메뉴 건너뛰기




Volumn 58, Issue , 1996, Pages 447-481

Thin filament-mediated regulation of cardiac contraction

Author keywords

actin; cooperativity; muscle proteins; tropomyosin; troponin

Indexed keywords

ACTIN; DNA BINDING PROTEIN; TROPOMYOSIN; TROPONIN C; TROPONIN I; TROPONIN T;

EID: 0030004861     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.ph.58.030196.002311     Document Type: Review
Times cited : (467)

References (211)
  • 2
    • 0026683429 scopus 로고
    • 2+-dependence of structural changes in troponin-C in demembranated fibers of rabbit psoas muscle
    • 2+-dependence of structural changes in troponin-C in demembranated fibers of rabbit psoas muscle. Biophys. J. 61:399-409
    • (1992) Biophys. J. , vol.61 , pp. 399-409
    • Allen, T.S.1    Yates, L.D.2    Gordon, A.M.3
  • 4
    • 0023664393 scopus 로고
    • The control of myocardial contraction with skeletal fast muscle troponin C
    • Babu A, Scordilis SP, Sonnenblick EH, Gulati J. 1987. The control of myocardial contraction with skeletal fast muscle troponin C. J. Biol. Chem. 262:5815-22
    • (1987) J. Biol. Chem. , vol.262 , pp. 5815-5822
    • Babu, A.1    Scordilis, S.P.2    Sonnenblick, E.H.3    Gulati, J.4
  • 6
    • 0025761629 scopus 로고
    • Cross-helix separation of tropomyosin molecules in acto-tropomyosin as determined by neutron scattering
    • Bivin DB, Stone DB, Schneider DK, Mendelson RA. 1991. Cross-helix separation of tropomyosin molecules in acto-tropomyosin as determined by neutron scattering. Biophys. J. 59:880-88
    • (1991) Biophys. J. , vol.59 , pp. 880-888
    • Bivin, D.B.1    Stone, D.B.2    Schneider, D.K.3    Mendelson, R.A.4
  • 7
    • 0023187156 scopus 로고
    • Cooperative interactions between troponin-tropomyosin units that extend the length of the thin filament in skeletal muscle
    • Brandt PW, Diamond MS, Rutchik JS, Schachat FH. 1987. Cooperative interactions between troponin-tropomyosin units that extend the length of the thin filament in skeletal muscle. J. Mol. Biol. 195:885-96
    • (1987) J. Mol. Biol. , vol.195 , pp. 885-896
    • Brandt, P.W.1    Diamond, M.S.2    Rutchik, J.S.3    Schachat, F.H.4
  • 8
    • 0021755958 scopus 로고
    • The thin filament of vertebrate skeletal muscle co-operatively activates as a unit
    • Brandt PW, Diamond MS, Schachat FH. 1984. The thin filament of vertebrate skeletal muscle co-operatively activates as a unit. J. Mol. Biol. 180:379-84
    • (1984) J. Mol. Biol. , vol.180 , pp. 379-384
    • Brandt, P.W.1    Diamond, M.S.2    Schachat, F.H.3
  • 9
    • 0000147671 scopus 로고
    • Manifestations of cooperative behavior in the regulated actin filament during actin-activated ATP hydrolysis in the presence of calcium
    • Bremel RD, Murray JM, Weber A. 1972. Manifestations of cooperative behavior in the regulated actin filament during actin-activated ATP hydrolysis in the presence of calcium. Cold Spring Harbor Symp. Quant. Biol. 37:267-75
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 267-275
    • Bremel, R.D.1    Murray, J.M.2    Weber, A.3
  • 10
    • 0015525066 scopus 로고
    • Cooperation within actin filament in vertebrate skeletal muscle
    • Bremel RD, Weber A. 1972. Cooperation within actin filament in vertebrate skeletal muscle. Nature New Biol. 238:97-101
    • (1972) Nature New Biol. , vol.238 , pp. 97-101
    • Bremel, R.D.1    Weber, A.2
  • 11
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc. Natl. Acad. Sci. USA 85:3265-69
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 12
    • 0027434034 scopus 로고
    • Calcium plays distinctive structural roles in the N- and C-terminal domains of cardiac troponin C
    • Brito RM, Krudy GA, Negele JC, Rosevear PR. 1993. Calcium plays distinctive structural roles in the N- and C-terminal domains of cardiac troponin C. J. Biol. Chem. 268:20966-73
    • (1993) J. Biol. Chem. , vol.268 , pp. 20966-20973
    • Brito, R.M.1    Krudy, G.A.2    Negele, J.C.3    Rosevear, P.R.4
  • 13
    • 0025840596 scopus 로고
    • Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II
    • Brito RM, Putkey JA, Strynadka NCJ, James MNG, Rosevear PR. 1991. Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II. Biochemistry 30:10236-45
    • (1991) Biochemistry , vol.30 , pp. 10236-10245
    • Brito, R.M.1    Putkey, J.A.2    Strynadka, N.C.J.3    James, M.N.G.4    Rosevear, P.R.5
  • 14
    • 0027240526 scopus 로고
    • Cooperative Interactions between adjacent troponin-tropomyosin complexes may be transmitted through the thin filament
    • Butters CA, Willadsen KA, Tobacman LS. 1993. Cooperative Interactions between adjacent troponin-tropomyosin complexes may be transmitted through the thin filament. J. Biol. Chem. 268:15565-70
    • (1993) J. Biol. Chem. , vol.268 , pp. 15565-15570
    • Butters, C.A.1    Willadsen, K.A.2    Tobacman, L.S.3
  • 16
    • 0026410049 scopus 로고
    • Interaction of troponin I and troponin C. Use of the two-dimensional nuclear magnetic resonance transferred nuclear Overhauser effect to determine the structure of the inhibitory peptide when bound to skeletal troponin C
    • Campbell AP, Sykes BD. 1991. Interaction of troponin I and troponin C. Use of the two-dimensional nuclear magnetic resonance transferred nuclear Overhauser effect to determine the structure of the inhibitory peptide when bound to skeletal troponin C. J. Mol. Biol. 222:405-21
    • (1991) J. Mol. Biol. , vol.222 , pp. 405-421
    • Campbell, A.P.1    Sykes, B.D.2
  • 17
    • 0026470719 scopus 로고
    • Interaction of troponin I and troponin C: Use of the two-dimensional transferred nuclear Overhauser effect to determine the structure of a Gly-110 peptide analog when bound to cardiac troponin C
    • Campbell AP, Van Eyk JE, Hodges RS, Sykes BD. 1992. Interaction of troponin I and troponin C: use of the two-dimensional transferred nuclear Overhauser effect to determine the structure of a Gly-110 peptide analog when bound to cardiac troponin C. Biochim. Biophys. Acta 1160:35-54
    • (1992) Biochim. Biophys. Acta , vol.1160 , pp. 35-54
    • Campbell, A.P.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 18
    • 0027509324 scopus 로고
    • Subsarcomeric distribution of calcium in demembranated fibers of rabbit psoas muscle
    • Cantino ME, Allen TS, Gordon AM. 1993. Subsarcomeric distribution of calcium in demembranated fibers of rabbit psoas muscle. Biophys. J. 64:211-22
    • (1993) Biophys. J. , vol.64 , pp. 211-222
    • Cantino, M.E.1    Allen, T.S.2    Gordon, A.M.3
  • 19
    • 0025970527 scopus 로고
    • Actin: Protein structure and filament dynamics
    • Carlier M-F. 1991. Actin: protein structure and filament dynamics. J. Biol. Chem. 266:1-4
    • (1991) J. Biol. Chem. , vol.266 , pp. 1-4
    • Carlier, M.-F.1
  • 20
    • 0027093717 scopus 로고
    • Actin mediated regulation of muscle contraction
    • Chalovich JM. 1992. Actin mediated regulation of muscle contraction. Pharmacol. Ther. 55:95-148
    • (1992) Pharmacol. Ther. , vol.55 , pp. 95-148
    • Chalovich, J.M.1
  • 21
    • 0019977525 scopus 로고
    • Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin
    • Chalovich JM, Eisenberg E. 1982. Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin. J. Biol. Chem. 257:2432-37
    • (1982) J. Biol. Chem. , vol.257 , pp. 2432-2437
    • Chalovich, J.M.1    Eisenberg, E.2
  • 22
    • 0028176943 scopus 로고
    • 2+, and troponin I inhibitory peptide binding to a Phe-154 to Trp mutant of chicken skeletal muscle troponin C
    • 2+, and troponin I inhibitory peptide binding to a Phe-154 to Trp mutant of chicken skeletal muscle troponin C. Biochemistry 33:2961-69
    • (1994) Biochemistry , vol.33 , pp. 2961-2969
    • Chandra, M.1    McCubbin, W.D.2    Oikawa, K.3    Kay, C.M.4    Smillie, L.B.5
  • 23
    • 0027385362 scopus 로고
    • Yeast actin with a mutation in the "hydrophobic plug" between subdomains 3 and 4 (L266D) displays a cold-sensitive polymerization defect
    • Chen X, Cook RK, Rubenstein P. 1993. Yeast actin with a mutation in the "hydrophobic plug" between subdomains 3 and 4 (L266D) displays a cold-sensitive polymerization defect. J. Cell Biol. 123:1185-95
    • (1993) J. Cell Biol. , vol.123 , pp. 1185-1195
    • Chen, X.1    Cook, R.K.2    Rubenstein, P.3
