (2006) Biophys. J. , vol.90 , pp. 4119-4127
    • Stelzer, J.E.1    Fitzsimons, D.P.2    Moss, R.L.3
  • 56
    • 0141887125 scopus 로고    scopus 로고
    • Fine tuning the myosin motor: the role of the essential light chain in striated muscle myosin
    • Timson D.J. Fine tuning the myosin motor: the role of the essential light chain in striated muscle myosin. Biochimie 2003, 85:639-645.
    • (2003) Biochimie , vol.85 , pp. 639-645
    • Timson, D.J.1
  • 57
    • 55449118232 scopus 로고    scopus 로고
    • Acceleration of crossbridge kinetics by protein kinase A phosphorylation of cardiac myosin binding protein C modulates cardiac function
    • Tong C.W., Stelzer J.E., Greaser M.L., Powers P.A., Moss R.L. Acceleration of crossbridge kinetics by protein kinase A phosphorylation of cardiac myosin binding protein C modulates cardiac function. Circ. Res. 2008, 103:974-982.
    • (2008) Circ. Res. , vol.103 , pp. 974-982
    • Tong, C.W.1    Stelzer, J.E.2    Greaser, M.L.3    Powers, P.A.4    Moss, R.L.5
  • 58
    • 0027407773 scopus 로고
    • Molecular cloning of chicken myosin-binding protein H (MyBP) H (86 KDa protein) reveals extensive homology with the MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs
    • Vaughan K.T., Weber F.E., Einheber S., Fischman D.A. Molecular cloning of chicken myosin-binding protein H (MyBP) H (86 KDa protein) reveals extensive homology with the MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs. J. Biol. Chem. 1993, 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
  • 59
    • 0029812703 scopus 로고    scopus 로고
    • Alteration of myosin cross-bridges by phosphorylation of myosin-binding protein C in cardiac muscle
    • Weisberg A., Winegrad S. Alteration of myosin cross-bridges by phosphorylation of myosin-binding protein C in cardiac muscle. Proc. Natl. Acad. Sci. 1996, 93:8999-9003.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 8999-9003
    • Weisberg, A.1    Winegrad, S.2
  • 60
    • 0032514222 scopus 로고    scopus 로고
    • Relation between crossbridge structure and actomyosin ATPase activity in rat heart
    • Weisberg A., Winegrad S. Relation between crossbridge structure and actomyosin ATPase activity in rat heart. Circ. Res. 1998, 83:60-72.
    • (1998) Circ. Res. , vol.83 , pp. 60-72
    • Weisberg, A.1    Winegrad, S.2
  • 61
    • 57449111078 scopus 로고    scopus 로고
    • Cardiac myosin-binding protein C decorates F-acti: implications for cardiac function
    • Whitten A.E., Jeffries C.M., Harris S.P., Trewhella J. Cardiac myosin-binding protein C decorates F-acti: implications for cardiac function. PNAS 2008, 105:18360-18365.
    • (2008) PNAS , vol.105 , pp. 18360-18365
    • Whitten, A.E.1    Jeffries, C.M.2    Harris, S.P.3    Trewhella, J.4
  • 62
    • 0023029653 scopus 로고
    • The binding of skeletal muscle C-protein to regulated actin
    • Yamamoto K. The binding of skeletal muscle C-protein to regulated actin. FEBS Lett. 1986, 208:123-127.
    • (1986) FEBS Lett. , vol.208 , pp. 123-127
    • Yamamoto, K.1
  • 63
    • 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., Obinata T. Complete primary structure of chicken cardiac C-protein (MyBP-C) and its expression in developing striated muscles. J. Mol. Cell Cardiol. 1995, 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


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