메뉴 건너뛰기




Volumn 273, Issue 1, 1997, Pages 238-255

Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75 Å resolution

Author keywords

Ca2+ binding protein; Ca2+ ligands; Conformational change; Muscle contraction; X ray crystallography

Indexed keywords

CALCIUM BINDING PROTEIN; MUSCLE PROTEIN; TROPONIN C;

EID: 0031576345     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1257     Document Type: Article
Times cited : (108)

References (74)
  • 3
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 Å resolution
    • Babu Y. S., Bugg C. E., Cook W. J. Structure of calmodulin refined at 2.2 Å resolution. J. Mol. Biol. 204:1988;191-204.
    • (1988) J. Mol. Biol. , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 7
    • 0019977525 scopus 로고
    • Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin
    • Chalovich J. M., Eisenberg E. Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin. J. Biol. Chem. 257:1982;2432-2437.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2432-2437
    • Chalovich, J.M.1    Eisenberg, E.2
  • 8
    • 0019519880 scopus 로고
    • Mechanism of action of troponin-tropomyosin inhibition of actomyosin
    • Chalovich J. M., Chock P. B., Eisenberg E. Mechanism of action of troponin-tropomyosin inhibition of actomyosin. J. Biol. Chem. 256:1981;575-578.
    • (1981) J. Biol. Chem. , vol.256 , pp. 575-578
    • Chalovich, J.M.1    Chock, P.B.2    Eisenberg, E.3
  • 10
    • 0029146286 scopus 로고
    • Releasing the calcium trigger
    • Chazin W. J. Releasing the calcium trigger. Nature Struct. Biol. 2:1995;707-710.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 707-710
    • Chazin, W.J.1
  • 11
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly M. L. Solvent-accessible surfaces of proteins and nucleic acids. Science. 221:1983;709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 12
    • 0026085987 scopus 로고
    • Calcium binding induces conformational changes in muscle regulatory proteins
    • da Silva A. C., Reinach F. C. Calcium binding induces conformational changes in muscle regulatory proteins. Trends Biochem. Sci. 16:1991;53-57.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 53-57
    • Da Silva, A.C.1    Reinach, F.C.2
  • 13
    • 0028605669 scopus 로고
    • The role of glycine residue 89 in the central helix of EF-hand protein troponin C exposed following amino-terminal α-helix deletion
    • Ding X. L., Akella A. B., Su H., Gulati J. The role of glycine residue 89 in the central helix of EF-hand protein troponin C exposed following amino-terminal α-helix deletion. Protein Sci. 3:1994;2089-2096.
    • (1994) Protein Sci. , vol.3 , pp. 2089-2096
    • Ding, X.L.1    Akella, A.B.2    Su, H.3    Gulati, J.4
  • 14
    • 0021970570 scopus 로고
    • Solution conformation of the C-terminal domain of skeletal troponin C: Cation, trifluoroperazine and troponin I binding effects
    • Drabikowski W., Dalgarno D. C., Levine B. A., Gergely J., Grabarek Z., Leavis P. C. Solution conformation of the C-terminal domain of skeletal troponin C: cation, trifluoroperazine and troponin I binding effects. Eur. J. Biochem. 151:1985;17-28.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 17-28
    • Drabikowski, W.1    Dalgarno, D.C.2    Levine, B.A.3    Gergely, J.4    Grabarek, Z.5    Leavis, P.C.6
  • 15
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah C. S., Reinach F. C. The troponin complex and regulation of muscle contraction. FASEB J. 9:1995;755-767.
    • (1995) FASEB J. , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 17
    • 0028670746 scopus 로고
    • Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C
    • Gagné S. M., Tsuda S., Li M. X., Chandra M., Smillie L. B., Sykes B. D. Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C. Protein Sci. 3:1994;1961-1974.