  • 24
    • 0023648329 scopus 로고
    • Interactions of troponin subunits: Free energy of binary and ternary complexes
    • Cheung HC, Wang CK, Malik NA. 1987. Interactions of troponin subunits: free energy of binary and ternary complexes. Biochemistry 26:5904-7
    • (1987) Biochemistry , vol.26 , pp. 5904-5907
    • Cheung, H.C.1    Wang, C.K.2    Malik, N.A.3
  • 25
    • 0025787595 scopus 로고
    • Relationship between alternatively spliced exons and functional domains in tropomyosin
    • Cho Y-J, Hitchcock-DeGregori SE. 1990. Relationship between alternatively spliced exons and functional domains in tropomyosin. Proc. Natl. Acad. Sci. USA 88:10153-57
    • (1990) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10153-10157
    • Cho, Y.-J.1    Hitchcock-DeGregori, S.E.2
  • 26
    • 0025105127 scopus 로고
    • The amino terminus of tropomyosin is a major determinant for function
    • Cho Y-J, Liu J, Hitchcock-DeGregori SE. 1990. The amino terminus of tropomyosin is a major determinant for function. J. Biol. Chem. 265:545
    • (1990) J. Biol. Chem. , vol.265 , pp. 545
    • Cho, Y.-J.1    Liu, J.2    Hitchcock-DeGregori, S.E.3
  • 27
    • 0020478670 scopus 로고
    • Proximity of sulfhydryl groups to the sites of interaction between components of the troponin complex from rabbit skeletal muscle
    • Chong PCS, Hodges RS. 1982. Proximity of sulfhydryl groups to the sites of interaction between components of the troponin complex from rabbit skeletal muscle. J. Biol. Chem. 257:2549-55
    • (1982) J. Biol. Chem. , vol.257 , pp. 2549-2555
    • Chong, P.C.S.1    Hodges, R.S.2
  • 28
    • 0020380464 scopus 로고
    • Photochemical cross-linking between rabbit skeletal troponin subunits. Troponin I-troponin T interactions
    • Chong PCS, Hodges RS. 1982. Photochemical cross-linking between rabbit skeletal troponin subunits. Troponin I-troponin T interactions. J. Biol. Chem. 257:11667-72
    • (1982) J. Biol. Chem. , vol.257 , pp. 11667-11672
    • Chong, P.C.S.1    Hodges, R.S.2
  • 29
    • 0028044116 scopus 로고
    • Equilibrium linkage analysis of cardiac thin filament assembly. Implications for the regulation of muscle contraction
    • Dahiya R, Butters CA, Tobacman LS. 1994. Equilibrium linkage analysis of cardiac thin filament assembly. Implications for the regulation of muscle contraction. J. Biol. Chem. 269:29457-61
    • (1994) J. Biol. Chem. , vol.269 , pp. 29457-29461
    • Dahiya, R.1    Butters, C.A.2    Tobacman, L.S.3
  • 31
    • 0027340391 scopus 로고
    • 2+ binding activity in mutated EF-hands of cardiac troponin C
    • 2+ binding activity in mutated EF-hands of cardiac troponin C. J. Biol. Chem. 268:24067-73
    • (1993) J. Biol. Chem. , vol.268 , pp. 24067-24073
    • Dotson, D.G.1    Putkey, J.A.2
  • 34
    • 0022378036 scopus 로고
    • Calcium-insensitive binding of heavy meromyosin to regulated actin at physiological ionic strength
    • El-Saleh SC, Potter JD. 1985. Calcium-insensitive binding of heavy meromyosin to regulated actin at physiological ionic strength. J. Biol. Chem. 260:14775-79
    • (1985) J. Biol. Chem. , vol.260 , pp. 14775-14779
    • El-Saleh, S.C.1    Potter, J.D.2
  • 35
    • 0017885455 scopus 로고
    • Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiac and skeletal muscles
    • Fabiato A, Fabiato F. 1978. Effects of pH on the myofilaments and the sarcoplasmic reticulum of skinned cells from cardiac and skeletal muscles. J. Physiol. 276:233-55
    • (1978) J. Physiol. , vol.276 , pp. 233-255
    • Fabiato, A.1    Fabiato, F.2
  • 38
    • 0020475827 scopus 로고
    • Troponin and its interactions with tropomyosin: An electron microscope study
    • Flicker PF, Phillips JGN, Cohen C. 1982. Troponin and its interactions with tropomyosin: an electron microscope study. J. Mol. Biol 162:495-501
    • (1982) J. Mol. Biol , vol.162 , pp. 495-501
    • Flicker, P.F.1    Phillips, J.G.N.2    Cohen, C.3
  • 39
    • 0026319614 scopus 로고
    • 2+-troponin C affinity in skeletal muscle
    • 2+-troponin C affinity in skeletal muscle. Am. J. Physiol. 261:C787-92
    • (1991) Am. J. Physiol. , vol.261
    • Fuchs, F.1    Wang, Y.P.2
  • 40
    • 0025270821 scopus 로고
    • Probing the calcium-induced conformational transition of troponin C with site-directed mutants
    • Fujimori K, Sorenson M, Herzberg O, Moult J, Reinach FC. 1990. Probing the calcium-induced conformational transition of troponin C with site-directed mutants. Nature 345:182-84
    • (1990) Nature , vol.345 , pp. 182-184
    • Fujimori, K.1    Sorenson, M.2    Herzberg, O.3    Moult, J.4    Reinach, F.C.5
  • 41
    • 0026343598 scopus 로고
    • Complete coding sequences of cDNAs of four variants of rabbit skeletal muscle troponin T
    • Fujita S, Maeda K, Maeda Y. 1991. Complete coding sequences of cDNAs of four variants of rabbit skeletal muscle troponin T. J. Muscle Res. Cell Motil. 12:560-65
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 560-565
    • Fujita, S.1    Maeda, K.2    Maeda, Y.3
  • 42
    • 0028670746 scopus 로고
    • Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C
    • Gangé SM, Tsuda S, Li MX, Chandra M, Smillie LB, Sykes BD. 1994. Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C. Protein Sci. 3:1961-74
    • (1994) Protein Sci. , vol.3 , pp. 1961-1974
    • Gangé, S.M.1    Tsuda, S.2    Li, M.X.3    Chandra, M.4    Smillie, L.B.5    Sykes, B.D.6
  • 43
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit
    • Geeves MA, Lehrer SS. 1994. Dynamics of the muscle thin filament regulatory switch: the size of the cooperative unit. Biophys. J. 67:273-82
    • (1994) Biophys. J. , vol.67 , pp. 273-282
    • Geeves, M.A.1    Lehrer, S.S.2
  • 44
    • 0027515534 scopus 로고
    • Cross-bridges affect both TnC structure and calcium affinity in muscle fibers
    • Gordon AM, Ridgway EB. 1993. Cross-bridges affect both TnC structure and calcium affinity in muscle fibers. Adv. Exp. Med. Biol. 332:183-94
    • (1993) Adv. Exp. Med. Biol. , vol.332 , pp. 183-194
    • Gordon, A.M.1    Ridgway, E.B.2
  • 45
    • 0019768628 scopus 로고
    • Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity
    • Grabarek Z, Drabikowski W, Leavis PC, Rosenfeld SS, Gergely J. 1981. Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity. J. Biol. Chem. 256:13121-27
    • (1981) J. Biol. Chem. , vol.256 , pp. 13121-13127
    • Grabarek, Z.1    Drabikowski, W.2    Leavis, P.C.3    Rosenfeld, S.S.4    Gergely, J.5
  • 47
    • 0022606964 scopus 로고
    • Calcium binding to the low affinity sites in troponin C induces conformational changes in the high affinity domain: A possible route of information transfer in activation of muscle contraction
    • Grabarek Z, Leavis PC, Gergely J. 1986. Calcium binding to the low affinity sites in troponin C induces conformational changes in the high affinity domain: a possible route of information transfer in activation of muscle contraction. J. Biol. Chem. 261:608-13
    • (1986) J. Biol. Chem. , vol.261 , pp. 608-613
    • Grabarek, Z.1    Leavis, P.C.2    Gergely, J.3
  • 48
    • 0025271923 scopus 로고
    • Inhibition of mutant troponin C activity by an infra-domain disulfide bond
    • Grabarek Z, Tan R-Y, Wang J, Tao T, Gergely J. 1990. Inhibition of mutant troponin C activity by an infra-domain disulfide bond. Nature 345:132-35
    • (1990) Nature , vol.345 , pp. 132-135
    • Grabarek, Z.1    Tan, R.-Y.2    Wang, J.3    Tao, T.4    Gergely, J.5
  • 49
    • 0017180839 scopus 로고
    • The amino acid sequence of rabbit cardiac troponin I
    • Grand RJA, Wilkinson JM, Mole LE. 1976. The amino acid sequence of rabbit cardiac troponin I. Biochem. J. 159:633-41
    • (1976) Biochem. J. , vol.159 , pp. 633-641
    • Grand, R.J.A.1    Wilkinson, J.M.2    Mole, L.E.3
  • 50
    • 0015218120 scopus 로고
    • Reconstitution of troponin activity from three protein components
    • Greaser ML, Gergely J. 1971. Reconstitution of troponin activity from three protein components. J. Biol. Chem. 246:4226-33
    • (1971) J. Biol. Chem. , vol.246 , pp. 4226-4233
    • Greaser, M.L.1    Gergely, J.2
  • 51
    • 0015935352 scopus 로고
    • Purification and properties of the components from troponin
