메뉴 건너뛰기




Volumn 286, Issue 3, 1999, Pages 933-949

Mutations in β-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C

Author keywords

Coiled coil; Hypertrophic cardiomyopathy; Myosin; Myosin binding protein C

Indexed keywords

BINDING PROTEIN; IMMUNOGLOBULIN; MYOSIN; MYOSIN LIGHT CHAIN;

EID: 0033605334     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2522     Document Type: Article
Times cited : (210)

References (70)
  • 1
    • 0024394549 scopus 로고
    • Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
    • Andersson S., Davis D. L., Dahlback H., Jornvall H., Russell D. W. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem. 264:1989;8222-8229.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8222-8229
    • Andersson, S.1    Davis, D.L.2    Dahlback, H.3    Jornvall, H.4    Russell, D.W.5
  • 2
    • 0030861651 scopus 로고    scopus 로고
    • Isoform-specific 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., Fischman D. A. Isoform-specific interaction of the myosin-binding proteins (MyBPs) with skeletal and cardiac myosin is a property of the C-terminal immunoglobulin domain. J. Biol. Chem. 272:1997;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
  • 4
    • 0022335214 scopus 로고
    • Heart C-protein is transiently expressed during skeletal muscle development in the embryo, but persists in cultured myogenic cells
    • Bähler M., Moser H., Eppenberger H. M., Wallimann T. Heart C-protein is transiently expressed during skeletal muscle development in the embryo, but persists in cultured myogenic cells. Dev. Biol. 112:1985;345-352.
    • (1985) Dev. Biol. , vol.112 , pp. 345-352
    • Bähler, M.1    Moser, H.2    Eppenberger, H.M.3    Wallimann, T.4
  • 5
    • 0022899276 scopus 로고
    • The ultrastructural localization of C-protein, X-protein and H-protein in rabbit muscle
    • Bennett P., Craig R., Starr R., Offer G. The ultrastructural localization of C-protein, X-protein and H-protein in rabbit muscle. J. Muscle Res. Cell Motil. 7:1986;550-567.
    • (1986) J. Muscle Res. Cell Motil. , vol.7 , pp. 550-567
    • Bennett, P.1    Craig, R.2    Starr, R.3    Offer, G.4
  • 8
    • 15144351296 scopus 로고    scopus 로고
    • Conservation within the myosin motor domain: Implications for structure and function
    • Cope M. J. T., Whisstock J., Rayment I., Kendrick-Jones J. Conservation within the myosin motor domain: implications for structure and function. Structure. 4:1996;969-987.
    • (1996) Structure , vol.4 , pp. 969-987
    • Cope, M.J.T.1    Whisstock, J.2    Rayment, I.3    Kendrick-Jones, J.4
  • 10
    • 0030976860 scopus 로고    scopus 로고
    • The in vitro motility activity of β-cardiac myosin depends on the nature of the β-myosin heavy chain mutation in hypertrophic cardiomyopathy
    • Cuda G., Fananapazir L., Epstein N. D., Sellers J. R. The in vitro motility activity of β-cardiac myosin depends on the nature of the β-myosin heavy chain mutation in hypertrophic cardiomyopathy. J. Muscle Res. Cell Motil. 18:1997;275-283.
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 275-283
    • Cuda, G.1    Fananapazir, L.2    Epstein, N.D.3    Sellers, J.R.4
  • 11
    • 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., Fischman D. A. Localization of C-protein isoforms in chicken skeletal muscle: ultrastructural detection using monoclonal antibodies. J. Cell Biol. 98:1984;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
  • 12
    • 0025246301 scopus 로고
    • Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: An intracellular member of the immunoglobulin superfamily
    • Einheber S., Fischman D. A. Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: an intracellular member of the immunoglobulin superfamily. Proc. Natl Acad. Sci. USA. 87:1990;2157-2161.
    • (1990) Proc. Natl 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 of titin and myosin-binding protein C: Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • Freiburg A., Gautel M. A molecular map of the interactions of titin and myosin-binding protein C: implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur. J. Biochem. 235:1996;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 characteriza tion of a full length human cDNA
    • Fürst D. O., Vinkemeier U., Weber K. Mammalian skeletal muscle C-protein: purification from bovine muscle, binding to titin and the characteriza tion of a full length human cDNA. J. Cell Sci. 102:1992;769-778.
