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Volumn 281, Issue 4, 1998, Pages 689-704

The effect of regulatory Ca2+ on the in situ structures of troponin C and troponin I: A neutron scattering study

Author keywords

Ca2+ switch; Neutron scattering; Regulation of muscle contraction; Troponin structure

Indexed keywords

CALCIUM ION; DEUTERIUM OXIDE; TROPONIN C; TROPONIN I; ADENOSINE TRIPHOSPHATASE (CALCIUM MAGNESIUM); CALCIUM; CALCIUM BINDING PROTEIN; MUSCLE PROTEIN; RECOMBINANT PROTEIN;

EID: 0032575371     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1965     Document Type: Article
Times cited : (58)

References (71)
  • 1
    • 84981841113 scopus 로고
    • Metal indicators. a phthalein responding to alkaline earth ions and its analytical applications
    • Anderegg G., Flaschka H., Sallmann R., Schwarzenbach G. Metal indicators. A phthalein responding to alkaline earth ions and its analytical applications. Helv. Chim. Acta. 37:1954;113-120
    • (1954) Helv. Chim. Acta , vol.37 , pp. 113-120
    • Anderegg, G.1    Flaschka, H.2    Sallmann, R.3    Schwarzenbach, G.4
  • 2
    • 11944270350 scopus 로고
    • Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzyme
    • Babbitt P.C., West B.L., Buechter D.D., Kuntz I.D., Kenyon G.L. Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzyme. Biotechnology (NY). 8:1990;945-949
    • (1990) Biotechnology (NY) , vol.8 , pp. 945-949
    • Babbitt, P.C.1    West, B.L.2    Buechter, D.D.3    Kuntz, I.D.4    Kenyon, G.L.5
  • 3
    • 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 troponin I peptide when bound to skeletal troponin C
    • Campbell A.P., Sykes B.D. 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 troponin I peptide when bound to skeletal troponin C. J. Mol. Biol. 222:1991;405-421
    • (1991) J. Mol. Biol. , vol.222 , pp. 405-421
    • Campbell, A.P.1    Sykes, B.D.2
  • 4
    • 0020478670 scopus 로고
    • Proximity of sulfhydryl groups to the sites of interaction between components of the troponin complex from rabbit skeletal muscle
    • Chong P.C., Hodges R.S. Proximity of sulfhydryl groups to the sites of interaction between components of the troponin complex from rabbit skeletal muscle. J. Biol. Chem. 257:1982;2549-2555
    • (1982) J. Biol. Chem. , vol.257 , pp. 2549-2555
    • Chong, P.C.1    Hodges, R.S.2
  • 5
    • 0013890720 scopus 로고
    • Determination of serum calcium by means of orthocresolphthalein complexone
    • Connerty H.V., Briggs A.R. Determination of serum calcium by means of orthocresolphthalein complexone. Am. J. Clin. Pathol. 45:1966;290-296
    • (1966) Am. J. Clin. Pathol. , vol.45 , pp. 290-296
    • Connerty, H.V.1    Briggs, A.R.2
  • 6
    • 0002113197 scopus 로고
    • The isolation of deuterated bacteriorhodopsin from fully deuterated Halobacterium halobium
    • Crespi H.L. The isolation of deuterated bacteriorhodopsin from fully deuterated Halobacterium halobium. Methods Enzymol. 88:1982;3-5
    • (1982) Methods Enzymol. , vol.88 , pp. 3-5
    • Crespi, H.L.1
  • 7
    • 84908087566 scopus 로고
    • Zerstreuung von Rontgenstrahlen
    • Debye P. Zerstreuung von Rontgenstrahlen. Annalen De Physik. 46:1915;809-823
    • (1915) Annalen de Physik , vol.46 , pp. 809-823
    • Debye, P.1
  • 8
    • 0025748858 scopus 로고
    • Analysis of the regulatory and structural defects of troponin C central helix mutants
    • Dobrowolski Z., Xu G.Q., Chen W., Hitchcock-DeGregori S.E. Analysis of the regulatory and structural defects of troponin C central helix mutants. Biochemistry. 30:1991;7089-7096
    • (1991) Biochemistry , vol.30 , pp. 7089-7096
    • Dobrowolski, Z.1    Xu, G.Q.2    Chen, W.3    Hitchcock-Degregori, S.E.4
  • 9
    • 0014344192 scopus 로고
    • Troponin. I. Preparation and physiological function
    • Ebashi S., Kodama A., Ebashi F. Troponin. I. Preparation and physiological function. J. Biochem. (Tokyo). 64:1968;465-477
    • (1968) J. Biochem. (Tokyo) , vol.64 , pp. 465-477