    • Greaser ML, Gergely J. 1973. Purification and properties of the components from troponin. J. Biol. Chem. 248:2125-33
    • (1973) J. Biol. Chem. , vol.248 , pp. 2125-2133
    • Greaser, M.L.1    Gergely, J.2
  • 52
    • 0020479910 scopus 로고
    • The effect of nucleotide on the binding of myosin subfragment 1 to regulated actin
    • Greene LE. 1982. The effect of nucleotide on the binding of myosin subfragment 1 to regulated actin. J. Biol. Chem. 257:13993-99
    • (1982) J. Biol. Chem. , vol.257 , pp. 13993-13999
    • Greene, L.E.1
  • 53
    • 0022624185 scopus 로고
    • Cooperative binding of myosin subfragment 1 to regulated actin as measured by fluorescence changes of troponin I modified with different fluorophores
    • Greene LE. 1986. Cooperative binding of myosin subfragment 1 to regulated actin as measured by fluorescence changes of troponin I modified with different fluorophores. J. Biol. Chem. 261:1279-85
    • (1986) J. Biol. Chem. , vol.261 , pp. 1279-1285
    • Greene, L.E.1
  • 54
    • 0019013686 scopus 로고
    • Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex
    • Greene LE, Eisenberg E. 1980. Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc. Natl. Acad. Sci. USA 77:2616-20
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2616-2620
    • Greene, L.E.1    Eisenberg, E.2
  • 55
    • 0023238920 scopus 로고
    • Regulation of actomyosin ATPase activity by troponin-tropomyosin: Effect of the binding of the myosin subfragment 1 (S-1)-ATP complex
    • Greene LE, Williams DL, Eisenberg E. 1987. Regulation of actomyosin ATPase activity by troponin-tropomyosin: effect of the binding of the myosin subfragment 1 (S-1)-ATP complex. Proc. Natl. Acad. Sci. USA 84:3102-6
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3102-3106
    • Greene, L.E.1    Williams, D.L.2    Eisenberg, E.3
  • 56
    • 0026455168 scopus 로고
    • 2+-deficient EF-hand in cardiac muscle, with genetically engineered cardiac-skeletal chimeric troponin C
    • 2+-deficient EF-hand in cardiac muscle, with genetically engineered cardiac-skeletal chimeric troponin C. J. Biol. Chem. 267:25073-77
    • (1992) J. Biol. Chem. , vol.267 , pp. 25073-25077
    • Gulati, J.1    Babu, A.2    Su, H.3
  • 58
    • 0023645610 scopus 로고
    • 2+-specific regulatory sites in skinned rabbit psoas fibers
    • 2+-specific regulatory sites in skinned rabbit psoas fibers. J. Biol. Chem. 262:13627-35
    • (1987) J. Biol. Chem. , vol.262 , pp. 13627-13635
    • Guth, K.1    Potter, J.D.2
  • 59
    • 0000733783 scopus 로고
    • X-ray evidence for a conformational change in the actin containing filaments of vertebrate striated muscle
    • Haselgrove JC. 1972. X-ray evidence for a conformational change in the actin containing filaments of vertebrate striated muscle. Cold Spring Harbor Symp. Quant. Biol. 37:341-52
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 341-352
    • Haselgrove, J.C.1
  • 60
    • 0028887715 scopus 로고
    • Characterization of the blocked and closed states of muscle thin filaments
    • Head JG, Ritchie MD, Geeves MA. 1995. Characterization of the blocked and closed states of muscle thin filaments. Eur. J. Biochem. 227:694-99
    • (1995) Eur. J. Biochem. , vol.227 , pp. 694-699
    • Head, J.G.1    Ritchie, M.D.2    Geeves, M.A.3
  • 61
    • 0023886229 scopus 로고
    • The structure of the amino terminus of tropomyosin is critical for binding to actin in the absence and presence of troponin
    • Heald RW, Hitchcock-DeGregori SE. 1988. The structure of the amino terminus of tropomyosin is critical for binding to actin in the absence and presence of troponin. J. Biol. Chem. 263:5254-59
    • (1988) J. Biol. Chem. , vol.263 , pp. 5254-5259
    • Heald, R.W.1    Hitchcock-DeGregori, S.E.2
  • 62
    • 0023664677 scopus 로고
    • The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin I and troponin C
    • Heeley DH, Golosinska K, Smillie LB. 1987. The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin I and troponin C. J. Biol. Chem. 262:9971-78
    • (1987) J. Biol. Chem. , vol.262 , pp. 9971-9978
    • Heeley, D.H.1    Golosinska, K.2    Smillie, L.B.3
  • 63
    • 0023733230 scopus 로고
    • Interaction of rabbit skeletal muscle troponin T and F-actin at physiological ionic strength
    • Heeley DH, Smillie LB. 1988. Interaction of rabbit skeletal muscle troponin T and F-actin at physiological ionic strength. Biochemistry 27:8227-32
    • (1988) Biochemistry , vol.27 , pp. 8227-8232
    • Heeley, D.H.1    Smillie, L.B.2
  • 64
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution
    • Herzberg O, James MNG. 1985. Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution. Nature 313:653-59
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.G.2
  • 65
    • 0022931544 scopus 로고
    • 2+-induced conformational transition of troponin C. A trigger for muscle contraction
    • 2+-induced conformational transition of troponin C. A trigger for muscle contraction. J. Biol. Chem. 261:2638-44
    • (1986) J. Biol. Chem. , vol.261 , pp. 2638-2644
    • Herzberg, O.1    Moult, J.2    James, M.N.G.3
  • 66
    • 0026672241 scopus 로고
    • Analysis of troponin-tropomyosin binding to actin. Troponin does not promote interactions between tropomyosin molecules
    • Hill LE, Mehegan JP, Butters CA, Tobacman LS. 1992. Analysis of troponin-tropomyosin binding to actin. Troponin does not promote interactions between tropomyosin molecules. J. Biol. Chem. 267:16106-13
    • (1992) J. Biol. Chem. , vol.267 , pp. 16106-16113
    • Hill, L.E.1    Mehegan, J.P.2    Butters, C.A.3    Tobacman, L.S.4
  • 67
    • 0021087754 scopus 로고
    • Two elementary models for the regulation of skeletal muscle contraction by calcium
    • Hill TL. 1983. Two elementary models for the regulation of skeletal muscle contraction by calcium. Biophys. J. 44:383-96
    • (1983) Biophys. J. , vol.44 , pp. 383-396
    • Hill, T.L.1
  • 69
    • 0019031856 scopus 로고
    • Theoretical model for cooperative equilibrium binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex
    • Hill TL, Eisenberg E, Greene LE. 1980. Theoretical model for cooperative equilibrium binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc. Natl. Acad. Sci. USA 77:3186-90
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3186-3190
    • Hill, T.L.1    Eisenberg, E.2    Greene, L.E.3
  • 70
    • 0020669295 scopus 로고
    • Alternate model for the cooperative equilibrium binding of the myosin subfragment-1-nucleotide complex to actin-troponin-tropomyosin
    • Hill TL, Eisenberg E, Greene LE. 1993. Alternate model for the cooperative equilibrium binding of the myosin subfragment-1-nucleotide complex to actin-troponin-tropomyosin. Proc. Natl. Acad. Sci. USA 80:60-64
    • (1993) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 60-64
    • Hill, T.L.1    Eisenberg, E.2    Greene, L.E.3
  • 71
    • 0018142608 scopus 로고
    • Calcium-binding properties of cardiac and skeletal troponin C as determined by circular dichroism and ultraviolet difference spectroscopy
    • Hincke MT, McCubbin WD, Kay CM. 1978. Calcium-binding properties of cardiac and skeletal troponin C as determined by circular dichroism and ultraviolet difference spectroscopy. Can. J. Biochem. 56:384-95
    • (1978) Can. J. Biochem. , vol.56 , pp. 384-395
    • Hincke, M.T.1    McCubbin, W.D.2    Kay, C.M.3
  • 72
    • 0016610748 scopus 로고
    • Regulation of muscle contraction: Binding of troponin and its components to actin and tropomyosin
    • Hitchcock SE. 1975. Regulation of muscle contraction: binding of troponin and its components to actin and tropomyosin. Eur. J. Biochem. 52:255-63
    • (1975) Eur. J. Biochem. , vol.52 , pp. 255-263
    • Hitchcock, S.E.1
  • 73
    • 0015899936 scopus 로고
    • Calcium sensitive binding of troponin to actin-tropomyosin: A two-site model for troponin action
    • Hitchcock SE, Huxley HE, Szent-Gyorgyi AG. 1973. Calcium sensitive binding of troponin to actin-tropomyosin: a two-site model for troponin action. J. Mol. Biol. 80:825-36
    • (1973) J. Mol. Biol. , vol.80 , pp. 825-836
    • Hitchcock, S.E.1    Huxley, H.E.2    Szent-Gyorgyi, A.G.3
  • 74
    • 0019887810 scopus 로고
    • Study of the structure of troponin-T by measuring the relative reactivities of lysines with acetic anhydride