    • (1992) J. Cell Sci. , vol.102 , pp. 769-778
    • Fürst, D.O.1    Vinkemeier, U.2    Weber, K.3
  • 15
    • 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. 249:1988;709-714.
    • (1988) Biochem. J. , vol.249 , pp. 709-714
    • Garvey, J.L.1    Kranias, E.G.2    Solaro, R.J.3
  • 16
    • 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. 14:1995;1952-1960.
    • (1995) EMBO J. , vol.14 , pp. 1952-1960
    • Gautel, M.1    Zuffardi, O.2    Freiburg, A.3    Labeit, S.4
  • 17
    • 0029859276 scopus 로고    scopus 로고
    • The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers
    • Gautel M., Goulding D., Bullard B., Weber K., Fürst D. O. The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers. J. Cell Sci. 1996;2747-2754.
    • (1996) J. Cell Sci. , pp. 2747-2754
    • Gautel, M.1    Goulding, D.2    Bullard, B.3    Weber, K.4    Fürst, D.O.5
  • 18
    • 0345131725 scopus 로고    scopus 로고
    • Isoform transitions of the myosin-binding protein C family in developing human and mouse muscles: Lack of isoform transcomplementation in cardiac muscle
    • Gautel M., Fürst D. O., Cocco A., Schiaffino S. Isoform transitions of the myosin-binding protein C family in developing human and mouse muscles: lack of isoform transcomplementation in cardiac muscle. Circul. Res. 82:1998;124-129.
    • (1998) Circul. Res. , vol.82 , pp. 124-129
    • Gautel, M.1    Fürst, D.O.2    Cocco, A.3    Schiaffino, S.4
  • 19
    • 0344387350 scopus 로고
    • The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorpora tion into the A-band of striated muscle
    • Gilbert R., Kelly M. G., Mikawa T., Fischman D. A. The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorpora tion into the A-band of striated muscle. J. Cell Sci. 108:1995;1-11.
    • (1995) J. Cell Sci. , vol.108 , pp. 1-11
    • Gilbert, R.1    Kelly, M.G.2    Mikawa, T.3    Fischman, D.A.4
  • 20
    • 0032478543 scopus 로고    scopus 로고
    • Wag the tail: Structural dynamics of actomyosin
    • Goldman Y. E. Wag the tail: structural dynamics of actomyosin. Cell. 93:1998;1-4.
    • (1998) Cell , vol.93 , pp. 1-4
    • Goldman, Y.E.1
  • 22
    • 0021713707 scopus 로고
    • 2+-calmodulin-dependent protein kinases
    • 2+-calmodulin-dependent protein kinases. J. Biol. Chem. 259:1984;15587-15596.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15587-15596
    • Hartzell, H.C.1    Glass, D.B.2
  • 23
    • 0021911378 scopus 로고
    • Structure of C-protein purified from cardiac muscle
    • Hartzell H. C., Sale W. S. Structure of C-protein purified from cardiac muscle. J. Cell Biol. 100:1985;208-215.
    • (1985) J. Cell Biol. , vol.100 , pp. 208-215
    • Hartzell, H.C.1    Sale, W.S.2
  • 24
    • 0020074903 scopus 로고
    • Effects of cholinergic and adrenergic agonists on phosphorylation of 165,000-dalton myofibrillar protein in intact cardiac muscle
    • Hartzell H. C., Titus L. Effects of cholinergic and adrenergic agonists on phosphorylation of 165,000-dalton myofibrillar protein in intact cardiac muscle. J. Biol. Chem. 257:1982;2111-2120.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2111-2120
    • Hartzell, H.C.1    Titus, L.2
  • 25
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction. Interference microscopy of living muscle fibers
    • Huxley A. F., Niedergerke R. Structural changes in muscle during contraction. Interference microscopy of living muscle fibers. Nature. 173:1954;971-973.
    • (1954) Nature , vol.173 , pp. 971-973
    • Huxley, A.F.1    Niedergerke, R.2
  • 26
    • 36949093311 scopus 로고
    • Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation
    • Huxley H. E., Hanson J. Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature. 173:1954;973-976.