    • Ebashi, S.1    Kodama, A.2    Ebashi, F.3
  • 10
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato A., Fabiato F. Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J. Physiol. 75:1979;463-505
    • (1979) J. Physiol. , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 11
    • 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
  • 13
    • 0020475827 scopus 로고
    • Troponin and its interactions with tropomyosin. An electron microscope study
    • Flicker P.F., Phillips G.N. Jr, Cohen C. Troponin and its interactions with tropomyosin. An electron microscope study. J. Mol. Biol. 162:1982;495-501
    • (1982) J. Mol. Biol. , vol.162 , pp. 495-501
    • Flicker, P.F.1    Phillips Jr., G.N.2    Cohen, C.3
  • 14
    • 0027448915 scopus 로고
    • Reconstitution of rabbit skeletal muscle troponin from the recombinant subunits all expressed in and purified from E. coli
    • Fujita-Becker S., Kluwe L., Miegel A., Maeda K., Maeda Y. Reconstitution of rabbit skeletal muscle troponin from the recombinant subunits all expressed in and purified from E. coli. J. Biochem. (Tokyo). 114:1993;438-444
    • (1993) J. Biochem. (Tokyo) , vol.114 , pp. 438-444
    • Fujita-Becker, S.1    Kluwe, L.2    Miegel, A.3    Maeda, K.4    Maeda, Y.5
  • 15
    • 0029094184 scopus 로고
    • The shapes of the motor domains of two oppositely directed microtubule motors, ncd and kinesin: A neutron scattering study
    • Fujiwara S., Kull F.J., Sablin E.P., Stone D.B., Mendelson R.A. The shapes of the motor domains of two oppositely directed microtubule motors, ncd and kinesin a neutron scattering study. Biophys. J. 69:1995;1563-1568
    • (1995) Biophys. J. , vol.69 , pp. 1563-1568
    • Fujiwara, S.1    Kull, F.J.2    Sablin, E.P.3    Stone, D.B.4    Mendelson, R.A.5
  • 16
    • 0029088936 scopus 로고
    • Structures of the troponin C regulatory domains in the apo and calcium-saturated states
    • Gagne 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
    • Gagne, S.M.1    Tsuda, S.2    Li, M.X.3    Smillie, L.B.4    Sykes, B.D.5
  • 18
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the Biuret reaction
    • Gornall A.G., Bardawill C.J., David M.M. Determination of serum proteins by means of the Biuret reaction. J. Biol. Chem. 177:1949;751-766
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 19
    • 0023845141 scopus 로고
    • Comparison of the crystal and solution structures of calmodulin and troponin C
    • Heidorn D.B., Trewhella J. Comparison of the crystal and solution structures of calmodulin and troponin C. Biochemistry. 27:1988;909-915
    • (1988) Biochemistry , vol.27 , pp. 909-915
    • Heidorn, D.B.1    Trewhella, J.2
  • 20
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution
    • Herzberg O., James M.N. Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution. Nature. 313:1985;653-659
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.2
  • 21
    • 0023771079 scopus 로고
    • Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution
    • Herzberg O., James M.N. 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.2
  • 22
    • 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. 261:1986;2638-2644
    • (1986) J. Biol. Chem. , vol.261 , pp. 2638-2644
    • Herzberg, O.1    Moult, J.2    James, M.N.3
  • 23
    • 0018800221 scopus 로고
    • Interaction of troponin subunits. the interaction between the inhibitory and tropomyosin-binding subunits
    • Horwitz J., Bullard B., Mercola D. Interaction of troponin subunits. The interaction between the inhibitory and tropomyosin-binding subunits. J. Biol. Chem. 254:1979;350-355
    • (1979) J. Biol. Chem. , vol.254 , pp. 350-355
    • Horwitz, J.1    Bullard, B.2    Mercola, D.3
  • 24
    • 0000244537 scopus 로고
    • Structural changes in the actin- and myosin-containing filaments during contraction