    • (1994) Protein Sci. , vol.3 , pp. 1961-1974
    • Gagné, S.M.1    Tsuda, S.2    Li, M.X.3    Chandra, M.4    Smillie, L.B.5    Sykes, B.D.6
  • 18
    • 0029088936 scopus 로고
    • Structures of the troponin C regulatory domains in the apo and calcium-saturated states
    • Gagné S. M., Tsuda S., Li M. X., Smillie L. B., Sykes B. D. Structures of the troponin C regulatory domains in the apo and calcium-saturated states. Nature Struct. Biol. 2:1995;784-789.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 784-789
    • Gagné, S.M.1    Tsuda, S.2    Li, M.X.3    Smillie, L.B.4    Sykes, B.D.5
  • 19
    • 0030936958 scopus 로고    scopus 로고
    • Mechanism of direct coupling between calcium-binding and induced structural changes in regulatory proteins
    • Gagné S. M., Li M. X., Sykes B. D. Mechanism of direct coupling between calcium-binding and induced structural changes in regulatory proteins. Biochemistry. 36:1997;4386-4392.
    • (1997) Biochemistry , vol.36 , pp. 4386-4392
    • Gagné, S.M.1    Li, M.X.2    Sykes, B.D.3
  • 21
    • 0019768628 scopus 로고
    • Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity
    • Grabarek Z., Drabikowski W., Leavis P. C., Rosenfeld S. S., Gergely J. Proteolytic fragments of troponin C. Interactions with the other troponin subunits and biological activity. J. Biol. Chem. 256:1981;13121-13127.
    • (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
  • 23
    • 0029149568 scopus 로고
    • Properties of troponin C acetylated at lysine residues
    • Grabarek Z., Mabuchi Y., Gergely J. Properties of troponin C acetylated at lysine residues. Biochemistry. 34:1995;11872-11881.
    • (1995) Biochemistry , vol.34 , pp. 11872-11881
    • Grabarek, Z.1    Mabuchi, Y.2    Gergely, J.3
  • 24
    • 0015935352 scopus 로고
    • Purification and properties of the components from troponin
    • Greaser M. L., Gergely J. Purification and properties of the components from troponin. J. Biol. Chem. 248:1973;2125-2133.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2125-2133
    • Greaser, M.L.1    Gergely, J.2
  • 25
    • 0027155675 scopus 로고
    • Identification of the regions conferring calmodulin-like properties to troponin C
    • Gulati J., Babu A., Su H., Zhang Y. F. Identification of the regions conferring calmodulin-like properties to troponin C. J. Biol. Chem. 268:1993;11685-11690.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11685-11690
    • Gulati, J.1    Babu, A.2    Su, H.3    Zhang, Y.F.4
  • 26
    • 0029020507 scopus 로고
    • Functional role of arginine-11 in the N-terminal helix of skeletal troponin C: Combined mutagenesis and molecular dynamics investigation
    • Gulati J., Akella A. B., Su H., Mehler E. L., Weinstein H. Functional role of arginine-11 in the N-terminal helix of skeletal troponin C: combined mutagenesis and molecular dynamics investigation. Biochemistry. 34:1995;7348-7355.
    • (1995) Biochemistry , vol.34 , pp. 7348-7355
    • Gulati, J.1    Akella, A.B.2    Su, H.3    Mehler, E.L.4    Weinstein, H.5
  • 27
    • 0016610095 scopus 로고
    • X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle
    • Haselgrove J. C. X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle. J. Mol. Biol. 92:1975;113-143.
    • (1975) J. Mol. Biol. , vol.92 , pp. 113-143
    • Haselgrove, J.C.1
  • 28
    • 0015801643 scopus 로고
    • X-ray evidence for radial cross-bridge movement and for the sliding filament model in actively contracting skeletal muscle
    • Haselgrove J. C., Huxley H. E. X-ray evidence for radial cross-bridge movement and for the sliding filament model in actively contracting skeletal muscle. J. Mol. Biol. 77:1973;549-568.