    • (1954) Nature , vol.173 , pp. 973-976
    • Huxley, H.E.1    Hanson, J.2
  • 27
    • 0019216704 scopus 로고
    • Phosphorylation of a myofibrillar protein of Mr 150000 in perfused rat heart, and the tentative identification of this as C-protein
    • Jeacocke S., England P. Phosphorylation of a myofibrillar protein of Mr 150000 in perfused rat heart, and the tentative identification of this as C-protein. FEBS Letters. 122:1980;129-132.
    • (1980) FEBS Letters , vol.122 , pp. 129-132
    • Jeacocke, S.1    England, P.2
  • 28
    • 0029913862 scopus 로고    scopus 로고
    • Dynamic behaviour of the head-tail junction of myosin
    • Knight P. J. Dynamic behaviour of the head-tail junction of myosin. J. Mol. Biol. 255:1996;269-274.
    • (1996) J. Mol. Biol. , vol.255 , pp. 269-274
    • Knight, P.J.1
  • 30
    • 0029837673 scopus 로고    scopus 로고
    • The intracompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of development expression as determined by double epitope-tagging competition
    • Komiyama M., Soldati T., von Arx P., Perriard J.-C. The intracompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of development expression as determined by double epitope-tagging competition. J. Cell Sci. 109:1996;2098-2099.
    • (1996) J. Cell Sci. , vol.109 , pp. 2098-2099
    • Komiyama, M.1    Soldati, T.2    Von Arx, P.3    Perriard, J.-C.4
  • 31
    • 0028824803 scopus 로고
    • Assembly of cardiac C-protein during myofibrillogenesis in myogenic cells in culture
    • Koshida S., Kurasawa M., Yasuda M., Sato N., Obinata T. Assembly of cardiac C-protein during myofibrillogenesis in myogenic cells in culture. Cell Struct. Funct. 20:1995;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
  • 32
    • 0026582867 scopus 로고
    • Towards a molecular understanding of titin
    • Labeit S., Gautel M., Lakey A., Trinick J. Towards a molecular understanding of titin. EMBO J. 11:1992;1711-1716.
    • (1992) EMBO J. , vol.11 , pp. 1711-1716
    • Labeit, S.1    Gautel, M.2    Lakey, A.3    Trinick, J.4
  • 33
    • 0030266484 scopus 로고    scopus 로고
    • Sensing the heat: The application of isothermal titration calorimetry to thermodynamic studies of biomeloceular interactions
    • Ladbury J. E., Chowdhry B. Z. Sensing the heat: the application of isothermal titration calorimetry to thermodynamic studies of biomeloceular interactions. Chem. Biol. 3:1996;791-801.
    • (1996) Chem. Biol. , vol.3 , pp. 791-801
    • Ladbury, J.E.1    Chowdhry, B.Z.2
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0032540229 scopus 로고    scopus 로고
    • The muscle thin filament as a classical cooperative/allosteric regulatory system
    • Lehrer S. S., Geeves M. A. The muscle thin filament as a classical cooperative/allosteric regulatory system. J. Mol. Biol. 277:1998;1081-1089.
    • (1998) J. Mol. Biol. , vol.277 , pp. 1081-1089
    • Lehrer, S.S.1    Geeves, M.A.2
  • 36
    • 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., Holtzer H. 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. 29:1994;1-19.
    • (1994) Cell Motil. Cytoskel. , 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
  • 37
    • 0019000664 scopus 로고
    • Identification of a region susceptible for proteolysis in myosin subfragment-2
    • Lu R. C. Identification of a region susceptible for proteolysis in myosin subfragment-2. Proc. Natl Acad. Sci. USA. 77:1980;2010-2013.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 2010-2013
    • Lu, R.C.1
  • 38
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian S. S., Lowey S. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85:1982;55-71.
    • (1982) Methods Enzymol. , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 40
    • 0016818769 scopus 로고
    • Interaction of C-protein with myosin, myosin rod and light meromyosin
    • Moos C., Offer G., Starr R., Bennet P. Interaction of C-protein with myosin, myosin rod and light meromyosin. J. Mol. Biol. 97:1975;1-9.
    • (1975) J. Mol. Biol. , vol.97 , pp. 1-9
    • Moos, C.1    Offer, G.2    Starr, R.3    Bennet, P.4
  • 41
    • 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. M., 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. 124:1978;571-586.