    • Hitchcock SE, Zimmerman CJ, Smalley C. 1981. Study of the structure of troponin-T by measuring the relative reactivities of lysines with acetic anhydride. J. Mol. Biol. 147:125-51
    • (1981) J. Mol. Biol. , vol.147 , pp. 125-151
    • Hitchcock, S.E.1    Zimmerman, C.J.2    Smalley, C.3
  • 75
    • 0020479286 scopus 로고
    • Study of the structure of troponin-I by measuring the relative reactivities of lysines with acetic anhydride
    • Hitchcock-DeGregori SE. 1982. Study of the structure of troponin-I by measuring the relative reactivities of lysines with acetic anhydride. J. Biol. Chem. 257:7372-80
    • (1982) J. Biol. Chem. , vol.257 , pp. 7372-7380
    • Hitchcock-DeGregori, S.E.1
  • 76
    • 0023655442 scopus 로고
    • Altered actin and troponin-binding of amino-terminal variants of chicken striated muscle α-tropomyosin expressed in Escherichia coli
    • Hitchcock-DeGregori SE, Heald RW. 1987. Altered actin and troponin-binding of amino-terminal variants of chicken striated muscle α-tropomyosin expressed in Escherichia coli. J. Biol. Chem. 262:9730-35
    • (1987) J. Biol. Chem. , vol.262 , pp. 9730-9735
    • Hitchcock-DeGregori, S.E.1    Heald, R.W.2
  • 77
    • 0025153066 scopus 로고
    • Tropomyosin has discrete actin-binding sites with sevenfold and four-teenfold periodicities
    • Hitchcock-DeGregori SE, Varnell TA. 1990. Tropomyosin has discrete actin-binding sites with sevenfold and four-teenfold periodicities. J. Mol. Biol. 214:885-96
    • (1990) J. Mol. Biol. , vol.214 , pp. 885-896
    • Hitchcock-DeGregori, S.E.1    Varnell, T.A.2
  • 78
    • 0023488538 scopus 로고
    • Evidence for a force-dependent component of calcium binding to cardiac troponin C
    • Hoffman PA, Fuchs F. 1987. Evidence for a force-dependent component of calcium binding to cardiac troponin C. Am. J. Physiol. 253:C541-46
    • (1987) Am. J. Physiol. , vol.253
    • Hoffman, P.A.1    Fuchs, F.2
  • 79
    • 0026579874 scopus 로고
    • Effects of calcium on shortening velocity in frog chemically skinned atrial myocytes and in mechanically disrupted ventricular myocardiaum from rat
    • Hoffman PA, Moss RL. 1992. Effects of calcium on shortening velocity in frog chemically skinned atrial myocytes and in mechanically disrupted ventricular myocardiaum from rat. Circ. Res. 70:885-92
    • (1992) Circ. Res. , vol.70 , pp. 885-892
    • Hoffman, P.A.1    Moss, R.L.2
  • 80
    • 0028954281 scopus 로고
    • The actomyosin interaction and its control by tropomyosin
    • Holmes KC. 1995. The actomyosin interaction and its control by tropomyosin. Biophys. J. 68:2s-7s
    • (1995) Biophys. J. , vol.68
    • Holmes, K.C.1
  • 82
    • 0019293605 scopus 로고
    • The calcium and magnesium binding sites on cardiac troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Holroyde MJ, Robertson SP, Johnson JD, Solaro RJ, Potter JD. 1980. The calcium and magnesium binding sites on cardiac troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 255:11688-93
    • (1980) J. Biol. Chem. , vol.255 , pp. 11688-11693
    • Holroyde, M.J.1    Robertson, S.P.2    Johnson, J.D.3    Solaro, R.J.4    Potter, J.D.5
  • 83
    • 0000244537 scopus 로고
    • Structural changes in the actin and myosin containing filaments during contraction
    • Huxley HE. 1972. Structural changes in the actin and myosin containing filaments during contraction. Cold Spring Harbor Symp. Quant. Biol. 37:361-76
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 85
    • 0023821821 scopus 로고
    • 2+ and subunit interactions on surface accessibility of cysteine residues in cardiac troponin
    • 2+ and subunit interactions on surface accessibility of cysteine residues in cardiac troponin. Biochemistry 27:5891-98
    • (1988) Biochemistry , vol.27 , pp. 5891-5898
    • Ingraham, R.H.1    Hodges, R.S.2
  • 86
    • 0021194790 scopus 로고
    • Binary interactions of troponin subunits
    • Ingraham RH, Swenson CA. 1984. Binary interactions of troponin subunits. J. Biol. Chem. 259:9544-88
    • (1984) J. Biol. Chem. , vol.259 , pp. 9544-9588
    • Ingraham, R.H.1    Swenson, C.A.2
  • 87
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • Isambert H, Venier P, Maggs AC, Fattoum A, Kassab R, et al. 1995. Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J. Biol. Chem. 270:11437-44
    • (1995) J. Biol. Chem. , vol.270 , pp. 11437-11444
    • Isambert, H.1    Venier, P.2    Maggs, A.C.3    Fattoum, A.4    Kassab, R.5
  • 88
    • 0025176817 scopus 로고
    • Excimer fluorescence of pyrenyliodoacetamide-labeled tropomyosin: A probe of the state of tropomyosin in reconstituted muscle thin filaments
    • Ishii Y, Lehrer SS. 1990. Excimer fluorescence of pyrenyliodoacetamide-labeled tropomyosin: a probe of the state of tropomyosin in reconstituted muscle thin filaments. Biochemistry 29:1160-66
    • (1990) Biochemistry , vol.29 , pp. 1160-1166
    • Ishii, Y.1    Lehrer, S.S.2
  • 89
    • 0016772481 scopus 로고
    • The primary structure of troponin T and the interaction with tropomyosin
    • Jackson P, Amphlett GN, Perry SV. 1975. The primary structure of troponin T and the interaction with tropomyosin. Biochem. J. 151:85-97
    • (1975) Biochem. J. , vol.151 , pp. 85-97
    • Jackson, P.1    Amphlett, G.N.2    Perry, S.V.3
  • 91
    • 0028141866 scopus 로고
    • Structure of the troponin complex. Implications of photocross-linking of troponin I to troponin C thiol mutants
    • Kobayashi T, Tao T, Gergely J, Collins JH. 1994. Structure of the troponin complex. Implications of photocross-linking of troponin I to troponin C thiol mutants. J. Biol. Chem. 269:5725-29
    • (1994) J. Biol. Chem. , vol.269 , pp. 5725-5729
    • Kobayashi, T.1    Tao, T.2    Gergely, J.3    Collins, J.H.4
  • 92
    • 0025911961 scopus 로고
    • Cross-linking of residue 57 in the regulatory domain of a mutant rabbit skeletal muscle troponin C to the inhibitory region of troponin I
    • Kobayashi T, Tao T, Grabarek Z, Gergely J, Collins JH. 1991. Cross-linking of residue 57 in the regulatory domain of a mutant rabbit skeletal muscle troponin C to the inhibitory region of troponin I. J. Biol. Chem. 266:13746-51
    • (1991) J. Biol. Chem. , vol.266 , pp. 13746-13751
    • Kobayashi, T.1    Tao, T.2    Grabarek, Z.3    Gergely, J.4    Collins, J.H.5
  • 93
    • 0019178255 scopus 로고
    • Role of the high affinity Ca binding sites of cardiac and fast skeletal troponins
    • Kohama K. 1980. Role of the high affinity Ca binding sites of cardiac and fast skeletal troponins. J. Biochem. 88:591-99
    • (1980) J. Biochem. , vol.88 , pp. 591-599
    • Kohama, K.1
  • 94
    • 0020123666 scopus 로고
    • Actin polymerization and its regulation by proteins from non-muscle cells
    • Korn ED. 1982. Actin polymerization and its regulation by proteins from non-muscle cells. Physiol. Rev. 62:672-737
    • (1982) Physiol. Rev. , vol.62 , pp. 672-737
    • Korn, E.D.1
  • 95
    • 0023042009 scopus 로고
    • Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction
    • Kress M, Huxley HE, Faruqi AR, Hendrix J. 1986. Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction. J. Mol. Biol. 188:325-42
    • (1986) J. Mol. Biol. , vol.188 , pp. 325-342
    • Kress, M.1    Huxley, H.E.2    Faruqi, A.R.3    Hendrix, J.4
  • 96
    • 0026546294 scopus 로고
    • Conformational changes in the metal binding sites of cardiac troponin C induced by calcium binding
    • Krudy GA, Brito RM, Putkey JA, Rosevear PR. 1992. Conformational changes in the metal binding sites of cardiac troponin C induced by calcium binding. Biochemistry 31:1595-602
    • (1992) Biochemistry , vol.31 , pp. 1595-1602
    • Krudy, G.A.1    Brito, R.M.2    Putkey, J.A.3    Rosevear, P.R.4
  • 97
  • 98
    • 0020595570 scopus 로고
    • Tropomyosin-troponin and tropomyosin-actin interactions: A fluorescence quenching study
    • Lamkin M, Tao T, Lehrer SS. 1983. Tropomyosin-troponin and tropomyosin-actin interactions: a fluorescence quenching study. Biochemistry 22:3053-58
    • (1983) Biochemistry , vol.22 , pp. 3053-3058
    • Lamkin, M.1    Tao, T.2    Lehrer, S.S.3
  • 99
    • 0021151109 scopus 로고
    • Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction
    • Leavis PC, Gergely J. 1984. Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction. CRC Crit. Rev. Biochem. 16:235-305
    • (1984) CRC Crit. Rev. Biochem. , vol.16 , pp. 235-305
    • Leavis, P.C.1    Gergely, J.2
  • 100
    • 0028179144 scopus 로고
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature 368:65-67
    • (1994) Nature , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 101
    • 0029131118 scopus 로고
    • Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments
    • 99a. Lehman W, Vibert P, Uman P, Craig R. 1995. Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments. J. Mol. Biol. 251:191-96
    • (1995) J. Mol. Biol. , vol.251 , pp. 191-196
    • Lehman, W.1    Vibert, P.2    Uman, P.3    Craig, R.4
  • 103
    • 0023727334 scopus 로고
    • Fluorescence properties of acrylodan-labeled tropomyosin and tropomyosin-actin: Evidence for myosin subfragment 1 induced changes in geometry between tropomyosin and actin
    • Lehrer SS, Ishii Y. 1988. Fluorescence properties of acrylodan-labeled tropomyosin and tropomyosin-actin: evidence for myosin subfragment 1 induced changes in geometry between tropomyosin and actin. Biochemistry 27:5899-906
    • (1988) Biochemistry , vol.27 , pp. 5899-5906
    • Lehrer, S.S.1    Ishii, Y.2
  • 104
    • 0023718224 scopus 로고
    • Cross-linking of rabbit skeletal muscle troponin subunits: Labeling of cysteine-98 of troponin-C with 4-male-imidobenzophenone and analysis of products formed in the binary complex with troponins I and T
    • Leszyk J, Collins JH, Leavis PC, Tao T. 1988. Cross-linking of rabbit skeletal muscle troponin subunits: labeling of cysteine-98 of troponin-C with 4-male-imidobenzophenone and analysis of products formed in the binary complex with troponins I and T. Biochemistry 27:6983-87
    • (1988) Biochemistry , vol.27 , pp. 6983-6987
    • Leszyk, J.1    Collins, J.H.2    Leavis, P.C.3    Tao, T.4
  • 106
  • 108
    • 0018938988 scopus 로고
    • The amino acid sequence of rabbit cardiac tropomyosin
    • Lewis WG, Smillie LB. 1980. The amino acid sequence of rabbit cardiac tropomyosin. J. Biol. Chem. 255:6854-59
    • (1980) J. Biol. Chem. , vol.255 , pp. 6854-6859
    • Lewis, W.G.1    Smillie, L.B.2
  • 109
    • 0027986739 scopus 로고
    • Coupling of calcium to the interaction of troponin I with troponin C from cardiac muscle
    • Liao R, Wang C-K, Cheung HC. 1994. Coupling of calcium to the interaction of troponin I with troponin C from cardiac muscle. Biochemistry 33:12729-34
    • (1994) Biochemistry , vol.33 , pp. 12729-12734
    • Liao, R.1    Wang, C.-K.2    Cheung, H.C.3
  • 110
    • 0020573633 scopus 로고
    • Calcium regulates troponin-tropomyosin binding to the reconstituted thin filament
    • Lin T-I, Lambert P, Dowben RM. 1983. Calcium regulates troponin-tropomyosin binding to the reconstituted thin filament. Biochem. Biophys. Res. Commun. 114:447-51
    • (1983) Biochem. Biophys. Res. Commun. , vol.114 , pp. 447-451
    • Lin, T.-I.1    Lambert, P.2    Dowben, R.M.3
  • 111
    • 0028578013 scopus 로고
    • Assignment and calcium dependence of methionyl epsilon C and epsilon H resonances in cardiac troponin C
    • Lin X, Krudy GA, Howarth J, Rosevear PR, Putkey JA. 1994. Assignment and calcium dependence of methionyl epsilon C and epsilon H resonances in cardiac troponin C. Biochemistry 33:14434-42
    • (1994) Biochemistry , vol.33 , pp. 14434-14442
    • Lin, X.1    Krudy, G.A.2    Howarth, J.3    Rosevear, P.R.4    Putkey, J.A.5
  • 112
    • 0028940312 scopus 로고
    • An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosin gels
    • Lorenz M, Poole KJV, Popp D, Rosenbaum G, Holmes KC. 1995. An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosin gels. J. Mol. Biol. 246:108-19
    • (1995) J. Mol. Biol. , vol.246 , pp. 108-119
    • Lorenz, M.1    Poole, K.J.V.2    Popp, D.3    Rosenbaum, G.4    Holmes, K.C.5
  • 113
    • 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 KC. 1993. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-36
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 114
    • 0019862956 scopus 로고
    • Structural interpretation of the two-site binding of troponin on the muscle thin filament
    • Mak AS, Smillie LB. 1981. Structural interpretation of the two-site binding of troponin on the muscle thin filament. J. Mol. Biol. 149:541-50
    • (1981) J. Mol. Biol. , vol.149 , pp. 541-550
    • Mak, A.S.1    Smillie, L.B.2
  • 115
    • 0015712520 scopus 로고
    • Troponin subunit interactions
    • Margossian SS, Cohen C. 1973. Troponin subunit interactions. J. Mol. Biol. 81:409-13
    • (1973) J. Mol. Biol. , vol.81 , pp. 409-413
    • Margossian, S.S.1    Cohen, C.2
  • 116
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: Cooperative and non-cooperative binding of large ligands to a one-dimensional lattice
    • McGhee JD, von Hippel PH. 1974. Theoretical aspects of DNA-protein interactions: cooperative and non-cooperative binding of large ligands to a one-dimensional lattice. J. Mol. Biol. 86:469-89
    • (1974) J. Mol. Biol. , vol.86 , pp. 469-489
    • McGhee, J.D.1    Von Hippel, P.H.2
  • 117
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop DFA, Geeves MA. 1993. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 65:693-701
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 118
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin PJ, Gooch JT, Mannerz H-G, Weeds AG. 1993. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364:685-92
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannerz, H.-G.3    Weeds, A.G.4
  • 119
    • 0026020902 scopus 로고
    • Cooperative interactions between troponin molecles bound to the cardiac thin filament
    • Mehegan JP, Tobacman LS. 1991. Cooperative interactions between troponin molecles bound to the cardiac thin filament. J. Biol. Chem. 266:966-72
    • (1991) J. Biol. Chem. , vol.266 , pp. 966-972
    • Mehegan, J.P.1    Tobacman, L.S.2
  • 120
    • 0028944618 scopus 로고
    • Myosin binding-induced cooperative activation of the thin filament in cardiac myocytes and skeletal muscle fibers
    • Metzger JM. 1995. Myosin binding-induced cooperative activation of the thin filament in cardiac myocytes and skeletal muscle fibers. Biophys. J. 68:1430-42
    • (1995) Biophys. J. , vol.68 , pp. 1430-1442
    • Metzger, J.M.1
  • 121
    • 0025824168 scopus 로고
    • 2+-sensitive cross-bridge state transition in skeletal muscle fibers. Effects due to variations in thin filament activation by extraction of troponin C
    • 2+-sensitive cross-bridge state transition in skeletal muscle fibers. Effects due to variations in thin filament activation by extraction of troponin C. J. Gen. Physiol. 98:233-48
    • (1991) J. Gen. Physiol. , vol.98 , pp. 233-248
    • Metzger, J.M.1    Moss, R.L.2
  • 122
    • 0027482724 scopus 로고
    • Skeletal troponin C reduces contractile sensitivity to acidosis in cardiac myocytes from transgenic mice
    • Metzger JM, Parmacek MS, Barr E, Pasyk K, Lin W, et al. 1993. Skeletal troponin C reduces contractile sensitivity to acidosis in cardiac myocytes from transgenic mice. Proc. Natl. Acad. Sci. USA 90:9036-40
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9036-9040
    • Metzger, J.M.1    Parmacek, M.S.2    Barr, E.3    Pasyk, K.4    Lin, W.5
  • 123
    • 0025052483 scopus 로고
    • Molecular structure of F-actin and location of surface binding sites
    • Milligan RA, Whittaker M, Safer D. 1990. Molecular structure of F-actin and location of surface binding sites. Nature 348:217-21
    • (1990) Nature , vol.348 , pp. 217-221
    • Milligan, R.A.1    Whittaker, M.2    Safer, D.3
  • 124
    • 0028172848 scopus 로고
    • 2+ binding to cardiac troponin C in the myofilament lattice and its relation to the myofibrillar ATPase activity
    • 2+ binding to cardiac troponin C in the myofilament lattice and its relation to the myofibrillar ATPase activity. Eur. J. Biochem. 226:597-602
    • (1994) Eur. J. Biochem. , vol.226 , pp. 597-602
    • Morimoto, S.1    Ohtsuki, I.2
  • 125
    • 0021251356 scopus 로고
    • Troponin-tropomyosin interactions. Fluorescence studies of the binding of troponin, troponin T, and chymotryptic troponin T fragments to specifically labeled tropomyosin