    • (1973) J. Mol. Biol. , vol.77 , pp. 549-568
    • Haselgrove, J.C.1    Huxley, H.E.2
  • 29
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin C at 2.8 Å resolution
    • Herzberg O., James M. N. G. Structure of the calcium regulatory muscle protein troponin C at 2.8 Å resolution. Nature. 313:1985a;653-659.
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.G.2
  • 31
    • 0023771079 scopus 로고
    • Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution
    • Herzberg O., James M. N. G. Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution. J. Mol. Biol. 203:1988;761-779.
    • (1988) J. Mol. Biol. , vol.203 , pp. 761-779
    • Herzberg, O.1    James, M.N.G.2
  • 33
    • 0015839814 scopus 로고
    • A note suggesting that the cross-bridge attachment during muscle contraction may take place in two stages
    • Huxley A. F. A note suggesting that the cross-bridge attachment during muscle contraction may take place in two stages. Proc. Roy. Soc. ser. B. Biol. Sci. 183:1973;83-86.
    • (1973) Proc. Roy. Soc. Ser. B. Biol. Sci. , vol.183 , pp. 83-86
    • Huxley, A.F.1
  • 34
    • 0016410843 scopus 로고
    • The origin of force in skeletal muscle
    • Huxley A. F. The origin of force in skeletal muscle. Ciba Found. Symp. 31:1975;271-290.
    • (1975) Ciba Found. Symp. , vol.31 , pp. 271-290
    • Huxley, A.F.1
  • 35
    • 0021194790 scopus 로고
    • Binary interactions of troponin subunits
    • Ingraham R. H., Swenson C. A. Binary interactions of troponin subunits. J. Biol. Chem. 259:1984;9544-9548.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9544-9548
    • Ingraham, R.H.1    Swenson, C.A.2
  • 36
    • 0029736684 scopus 로고    scopus 로고
    • Photo-cross-linking of rabbit skeletal troponin I deletion mutants with troponin C and its thiol mutants: The inhibitory region enhances binding of troponin I fragments to troponin C
    • Jha P. K., Mao C., Sarkar S. Photo-cross-linking of rabbit skeletal troponin I deletion mutants with troponin C and its thiol mutants: the inhibitory region enhances binding of troponin I fragments to troponin C. Biochemistry. 35:1996;11026-11035.
    • (1996) Biochemistry , vol.35 , pp. 11026-11035
    • Jha, P.K.1    Mao, C.2    Sarkar, S.3
  • 37
    • 84889120137 scopus 로고
    • Improved methods for building protein molecules in electron density maps and the location of errors in these models
    • Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein molecules in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 38
    • 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., Toa T., Grabarek Z., Gergely J., Collins J. H. 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. 266:1991;13746-13751.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13746-13751
    • Kobayashi, T.1    Toa, T.2    Grabarek, Z.3    Gergely, J.4    Collins, J.H.5
  • 39
    • 0029094980 scopus 로고
    • Extensive interactions between troponin C and I. Zero-cross length cross-linking of troponin I and acetylated troponin C
    • Kobayashi T., Grabarek Z., Gergely J., Collins J. H. Extensive interactions between troponin C and I. Zero-cross length cross-linking of troponin I and acetylated troponin C. Biochemistry. 34:1995;10946-10952.
    • (1995) Biochemistry , vol.34 , pp. 10946-10952
    • Kobayashi, T.1    Grabarek, Z.2    Gergely, J.3    Collins, J.H.4
  • 40
    • 0029892633 scopus 로고    scopus 로고
    • Interaction of a troponin I inhibitory peptide with both domains of troponin C
    • Kobayashi T., Leavis P. C., Collins J. H. Interaction of a troponin I inhibitory peptide with both domains of troponin C. Biochim. Biophys. Acta. 1294:1996;25-30.