    • (1978) J. Mol. Biol. , vol.124 , pp. 571-586
    • Moos, C.1    Mason, C.M.2    Besterman, J.M.3    Feng, I.M.4    Dubin, J.H.5
  • 42
    • 0028839440 scopus 로고
    • The leucine zippers of the HLH-LZ proteins Max and c-Myc preferentially form heterodimers
    • Muhle-Goll C., Nilges M., Pastore A. The leucine zippers of the HLH-LZ proteins Max and c-Myc preferentially form heterodimers. Biochemistry. 34:1995;13554-13564.
    • (1995) Biochemistry , vol.34 , pp. 13554-13564
    • Muhle-Goll, C.1    Nilges, M.2    Pastore, A.3
  • 44
    • 0021340227 scopus 로고
    • Immunochemical analysis of C-protein isoform transitions during the development of chicken skeletal muscle
    • Obinata T., Reinach F. C., Bader D. M., Masaki T., Kitani S., Fischman D. A. Immunochemical analysis of C-protein isoform transitions during the development of chicken skeletal muscle. Dev. Biol. 101:1984;116-124.
    • (1984) Dev. Biol. , vol.101 , pp. 116-124
    • Obinata, T.1    Reinach, F.C.2    Bader, D.M.3    Masaki, T.4    Kitani, S.5    Fischman, D.A.6
  • 45
    • 0011019432 scopus 로고
    • C-protein and the periodicity in the thick filaments of vertebrate skeletal muscle
    • Offer G. C-protein and the periodicity in the thick filaments of vertebrate skeletal muscle. Cold Spring Harbor Symp. Quant. Biol. 37:1972;87-95.
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 87-95
    • Offer, G.1
  • 46
    • 0029870409 scopus 로고    scopus 로고
    • The structure of the head-tail junction of the myosin molecule
    • Offer G., Knight P. J. The structure of the head-tail junction of the myosin molecule. J. Mol. Biol. 256:1996;407-416.
    • (1996) J. Mol. Biol. , vol.256 , pp. 407-416
    • Offer, G.1    Knight, P.J.2
  • 47
    • 0015924821 scopus 로고
    • A new protein of the thick filaments. Extraction, purification, and characterization
    • Offer G., Moos C., Starr R. A new protein of the thick filaments. Extraction, purification, and characterization. J. Mol. Biol. 74:1973;653-676.
    • (1973) J. Mol. Biol. , vol.74 , pp. 653-676
    • Offer, G.1    Moos, C.2    Starr, R.3
  • 48
    • 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. 123:1993;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
  • 49
    • 0029024879 scopus 로고
    • Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy
    • Rayment L., Holden H., Sellers J., Fananapazir L., Epstein N. D. Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy. Proc. Natl Acad. Sci. USA. 92:1995;3864-3868.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3864-3868
    • Rayment, L.1    Holden, H.2    Sellers, J.3    Fananapazir, L.4    Epstein, N.D.5
  • 51
    • 0030852878 scopus 로고    scopus 로고
    • Novel splice donor site mutation in the cardiac myosin-binding protein-C gene in familial hypertrophic cardiomyopathy. characterization of transcript and protein
    • Rottbauer W., Gautel M., Zehelein J., Labeit S., Franz W. M., Grünig E., Brown B. D., Vollrath B., Mall G., Dietz R., Katus H. A. Novel splice donor site mutation in the cardiac myosin-binding protein-C gene in familial hypertrophic cardiomyopathy. characterization of transcript and protein. J. Clin. Invest. 100:1997;475-482.
    • (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    Grünig, E.6    Brown, B.D.7    Vollrath, B.8    Mall, G.9    Dietz, R.10    Katus, H.A.11
  • 52
    • 0025727168 scopus 로고
    • Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II
    • Schlender K. K., Bean L. J. Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 266:1991;2811-2817.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2811-2817
    • Schlender, K.K.1    Bean, L.J.2
  • 53
    • 0024232653 scopus 로고
    • Terminally differentiated neonatal rat myocardial cells proliferate and maintain specific differentiated functions following expression of SV 40 large T antigen
    • Sen A., Preston D., Henderson S. A., Gerard R. D., Chien K. R. Terminally differentiated neonatal rat myocardial cells proliferate and maintain specific differentiated functions following expression of SV 40 large T antigen. J. Biol. Chem. 35:1988;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
  • 54
    • 0027536473 scopus 로고
    • A survey of interactions made by the giant protein titin
    • Soteriou A., Gamage M., Trinick J. A survey of interactions made by the giant protein titin. J. Cell Sci. 104:1993;119-123.