    • Huxley H.E. Structural changes in the actin- and myosin-containing filaments during contraction. Cold Spring Harbor Symp. Quant. Biol. 37:1972;361-376
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 25
    • 0016640142 scopus 로고
    • Comparison of neutron and X-ray scattering of dilute myoglobin solutions
    • Ibel K., Stuhrmann H.B. Comparison of neutron and X-ray scattering of dilute myoglobin solutions. J. Mol. Biol. 93:1975;255-265
    • (1975) J. Mol. Biol. , vol.93 , pp. 255-265
    • Ibel, K.1    Stuhrmann, H.B.2
  • 26
    • 84985698663 scopus 로고
    • Determination of molecular weight by neutron scattering
    • Jacrot B., Zaccai G. Determination of molecular weight by neutron scattering. Biopolymers. 20:1981;2413-2426
    • (1981) Biopolymers , vol.20 , pp. 2413-2426
    • Jacrot, B.1    Zaccai, G.2
  • 27
    • 0027298766 scopus 로고
    • E. coli expression and characterization of a mutant troponin I with the three cysteine residues substituted
    • Kluwe L., Maeda K., Maeda Y. E. coli expression and characterization of a mutant troponin I with the three cysteine residues substituted. FEBS Letters. 323:1993;83-88
    • (1993) FEBS Letters , vol.323 , pp. 83-88
    • Kluwe, L.1    Maeda, K.2    Maeda, Y.3
  • 28
    • 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. 368:1994;65-67
    • (1994) Nature , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 29
    • 0030610913 scopus 로고    scopus 로고
    • 2+ dependence of the distance between Cys48 and Cys133 of troponin I in the ternary troponin complex and reconstituted thin filaments
    • 2+ dependence of the distance between Cys48 and Cys133 of troponin I in the ternary troponin complex and reconstituted thin filaments. Biochemistry. 36:1997;11027-11035
    • (1997) Biochemistry , vol.36 , pp. 11027-11035
    • Luo, Y.1    Wu, J.L.2    Gergely, J.3    Tao, T.4
  • 30
    • 0018778063 scopus 로고
    • Structure of serum low-density lipoprotein. I. a solution X-ray scattering study of a hyperlipidemic monkey low-density lipoprotein
    • Luzzati V., Tardieu A., Aggerbeck L.P. Structure of serum low-density lipoprotein. I. A solution X-ray scattering study of a hyperlipidemic monkey low-density lipoprotein. J. Mol. Biol. 131:1979;435-473
    • (1979) J. Mol. Biol. , vol.131 , pp. 435-473
    • Luzzati, V.1    Tardieu, A.2    Aggerbeck, L.P.3
  • 31
    • 0028222411 scopus 로고
    • Assembly of functional skeletal muscle troponin complex in Escherichia coli
    • Malnic B., Reinach F.C. Assembly of functional skeletal muscle troponin complex in Escherichia coli. Eur. J. Biochem. 222:1994;49-54
    • (1994) Eur. J. Biochem. , vol.222 , pp. 49-54
    • Malnic, B.1    Reinach, F.C.2
  • 32
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian S.S., Lowey S. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 85:(part B):1982;55-71
    • (1982) Methods Enzymol. , vol.85 , Issue.PART B , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 33
    • 0030692043 scopus 로고    scopus 로고
    • Interaction of the second binding region of troponin I with the regulatory domain of skeletal muscle troponin C as determined by NMR spectroscopy
    • McKay R.T., Tripet B.P., Hodges R.S., Sykes B.D. Interaction of the second binding region of troponin I with the regulatory domain of skeletal muscle troponin C as determined by NMR spectroscopy. J. Biol. Chem. 272:1997;28494-28500
    • (1997) J. Biol. Chem. , vol.272 , pp. 28494-28500
    • McKay, R.T.1    Tripet, B.P.2    Hodges, R.S.3    Sykes, B.D.4
  • 34
    • 0019328946 scopus 로고
    • Structure of myosin subfragment 1 from low-angle X-ray scattering
    • Mendelson R., Kretzschmar K.M. Structure of myosin subfragment 1 from low-angle X-ray scattering. Biochemistry. 19:1980;4103-4108
    • (1980) Biochemistry , vol.19 , pp. 4103-4108
    • Mendelson, R.1    Kretzschmar, K.M.2
  • 35
    • 0038915758 scopus 로고
    • On the estimation of the radius of gyration of the subunits of macromolecular aggregates of biological origin in situ