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 25-30
    • Kobayashi, T.1    Leavis, P.C.2    Collins, J.H.3
  • 42
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein II. Structure determination and general description
    • Kretsinger R. H., Nockolds C. E. Carp muscle calcium-binding protein II. Structure determination and general description. J. Biol. Chem. 248:1973;3313-3326.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 44
    • 0021151109 scopus 로고
    • Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction
    • Leavis P. C., Gergely J. Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction. CRC Crit. Rev. Biochem. 16:1984;235-305.
    • (1984) CRC Crit. Rev. Biochem. , vol.16 , pp. 235-305
    • Leavis, P.C.1    Gergely, J.2
  • 45
    • 0017694975 scopus 로고
    • Calcium binding by troponin-C. A proton magnetic resonance study
    • Levine B. A., Coffman D. M. D., Thornton J. M. Calcium binding by troponin-C. A proton magnetic resonance study. J. Mol. Biol. 115:1977;743-760.
    • (1977) J. Mol. Biol. , vol.115 , pp. 743-760
    • Levine, B.A.1    Coffman, D.M.D.2    Thornton, J.M.3
  • 47
    • 0028980851 scopus 로고
    • Calcium binding to the regulatory N-domain of skeletal muscle troponin C occurs in a stepwise manner
    • Li M. X., Gagné S. M., Tsuda S., Kay C. M., Smillie L. B., Sykes B. D. Calcium binding to the regulatory N-domain of skeletal muscle troponin C occurs in a stepwise manner. Biochemistry. 34:1995;8330-8340.
    • (1995) Biochemistry , vol.34 , pp. 8330-8340
    • Li, M.X.1    Gagné, S.M.2    Tsuda, S.3    Kay, C.M.4    Smillie, L.B.5    Sykes, B.D.6
  • 48
    • 0014432781 scopus 로고
    • Estimation of the solvent content in proteins
    • Matthews B. W. Estimation of the solvent content in proteins. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 51
    • 0001507692 scopus 로고
    • On the fast rotation function
    • Navaza J. On the fast rotation function. Acta Crystallog. sect A. 43:1993;645-660.
    • (1993) Acta Crystallog. Sect A , vol.43 , pp. 645-660
    • Navaza, J.1
  • 52
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K. A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 55
    • 0031003385 scopus 로고    scopus 로고
    • Interactions of structural C and regulatory N domains of troponin C with repeated sequence motifs in troponin I
    • Pearlstone J. R., Sykes B. D., Smillie L. B. Interactions of structural C and regulatory N domains of troponin C with repeated sequence motifs in troponin I. Biochemistry. 36:1997;7601-7606.
    • (1997) Biochemistry , vol.36 , pp. 7601-7606
    • Pearlstone, J.R.1    Sykes, B.D.2    Smillie, L.B.3
  • 56
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Potter J. D., Gergley J. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250:1975;4628-4633.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4628-4633
    • Potter, J.D.1    Gergley, J.2
  • 57
    • 0013815214 scopus 로고
    • Stereochemical criteria for polypeptide and protein chain conformations
    • Ramakrishnan C., Ramachandran G. N. Stereochemical criteria for polypeptide and protein chain conformations. Biophys. J. 5:1965;909-933.
    • (1965) Biophys. J. , vol.5 , pp. 909-933
    • Ramakrishnan, C.1    Ramachandran, G.N.2
  • 58
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read R. J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A. 42:1986;140-149.
    • (1986) Acta Crystallog. Sect. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 59
    • 0023947009 scopus 로고
    • Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2 Å resolution
    • Satyshur K. A., Rao S. T., Pyzalska D., Drendel W., Greaser M., Sundaralingam M. Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2 Å resolution. J. Biol. Chem. 263:1988;1628-1647.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1628-1647
    • Satyshur, K.A.1    Rao, S.T.2    Pyzalska, D.3    Drendel, W.4    Greaser, M.5    Sundaralingam, M.6
  • 60
    • 0028891899 scopus 로고
    • NMR solution structure of calcium-saturated skeletal muscle troponin C
    • Slupsky C. M., Sykes B. D. NMR solution structure of calcium-saturated skeletal muscle troponin C. Biochemistry. 34:1995;15953-15964.