    • (1993) J. Cell Sci. , vol.104 , pp. 119-123
    • Soteriou, A.1    Gamage, M.2    Trinick, J.3
  • 55
    • 0017826080 scopus 로고
    • The interaction of C-protein with heavy meromyosin and subfragment-2
    • Starr R., Offer G. The interaction of C-protein with heavy meromyosin and subfragment-2. Biochem. J. 171:1978;813-816.
    • (1978) Biochem. J. , vol.171 , pp. 813-816
    • Starr, R.1    Offer, G.2
  • 57
    • 0026769955 scopus 로고
    • Contraction characteristics and ATPase activity of skeletal muscle fibres in the presence of antibody to myosin subfragment 2
    • Sugi H., Kobayashi T., Gross T., Noguchi K., Karr T., Harrington W. F. Contraction characteristics and ATPase activity of skeletal muscle fibres in the presence of antibody to myosin subfragment 2. Proc. Natl Acad. Sci. USA. 89:1992;6134-6137.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6134-6137
    • Sugi, H.1    Kobayashi, T.2    Gross, T.3    Noguchi, K.4    Karr, T.5    Harrington, W.F.6
  • 58
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J. D., Higgins D. G., Gibson T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:1994;4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 60
    • 0032006681 scopus 로고    scopus 로고
    • The role of cytoskeletal proteins in cardiomyopathies
    • Towbin J. A. The role of cytoskeletal proteins in cardiomyopathies. Curr. Opin. Cell Biol. 10:1998;131-139.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 131-139
    • Towbin, J.A.1
  • 61
    • 0030046902 scopus 로고    scopus 로고
    • Contractile protein mutations and heart disease
    • Vikstrom K. L., Leinwand L. A. Contractile protein mutations and heart disease. Curr. Opin. Cell Biol. 8:1996;97-105.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 97-105
    • Vikstrom, K.L.1    Leinwand, L.A.2
  • 62
    • 0028265391 scopus 로고
    • Myosin mutations in hypertrophic cardiomyopathy and functional implications
    • Vosberg H.-P. Myosin mutations in hypertrophic cardiomyopathy and functional implications. Herz. 19:1994;75-83.
    • (1994) Herz , vol.19 , pp. 75-83
    • Vosberg, H.-P.1
  • 64
    • 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., Reinach F. C., Fischman D. A. 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. 16:1993;661-669.
    • (1993) Eur. J. Biochem. , vol.16 , pp. 661-669
    • Weber, F.E.1    Vaughan, K.T.2    Reinach, F.C.3    Fischman, D.A.4
  • 65
    • 0029812703 scopus 로고    scopus 로고
    • Alteration of myosin cross bridges by phosphorylation of myosin-bindig protein C in cardiac muscle
    • Weinberg A., Winegrad S. Alteration of myosin cross bridges by phosphorylation of myosin-bindig protein C in cardiac muscle. Proc. Natl Acad. Sci. USA. 93:1996;8999-9003.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8999-9003
    • Weinberg, A.1    Winegrad, S.2
  • 66
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T., Williston S., Brandts J. F., Lin L.-N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179:1989;131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 67
    • 0020522788 scopus 로고
    • The C-proteins of rabbit red, white and cardiac muscles
    • Yamamoto K., Moos C. The C-proteins of rabbit red, white and cardiac muscles. J. Biol. Chem. 258:1983;8395-8401.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8395-8401
    • Yamamoto, K.1    Moos, C.2
  • 68
    • 0028808791 scopus 로고
    • Complete primary structure of chicken cardiac C-protein (MyBP-C) its expression in developing striated muscles
    • Yasuda M., Koshida S., Sato N., Obinata T. Complete primary structure of chicken cardiac C-protein (MyBP-C) its expression in developing striated muscles. J. Mol. Cell Cardiol. 27:1995;2275-2286.
    • (1995) J. Mol. Cell Cardiol. , vol.27 , pp. 2275-2286
    • Yasuda, M.1    Koshida, S.2    Sato, N.3    Obinata, T.4
  • 69
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of α-actinin
    • Young P., Ferguson C., Ba ñ S., Cautel M. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of α-actinin. EMBO J. 17:1998;1614-1624.
    • (1998) EMBO J. , vol.17 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Ba Ñ., S.3    Cautel, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.