    • Moore P. On the estimation of the radius of gyration of the subunits of macromolecular aggregates of biological origin in situ. J. Appl. Crystallog. 14:1981;237-240
    • (1981) J. Appl. Crystallog. , vol.14 , pp. 237-240
    • Moore, P.1
  • 36
    • 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 F.D., Hodges R.S. Photochemical cross-linking between native rabbit skeletal troponin C and benzoylbenzoyl-troponin I inhibitory peptide, residues 104-115. J. Biol. Chem. 269:1994;2165-2172
    • (1994) J. Biol. Chem. , vol.269 , pp. 2165-2172
    • Ngai, S.M.1    Sonnichsen, F.D.2    Hodges, R.S.3
  • 37
    • 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. 33:1994;12800-12806
    • (1994) Biochemistry , vol.33 , pp. 12800-12806
    • Olah, G.A.1    Trewhella, J.2
  • 38
    • 0030330707 scopus 로고    scopus 로고
    • 2+·troponin C·troponin I. Monte Carlo modeling analysis of small-angle X-ray data
    • 2+·troponin C·troponin I. Monte Carlo modeling analysis of small-angle X-ray data. Basic Life Sci. 64:1996;137-147
    • (1996) Basic Life Sci. , vol.64 , pp. 137-147
    • Olah, G.A.1    Trewhella, J.2
  • 40
    • 0028176711 scopus 로고
    • A disulfide crosslink between Cys98 of troponin-C and Cys133 of troponin-I abolishes the activity of rabbit skeletal troponin
    • Park H.S., Gong B.J., Tao T. A disulfide crosslink between Cys98 of troponin-C and Cys133 of troponin-I abolishes the activity of rabbit skeletal troponin. Biophys. J. 66:1994;2062-2065
    • (1994) Biophys. J. , vol.66 , pp. 2062-2065
    • Park, H.S.1    Gong, B.J.2    Tao, T.3
  • 41
    • 0015935349 scopus 로고
    • Structural role of tropomyosin in muscle regulation: Analysis of the X-ray diffraction patterns from relaxed and contracting muscles
    • Parry D.A., Squire J.M. Structural role of tropomyosin in muscle regulation analysis of the X-ray diffraction patterns from relaxed and contracting muscles. J. Mol. Biol. 75:1973;33-55
    • (1973) J. Mol. Biol. , vol.75 , pp. 33-55
    • Parry, D.A.1    Squire, J.M.2
  • 42
    • 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
  • 43
    • 0020015131 scopus 로고
    • Preparation of troponin and its subunits
    • Potter J.D. Preparation of troponin and its subunits. Methods Enzymol. 85:(part B):1982;241-263
    • (1982) Methods Enzymol. , vol.85 , Issue.PART B , pp. 241-263
    • Potter, J.D.1
  • 44
    • 0016783764 scopus 로고
    • The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase
    • Potter J.D., Gergely 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    Gergely, J.2
  • 47
    • 0027197251 scopus 로고
    • Cloning and expression of chicken skeletal muscle troponin I in Escherichia coli: The role of rare codons on the expression level
    • Quaggio R.B., Ferro J.A., Monteiro P.B., Reinach F.C. Cloning and expression of chicken skeletal muscle troponin I in Escherichia coli the role of rare codons on the expression level. Protein Sci. 2:1993;1053-1056
    • (1993) Protein Sci. , vol.2 , pp. 1053-1056
    • Quaggio, R.B.1    Ferro, J.A.2    Monteiro, P.B.3    Reinach, F.C.4
  • 49
    • 0030994920 scopus 로고    scopus 로고
    • Structural interactions responsible for the assembly of the troponin complex on the muscle thin filament
    • Reinach F.C., Farah C.S., Monteiro P.B., Malnic B. Structural interactions responsible for the assembly of the troponin complex on the muscle thin filament. Cell Struct. Funct. 22:1997;219-223
    • (1997) Cell Struct. Funct. , vol.22 , pp. 219-223
    • Reinach, F.C.1    Farah, C.S.2    Monteiro, P.B.3    Malnic, B.4
  • 50
    • 0342862068 scopus 로고
    • Solvent deuterium isotope effects on acid-base equilibria
    • Salomaa P., Schaleger L.L., Long F.A. Solvent deuterium isotope effects on acid-base equilibria. J. Am. Chem. Soc. 86:1964;1-7
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 1-7
    • Salomaa, P.1    Schaleger, L.L.2    Long, F.A.3
  • 51
    • 0026444089 scopus 로고