    • Morris EP, Lehrer SS. 1984. Troponin-tropomyosin interactions. Fluorescence studies of the binding of troponin, troponin T, and chymotryptic troponin T fragments to specifically labeled tropomyosin. Biochemistry 23:2214-20
    • (1984) Biochemistry , vol.23 , pp. 2214-2220
    • Morris, E.P.1    Lehrer, S.S.2
  • 126
    • 0022491789 scopus 로고
    • Effects of partial extraction of troponin complex upon the tension-pCa relation in rabbit skeletal muscle. Further evidence that tension development involves cooperative effects within the thin filament
    • Moss RL, Allen JD, Greaser ML. 1986. Effects of partial extraction of troponin complex upon the tension-pCa relation in rabbit skeletal muscle. Further evidence that tension development involves cooperative effects within the thin filament. J. Gen. Physiol. 87:761-74
    • (1986) J. Gen. Physiol. , vol.87 , pp. 761-774
    • Moss, R.L.1    Allen, J.D.2    Greaser, M.L.3
  • 127
    • 0022412866 scopus 로고
    • The effects of partial extraction of TnC upon the tension-pCa relationship in skinned rabbit skeletal muscle fibers
    • Moss RL, Guilian GG, Greaser ML. 1985. The effects of partial extraction of TnC upon the tension-pCa relationship in skinned rabbit skeletal muscle fibers. J. Gen. Physiol. 86:585-600
    • (1985) J. Gen. Physiol. , vol.86 , pp. 585-600
    • Moss, R.L.1    Guilian, G.G.2    Greaser, M.L.3
  • 128
    • 0028228518 scopus 로고
    • Dynamic properties of actin. Structural changes induced by beryllium fluoride
    • Muhlrad A, Cheung P, Phan BC, Miller C, Reisler E. 1994. Dynamic properties of actin. Structural changes induced by beryllium fluoride. J. Biol. Chem. 269:11852-58
    • (1994) J. Biol. Chem. , vol.269 , pp. 11852-11858
    • Muhlrad, A.1    Cheung, P.2    Phan, B.C.3    Miller, C.4    Reisler, E.5
  • 129
    • 0020024384 scopus 로고
    • Studies on cooperative properties of tropomyosin-actin and tropomyosin-troponin-actin complexes by the use of N-ethylmaleimide-treated and untreated species of myosin subfragment 1
    • Nagashima H, Asakura S. 1982. Studies on cooperative properties of tropomyosin-actin and tropomyosin-troponin-actin complexes by the use of N-ethylmaleimide-treated and untreated species of myosin subfragment 1. J. Mol. Biol. 155:409-28
    • (1982) J. Mol. Biol. , vol.155 , pp. 409-428
    • Nagashima, H.1    Asakura, S.2
  • 130
  • 131
    • 0028012350 scopus 로고
    • Photochemical cross-linking between native rabbit skeletal troponin C and benzoylbenzoyl-troponin I inhibitory peptide, residues 104-115
    • Ngai S-M, Sonnichsen FD, Hodges RS. 1994. Photochemical cross-linking between native rabbit skeletal troponin C and benzoylbenzoyl-troponin I inhibitory peptide, residues 104-115. J. Biol. Chem. 269:2165-72
    • (1994) J. Biol. Chem. , vol.269 , pp. 2165-2172
    • Ngai, S.-M.1    Sonnichsen, F.D.2    Hodges, R.S.3
  • 132
    • 0028077249 scopus 로고
    • 2+-troponin C-troponin I derived from small-angle scattering data: Implications for regulation
    • 2+-troponin C-troponin I derived from small-angle scattering data: implications for regulation. Biochemistry 33:12800-6
    • (1994) Biochemistry , vol.33 , pp. 12800-12806
    • Olah, G.A.1    Trewella, J.2
  • 134
    • 0026437417 scopus 로고
    • Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis
    • Orlova A, Egelman EH. 1992. Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis. J. Mol. Biol. 227:1043-53
    • (1992) J. Mol. Biol. , vol.227 , pp. 1043-1053
    • Orlova, A.1    Egelman, E.H.2
  • 135
    • 0028907435 scopus 로고
    • Structural dynamics of F-actin: I. Changes in the C terminus
    • Orlova A, Egelman EH. 1995. Structural dynamics of F-actin: I. Changes in the C terminus. J. Mol. Biol. 245:582-97
    • (1995) J. Mol. Biol. , vol.245 , pp. 582-597
    • Orlova, A.1    Egelman, E.H.2
  • 136
    • 0028920157 scopus 로고
    • Structural dynamics of F-actin: II. Cooperativity in structural transitions
    • Orlova A, Prochniewicz E, Egelman EH. 1995. Structural dynamics of F-actin: II. Cooperativity in structural transitions. J. Mol. Biol. 245:598-607
    • (1995) J. Mol. Biol. , vol.245 , pp. 598-607
    • Orlova, A.1    Prochniewicz, E.2    Egelman, E.H.3
  • 137
    • 0024349096 scopus 로고
    • Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle
    • Pan B-S, Gordon AM, Luo Z. 1989. Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle. J. Biol. Chem. 264:8495-98
    • (1989) J. Biol. Chem. , vol.264 , pp. 8495-8498
    • Pan, B.-S.1    Gordon, A.M.2    Luo, Z.3
  • 138
    • 0023644924 scopus 로고
    • Calcium-binding properties of troponin C in detergent-skinned heart muscle fibers
    • Pan B-S, Solaro RJ. 1987. Calcium-binding properties of troponin C in detergent-skinned heart muscle fibers. J. Biol. Chem. 262:7839-49
    • (1987) J. Biol. Chem. , vol.262 , pp. 7839-7849
    • Pan, B.-S.1    Solaro, R.J.2
  • 139
    • 0026039109 scopus 로고
    • Structure, function, and regulation of troponin C
    • Parmacek MS, Leiden JM. 1991. Structure, function, and regulation of troponin C. Circulation 84:991-1003
    • (1991) Circulation , vol.84 , pp. 991-1003
    • Parmacek, M.S.1    Leiden, J.M.2
  • 140
    • 0015935349 scopus 로고
    • Structural role of tropomyosin in muscle regulation: Analysis of the X-ray diffraction patterns from relaxed and contracting muscles
    • Parry DAD, Squire JM. 1973. Structural role of tropomyosin in muscle regulation: analysis of the X-ray diffraction patterns from relaxed and contracting muscles. J. Mol. Biol. 75:33-55
    • (1973) J. Mol. Biol. , vol.75 , pp. 33-55
    • Parry, D.A.D.1    Squire, J.M.2
  • 143
    • 0017540699 scopus 로고
    • The binding site of rabbit skeletal α-tropomyosin on troponin-T
    • Pearlstone JR, Smillie LB. 1977. The binding site of rabbit skeletal α-tropomyosin on troponin-T. Can. J. Biochem. 55:1032-38
    • (1977) Can. J. Biochem. , vol.55 , pp. 1032-1038
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 146
  • 147
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips JGN, Fillers JP, Cohen C. 1986. Tropomyosin crystal structure and muscle regulation. J. Mol. Biol. 192:111-31
    • (1986) J. Mol. Biol. , vol.192 , pp. 111-131
    • Phillips, J.G.N.1    Fillers, J.P.2    Cohen, C.3
  • 150
    • 0027447838 scopus 로고
    • Calcium ions and the structure of muscle actin filament. An X-ray diffraction study
    • Popp D, Maeda Y. 1993. Calcium ions and the structure of muscle actin filament. An X-ray diffraction study. J. Mol. Biol. 229:279-85
    • (1993) J. Mol. Biol. , vol.229 , pp. 279-285
    • Popp, D.1    Maeda, Y.2
  • 152
  • 153
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Potter JD, Gergely J. 1975. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250:4628-33
    • (1975) J. Biol. Chem. , vol.250 , pp. 4628-4633
    • Potter, J.D.1    Gergely, J.2
  • 155
    • 0024413451 scopus 로고
    • Site-directed mutation of the trigger calcium-binding sites in cardiac troponin C
    • Putkey JA, Sweeney HL, Campbell ST. 1989. Site-directed mutation of the trigger calcium-binding sites in cardiac troponin C. J. Biol. Chem. 264:12370-78
    • (1989) J. Biol. Chem. , vol.264 , pp. 12370-12378
    • Putkey, J.A.1    Sweeney, H.L.2    Campbell, S.T.3
  • 156
    • 9244263644 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 157
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I, Holden HM, Whittaker M, Yohn CB, Lorenz M, et al. 1993. Structure of the actin-myosin complex and its implications for muscle contraction. Science 261:58-65
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1    Holden, H.M.2    Whittaker, M.3    Yohn, C.B.4    Lorenz, M.5
  • 159
    • 0021916996 scopus 로고
    • Kinetic studies of calcium binding to regulatory complexes from skeletal muscle
    • Rosenfeld SS, Taylor EW. 1985. Kinetic studies of calcium binding to regulatory complexes from skeletal muscle. J. Biol. Chem. 260:252-61
    • (1985) J. Biol. Chem. , vol.260 , pp. 252-261
    • Rosenfeld, S.S.1    Taylor, E.W.2
  • 161
    • 0028933051 scopus 로고
    • Structural studies on the ribbon-to-helix transition in profilin:actin crystals