    • (1995) Biochemistry , vol.34 , pp. 15953-15964
    • Slupsky, C.M.1    Sykes, B.D.2
  • 61
    • 0028364242 scopus 로고
    • The effects of deletion of the amino-terminal helix on troponin C function and stability
    • Smith L., Greenfield N. J., Hitchcock-Degregori S. E. The effects of deletion of the amino-terminal helix on troponin C function and stability. J. Biol. Chem. 269:1994;9857-9863.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9857-9863
    • Smith, L.1    Greenfield, N.J.2    Hitchcock-Degregori, S.E.3
  • 63
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium-binding proteins
    • Strynadka N. C., James M. N. Crystal structures of the helix-loop-helix calcium-binding proteins. Annu. Rev. Biochem. 58:1989;951-998.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 951-998
    • Strynadka, N.C.1    James, M.N.2
  • 64
    • 0023900654 scopus 로고
    • Two trifluoroperazine binding sites on calmodulin predicted from comparative molecular modelling with troponin C
    • Strynadka N. C. J., James M. N. G. Two trifluoroperazine binding sites on calmodulin predicted from comparative molecular modelling with troponin C. Proteins: Struct. Funct. Genet. 3:1988;1-17.
    • (1988) Proteins: Struct. Funct. Genet. , vol.3 , pp. 1-17
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 65
    • 0000596916 scopus 로고
    • Towards an understanding of the effects of calcium on protein structure and function
    • Strynadka N. C. J., James M. N. G. Towards an understanding of the effects of calcium on protein structure and function. Curr. Opin. Struct. Biol. 1:1991;905-914.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 905-914
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 69
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacaman L. Thin filament-mediated regulation of cardiac contraction. Annu. Rev. Phys. 58:1996;447-481.
    • (1996) Annu. Rev. Phys. , vol.58 , pp. 447-481
    • Tobacaman, L.1
  • 70
    • 84945074880 scopus 로고
    • Conjugate-direction minimization: An improved method for the refinement of macromolecules
    • Tronrud D. E. Conjugate-direction minimization: an improved method for the refinement of macromolecules. Acta. Crystallog. sect. A. 48:1992;912-916.
    • (1992) Acta. Crystallog. Sect. A , vol.48 , pp. 912-916
    • Tronrud, D.E.1
  • 71
    • 0016833750 scopus 로고
    • Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin T-troponin-I complex
    • Wakabayashi T., Huxley H. E., Amos L. A., Klug A. Three-dimensional image reconstruction of actin-tropomyosin complex and actin-tropomyosin-troponin T-troponin-I complex. J. Mol. Biol. 93:1975;477-497.
    • (1975) J. Mol. Biol. , vol.93 , pp. 477-497
    • Wakabayashi, T.1    Huxley, H.E.2    Amos, L.A.3    Klug, A.4
  • 72
    • 0022367130 scopus 로고
    • Energetics of the binding of calcium and troponin I to troponin C from rabbit skeletal muscle
    • Wang C. K., Cheung H. C. Energetics of the binding of calcium and troponin I to troponin C from rabbit skeletal muscle. Biophys. J. 48:1985;727-739.
    • (1985) Biophys. J. , vol.48 , pp. 727-739
    • Wang, C.K.1    Cheung, H.C.2
  • 73
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang M., Tanaka T., Ikura M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nature Struct. Biol. 2:1995;758-767.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 74
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot A. S., Potter J. D. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu. Rev. Biophys. Biophys. Chem. 16:1987;535-559.
    • (1987) Annu. Rev. Biophys. Biophys. Chem. , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.