    • Schutt CE, Rozycki MD, Chik JK, Lindberg U. 1995. Structural studies on the ribbon-to-helix transition in profilin:actin crystals. Biophys. J. 68:12s-18s
    • (1995) Biophys. J. , vol.68
    • Schutt, C.E.1    Rozycki, M.D.2    Chik, J.K.3    Lindberg, U.4
  • 163
    • 0020170120 scopus 로고
    • Activation of thin-filament-regulated muscle by calcium ion: Considerations based on nearest-neighbor lattice statistics
    • Shiner JS, Solaro RJ. 1982. Activation of thin-filament-regulated muscle by calcium ion: considerations based on nearest-neighbor lattice statistics. Proc. Natl. Acad. Sci. USA 79:4637-41
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4637-4641
    • Shiner, J.S.1    Solaro, R.J.2
  • 164
    • 0021646425 scopus 로고
    • 2+-activation of striated muscle contraction
    • 2+-activation of striated muscle contraction. Biophys. J. 46:541-43
    • (1984) Biophys. J. , vol.46 , pp. 541-543
    • Shiner, J.S.1    Solaro, R.J.2
  • 165
    • 0028144280 scopus 로고
    • 2+-sensitive ATPase activity of rabbit skeletal myofibrils
    • 2+-sensitive ATPase activity of rabbit skeletal myofibrils. J. Biochem. 115:171-73
    • (1994) J. Biochem. , vol.115 , pp. 171-173
    • Shiraishi, F.1    Yamamoto, K.2
  • 166
    • 0028912345 scopus 로고
    • Concerted action of the high affinity calcium binding sites in skeletal muscle troponin C
    • Sorenson MM, da Silva ACR, Gouveia CS, Sousa VP, Oshima W, et al. 1995. Concerted action of the high affinity calcium binding sites in skeletal muscle troponin C. J. Biol. Chem. 270:9770-77
    • (1995) J. Biol. Chem. , vol.270 , pp. 9770-9777
    • Sorenson, M.M.1    Da Silva, A.C.R.2    Gouveia, C.S.3    Sousa, V.P.4    Oshima, W.5
  • 167
    • 0001020594 scopus 로고
    • Muscle thin filament structure and regulation: Actin subdomain movements and the tropomyosin shift modelled from low angle X-ray diffraction
    • Squire JM, Al-Khayat HA, Yagi N. 1993. Muscle thin filament structure and regulation: actin subdomain movements and the tropomyosin shift modelled from low angle X-ray diffraction. J. Chem. Soc. Faraday Trans. 89:2717-26
    • (1993) J. Chem. Soc. Faraday Trans. , vol.89 , pp. 2717-2726
    • Squire, J.M.1    Al-Khayat, H.A.2    Yagi, N.3
  • 168
    • 0021950702 scopus 로고
    • Molecular structure of troponin C from chicken skeletal muscle at 3 Å resolution
    • Sundaralingam M, Bergstrom R, Strasburg G, Rao ST, Roychowdhury P, et al. 1985. Molecular structure of troponin C from chicken skeletal muscle at 3 Å resolution. Science 227:945-48
    • (1985) Science , vol.227 , pp. 945-948
    • Sundaralingam, M.1    Bergstrom, R.2    Strasburg, G.3    Rao, S.T.4    Roychowdhury, P.5
  • 169
    • 0025572631 scopus 로고
    • 2+-binding sites in cardiac/slow skeletal muscle troponin C perform distinct functions: Site I alone cannot trigger contraction
    • 2+-binding sites in cardiac/slow skeletal muscle troponin C perform distinct functions: site I alone cannot trigger contraction. Proc. Natl. Acad. Sci. USA 87:9538-42
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9538-9542
    • Sweeney, H.L.1    Brito, R.M.2    Rosevear, P.R.3    Putkey, J.A.4
  • 170
    • 0025606303 scopus 로고
    • 2+-sensitive force in permeabilized myocardium and skeletal muscle
    • 2+-sensitive force in permeabilized myocardium and skeletal muscle. J. Gen. Physiol. 96:1221-45
    • (1990) J. Gen. Physiol. , vol.96 , pp. 1221-1245
    • Sweitzer, N.K.1    Moss, R.L.2
  • 171
    • 0026530360 scopus 로고
    • Interaction of troponin C and troponin C fragments with troponin I and the troponin I inhibitory peptide
    • Swenson CA, Fredrickson RS. 1992. Interaction of troponin C and troponin C fragments with troponin I and the troponin I inhibitory peptide. Biochemistry 31:3420-29
    • (1992) Biochemistry , vol.31 , pp. 3420-3429
    • Swenson, C.A.1    Fredrickson, R.S.2
  • 172
    • 0015980244 scopus 로고
    • A new method of preparation of troponin I (inhibitory protein) using affinity chromatography. Evidence for three different forms of troponin I in striated muscle
    • Syska H, Perry SV, Trayer IP. 1974. A new method of preparation of troponin I (inhibitory protein) using affinity chromatography. Evidence for three different forms of troponin I in striated muscle. FEBS Lett. 40:253-57
    • (1974) FEBS Lett. , vol.40 , pp. 253-257
    • Syska, H.1    Perry, S.V.2    Trayer, I.P.3
  • 173
    • 0017280755 scopus 로고
    • The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit
    • Syska H, Wilkinson JM, Grand RJA, Perry SV. 1976. The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit. Biochem. J. 153:375-87
    • (1976) Biochem. J. , vol.153 , pp. 375-387
    • Syska, H.1    Wilkinson, J.M.2    Grand, R.J.A.3    Perry, S.V.4
  • 174
  • 175
    • 0019474543 scopus 로고
    • Synthetic studies on the inhibitory region of rabbit skeletal troponin I. Relationship of amino acid sequence to biological activity
    • Talbot JA, Hodges RS. 1981. Synthetic studies on the inhibitory region of rabbit skeletal troponin I. Relationship of amino acid sequence to biological activity. J. Biol. Chem. 256:2798-802
    • (1981) J. Biol. Chem. , vol.256 , pp. 2798-2802
    • Talbot, J.A.1    Hodges, R.S.2
  • 176
    • 0019806420 scopus 로고
    • Comparative studies on the inhibitory region of selected species of troponin-I. the use of synthetic peptide analogs to probe structure-function relationships
    • Talbot JA, Hodges RS. 1981. Comparative studies on the inhibitory region of selected species of troponin-I. The use of synthetic peptide analogs to probe structure-function relationships. J. Biol. Chem. 256:12374-78
    • (1981) J. Biol. Chem. , vol.256 , pp. 12374-12378
    • Talbot, J.A.1    Hodges, R.S.2
  • 177
    • 0021240101 scopus 로고
    • Interactions among chymotryptic troponin T subfragments, tropomyosin, troponin I, and troponin C
    • Tanokura M, Ohtsuki I. 1984. Interactions among chymotryptic troponin T subfragments, tropomyosin, troponin I, and troponin C. J. Biochem. 95:1417-21
    • (1984) J. Biochem. , vol.95 , pp. 1417-1421
    • Tanokura, M.1    Ohtsuki, I.2
  • 178
    • 0020967760 scopus 로고
    • Chymotryptic subfragments of troponin T from rabbit skeletal muscle. Interactions with tropomyosin, troponin I and troponin C
    • Tanokura M, Tawada Y, Ono A, Ohtsuki I. 1983. Chymotryptic subfragments of troponin T from rabbit skeletal muscle. Interactions with tropomyosin, troponin I and troponin C. J. Biochem. 93:331-37
    • (1983) J. Biochem. , vol.93 , pp. 331-337
    • Tanokura, M.1    Tawada, Y.2    Ono, A.3    Ohtsuki, I.4
  • 179
    • 0022853074 scopus 로고
    • Site-specific photo-cross-linking studies on interactions between troponin and tropomyosin and between subunits of troponin
    • Tao T, Scheiner CJ, Lamkin M. 1986. Site-specific photo-cross-linking studies on interactions between troponin and tropomyosin and between subunits of troponin. Biochemistry 25:7633-39
    • (1986) Biochemistry , vol.25 , pp. 7633-7639
    • Tao, T.1    Scheiner, C.J.2    Lamkin, M.3
  • 180
    • 0027511431 scopus 로고
    • Normal mode analysis of G-actin
    • Tirion MM, ben-Avrabam D. 1993. Normal mode analysis of G-actin. J. Mol. Biol. 230:186-95
    • (1993) J. Mol. Biol. , vol.230 , pp. 186-195
    • Tirion, M.M.1    Ben-Avrabam, D.2
  • 181
    • 0023112325 scopus 로고
    • 2+ shows cooperativity intrinsic to the thin filament
    • 2+ shows cooperativity intrinsic to the thin filament. Biochemistry 26:492-97
    • (1987) Biochemistry , vol.26 , pp. 492-497
    • Tobacman, L.S.1
  • 182
    • 0022549660 scopus 로고
    • Mechanism of regulation of cardiac actin-myosin subfragment 1 by troponin-tropomyosin
    • Tobacman LS, Adelstein RS. 1986. Mechanism of regulation of cardiac actin-myosin subfragment 1 by troponin-tropomyosin. Biochemistry 25:798-802
    • (1986) Biochemistry , vol.25 , pp. 798-802
    • Tobacman, L.S.1    Adelstein, R.S.2
  • 183
    • 9244255900 scopus 로고    scopus 로고
    • 2+ binding. Studies of cardiac thin filaments containing mixtures of TnC and regulatory site mutant TnC
    • In press
    • 2+ binding. Studies of cardiac thin filaments containing mixtures of TnC and regulatory site mutant TnC. Biophys. J. Abstr. In press
    • (1996) Biophys. J. Abstr.
    • Tobacman, L.S.1    Butters, C.A.2
  • 184
    • 0025174179 scopus 로고
    • Calcium binds cooperatively to the regulatory sites of the cardiac thin filament
    • Tobacman LS, Sawyer D. 1990. Calcium binds cooperatively to the regulatory sites of the cardiac thin filament. J. Biol. Chem. 265:931-39
    • (1990) J. Biol. Chem. , vol.265 , pp. 931-939
    • Tobacman, L.S.1    Sawyer, D.2
  • 185
    • 0019128230 scopus 로고
    • Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
    • Trybus KM, Taylor EW. 1980. Kinetic studies of the cooperative binding of subfragment 1 to regulated actin. Proc. Natl. Acad. Sci. USA 77:7209-13
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7209-7213
    • Trybus, K.M.1    Taylor, E.W.2
  • 186
    • 0020136020 scopus 로고
    • Cooperative binding of n-mers with steric hindrance to finite and
    • Tsuchiya T, Szabo A. 1982. Cooperative binding of n-mers with steric hindrance to finite and infinite one-dimensional lattices. Biopolymers 21:979-94
    • (1982) Biopolymers , vol.21 , pp. 979-994
    • Tsuchiya, T.1    Szabo, A.2
  • 187
    • 0016757164 scopus 로고
    • The amino acid sequence of bovine cardiac troponin C. Comparison with rabbit skeletal troponin C
    • van Herd J-P, Takahashi K. 1975. The amino acid sequence of bovine cardiac troponin C. Comparison with rabbit skeletal troponin C. Biochem. Biophys. Res. Commun. 64:122-27
    • (1975) Biochem. Biophys. Res. Commun. , vol.64 , pp. 122-127
    • Van Herd, J.-P.1    Takahashi, K.2
  • 188
    • 0023930339 scopus 로고
    • The biological importance of each amino acid residue of the troponin I inhibitory sequence 104-115 in the interaction with troponin C and tropomyosin-actin
    • Van Eyk JE, Hodges RS. 1988. The biological importance of each amino acid residue of the troponin I inhibitory sequence 104-115 in the interaction with troponin C and tropomyosin-actin. J. Biol. Chem. 263:1726-32
    • (1988) J. Biol. Chem. , vol.263 , pp. 1726-1732
    • Van Eyk, J.E.1    Hodges, R.S.2
  • 189
    • 0026091724 scopus 로고
    • A comparative study of the interactions of synthetic peptides of the skeletal and cardiac troponin I inhibitory region wiht skeletal and cardiac troponin C
    • Van Eyk JE, Kay CM, Hodges RS. 1991. A comparative study of the interactions of synthetic peptides of the skeletal and cardiac troponin I inhibitory region wiht skeletal and cardiac troponin C. Biochemistry 30:9974-81
    • (1991) Biochemistry , vol.30 , pp. 9974-9981
    • Van Eyk, J.E.1    Kay, C.M.2    Hodges, R.S.3
  • 190
    • 0021706668 scopus 로고
    • 2+-sensitive interaction of myosin and heavy meromyosin with regulated actin
    • 2+-sensitive interaction of myosin and heavy meromyosin with regulated actin. Biochemistry 23:5950-56
    • (1984) Biochemistry , vol.23 , pp. 5950-5956
    • Wagner, P.D.1
  • 191
    • 0026609631 scopus 로고
    • 2+ on the kinetics of phosphate release in skeletal muscle
    • 2+ on the kinetics of phosphate release in skeletal muscle. J. Biol. Chem. 267:2459-66
    • (1992) J. Biol. Chem. , vol.267 , pp. 2459-2466
    • Walker, J.W.1    Lu, Z.2    Moss, R.L.3
  • 192
    • 0022429269 scopus 로고
    • Removal of tropomyosin overlap and the co-operative response to increasing calcium concentrations of the acto-subfragment-I ATPase
    • Walsh TP, Trueblood CE, Evans R, Weber A. 1984. Removal of tropomyosin overlap and the co-operative response to increasing calcium concentrations of the acto-subfragment-I ATPase. J. Mol. Biol. 182:265-69
    • (1984) J. Mol. Biol. , vol.182 , pp. 265-269
    • Walsh, T.P.1    Trueblood, C.E.2    Evans, R.3    Weber, A.4
  • 193
  • 194
    • 0018324977 scopus 로고
    • Equilibrium of the actin-tropomyosin interaction
    • Wegner A. 1979. Equilibrium of the actin-tropomyosin interaction. J. Mol. Biol. 131:839-53
    • (1979) J. Mol. Biol. , vol.131 , pp. 839-853
    • Wegner, A.1
  • 195
    • 0019850741 scopus 로고
    • Interaction of tropomyosin-troponin with actin filaments
    • Wegner A, Walsh TP. 1981. Interaction of tropomyosin-troponin with actin filaments. Biochemistry 20:5633-42
    • (1981) Biochemistry , vol.20 , pp. 5633-5642
    • Wegner, A.1    Walsh, T.P.2
  • 196
    • 0026339891 scopus 로고
    • Rate and mechanism of assembly of tropomyosin with actin filaments
    • Weigt C, Wegner A, Koch MHJ. 1991. Rate and mechanism of assembly of tropomyosin with actin filaments. Biochemistry 30:10700-7
    • (1991) Biochemistry , vol.30 , pp. 10700-10707
    • Weigt, C.1    Wegner, A.2    Koch, M.H.J.3
  • 199
    • 0023091230 scopus 로고
    • Structure of co-crystals of tropomyosin and troponin
    • White SP, Cohen C, Phillips JGN. 1987. Structure of co-crystals of tropomyosin and troponin. Nature 325:826-28
    • (1987) Nature , vol.325 , pp. 826-828
    • White, S.P.1    Cohen, C.2    Phillips, J.G.N.3
  • 200
    • 0017919767 scopus 로고
    • Comparison of amino acid sequence of troponin I from different striated muscles
    • Wilkinson JM, Grand RJA. 1978. Comparison of amino acid sequence of troponin I from different striated muscles. Nature 271:31-35
    • (1978) Nature , vol.271 , pp. 31-35
    • Wilkinson, J.M.1    Grand, R.J.A.2
  • 201
    • 0027082784 scopus 로고
    • Effects of the amino-terminal regions of tropomyosin and troponin T on thin filament assembly
    • Willadsen KA, Butters CA, Hill LE, Tobacman LS. 1992. Effects of the amino-terminal regions of tropomyosin and troponin T on thin filament assembly. J. Biol. Chem. 267:23746-52
    • (1992) J. Biol. Chem. , vol.267 , pp. 23746-23752
    • Willadsen, K.A.1    Butters, C.A.2    Hill, L.E.3    Tobacman, L.S.4
  • 202
    • 0020549741 scopus 로고
    • Comparison of the effects of tropomyosin and troponin-tropomyosin on the binding of myosin subfragment 1 to actin
    • Williams DL, Greene LE. 1983. Comparison of the effects of tropomyosin and troponin-tropomyosin on the binding of myosin subfragment 1 to actin. Biochemistry 22:2770-74
    • (1983) Biochemistry , vol.22 , pp. 2770-2774
    • Williams, D.L.1    Greene, L.E.2
  • 203
    • 0023747148 scopus 로고
    • Cooperative turning on of myosin subfragment 1 adenosine triphosphatase activity by the troponin-tropomyosin-actin complex
    • Williams DL, Greene LE, Eisenberg E. 1988. Cooperative turning on of myosin subfragment 1 adenosine triphosphatase activity by the troponin-tropomyosin-actin complex. Biochemistry 27:6897-993
    • (1988) Biochemistry , vol.27 , pp. 6897-6993
    • Williams, D.L.1    Greene, L.E.2    Eisenberg, E.3
  • 204
    • 0021192049 scopus 로고
    • Regulation of actomyosin ATPase by a single calcium-binding site on troponin C from crayfish
    • Wnuk W, Schoechlin M, Stein EA. 1984. Regulation of actomyosin ATPase by a single calcium-binding site on troponin C from crayfish. J. Biol. Chem. 259:9017-23
    • (1984) J. Biol. Chem. , vol.259 , pp. 9017-9023
    • Wnuk, W.1    Schoechlin, M.2    Stein, E.A.3
  • 205
    • 0028919177 scopus 로고
    • Rate of tension development in cardiac muscle varies with level of activator calcium
    • Wolff MR, McDonald KS, Moss RL. 1995. Rate of tension development in cardiac muscle varies with level of activator calcium. Circ. Res. 76:154-60
    • (1995) Circ. Res. , vol.76 , pp. 154-160
    • Wolff, M.R.1    McDonald, K.S.2    Moss, R.L.3
  • 206
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman J Jr. 1964. Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Protein Chem. 19:223-86
    • (1964) Adv. Protein Chem. , vol.19 , pp. 223-286
    • Wyman Jr., J.1
  • 207
    • 0024974910 scopus 로고
    • Structural changes in the thin filament during activation studied by X-ray diffraction of highly stretched skeletal muscle
    • Yagi N, Matsubara I. 1989. Structural changes in the thin filament during activation studied by X-ray diffraction of highly stretched skeletal muscle. J. Mol. Biol. 208:359-63
    • (1989) J. Mol. Biol. , vol.208 , pp. 359-363
    • Yagi, N.1    Matsubara, I.2
  • 208
    • 0016326710 scopus 로고
    • Cooformational changes in F-actin in the thin filaments of muscle induced in vivo and in vitro by calcium ions
    • Yanagida T, Taniguchi M, Oosawa F. 1974. Cooformational changes in F-actin in the thin filaments of muscle induced in vivo and in vitro by calcium ions. J. Mol. Biol. 90:509-22
    • (1974) J. Mol. Biol. , vol.90 , pp. 509-522
    • Yanagida, T.1    Taniguchi, M.2    Oosawa, F.3
  • 210
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot AS, Potter JD. 1987. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu. Rev. Biophys. Biophys. Chem. 16:535-59
    • (1987) Annu. Rev. Biophys. Biophys. Chem. , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2
  • 211
    • 0023426125 scopus 로고
    • Calcium binding and fluorescence measurements of dansylaziridine-labelled troponin C in reconstituted thin filaments
    • Zot HG, Potter JD. 1987. Calcium binding and fluorescence measurements of dansylaziridine-labelled troponin C in reconstituted thin filaments. J. Muscle Res. Cell Motil. 8:428-36
    • (1987) J. Muscle Res. Cell Motil. , vol.8 , pp. 428-436
    • Zot, H.G.1    Potter, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.