    • 2 terminus of fast skeletal muscle troponin I in its biological activity
    • 2 terminus of fast skeletal muscle troponin I in its biological activity. J. Biol. Chem. 267:1992;25407-25413
    • (1992) J. Biol. Chem. , vol.267 , pp. 25407-25413
    • Sheng, Z.1    Pan, B.S.2    Miller, T.E.3    Potter, J.D.4
  • 52
    • 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
  • 53
    • 0027008772 scopus 로고
    • 1H NMR study of a ternary peptide complex that mimics the interaction between troponin C and troponin I
    • 1H NMR study of a ternary peptide complex that mimics the interaction between troponin C and troponin I. Protein Sci. 1:1992;1595-1603
    • (1992) Protein Sci. , vol.1 , pp. 1595-1603
    • Slupsky, C.M.1    Shaw, G.S.2    Campbell, A.P.3    Sykes, B.D.4
  • 54
    • 0020023850 scopus 로고
    • Preparation and identification of alpha- and beta-tropomyosins
    • Smillie L.B. Preparation and identification of alpha- and beta-tropomyosins. Methods Enzymol. 85:(part B):1982;234-241
    • (1982) Methods Enzymol. , vol.85 , Issue.PART B , pp. 234-241
    • Smillie, L.B.1
  • 55
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J.A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:1971;4866-4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 56
    • 0029084279 scopus 로고
    • The radius of gyration of native and reductively methylated myosin subfragment-1 from neutron scattering
    • Stone D.B., Schneider D.K., Huang Z., Mendelson R.A. The radius of gyration of native and reductively methylated myosin subfragment-1 from neutron scattering. Biophys. J. 69:1995;767-776
    • (1995) Biophys. J. , vol.69 , pp. 767-776
    • Stone, D.B.1    Schneider, D.K.2    Huang, Z.3    Mendelson, R.A.4
  • 57
    • 0031576345 scopus 로고    scopus 로고
    • 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 angstrom resolution
    • Strynadka N.C.J., Cherney M., Sielecki A.R., Li M.X., Smillie L.B., James M.N.G. 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 angstrom resolution. J. Mol. Biol. 273:1997;238-255
    • (1997) J. Mol. Biol. , vol.273 , pp. 238-255
    • Strynadka, N.C.J.1    Cherney, M.2    Sielecki, A.R.3    Li, M.X.4    Smillie, L.B.5    James, M.N.G.6
  • 59
    • 0030338146 scopus 로고    scopus 로고
    • Structural model of the 50S subunit of E. coli ribosomes from solution scattering
    • Svergun D.I., Koch M.H., Pedersen J.S., Serdyuk I.N. Structural model of the 50S subunit of E. coli ribosomes from solution scattering. Basic Life Sci. 64:1996;149-174
    • (1996) Basic Life Sci. , vol.64 , pp. 149-174
    • Svergun, D.I.1    Koch, M.H.2    Pedersen, J.S.3    Serdyuk, I.N.4
  • 60
    • 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 S.V., Trayer I.P. 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 Letters. 40:1974;253-257
    • (1974) FEBS Letters , vol.40 , pp. 253-257
    • Syska, H.1    Perry, S.V.2    Trayer, I.P.3
  • 61
    • 0030952840 scopus 로고    scopus 로고
    • Structural and functional domains of the troponin complex revealed by limited digestion
    • Takeda S., Kobayashi T., Taniguchi H., Hayashi H., Maeda Y. Structural and functional domains of the troponin complex revealed by limited digestion. Eur. J. Biochem. 246:1997;611-617
    • (1997) Eur. J. Biochem. , vol.246 , pp. 611-617
    • Takeda, S.1    Kobayashi, T.2    Taniguchi, H.3    Hayashi, H.4    Maeda, Y.5
  • 62
    • 0024473838 scopus 로고
    • 2+ dependence of the distance between Cys-98 of troponin C and Cys-133 of troponin I in the ternary troponin complex. Resonance energy transfer measurements
    • 2+ dependence of the distance between Cys-98 of troponin C and Cys-133 of troponin I in the ternary troponin complex. Resonance energy transfer measurements. Biochemistry. 28:1989;5902-5908
    • (1989) Biochemistry , vol.28 , pp. 5902-5908
    • Tao, T.1    Gowell, E.2    Strasburg, G.M.3    Gergely, J.4    Leavis, P.C.5
  • 63
    • 0025356099 scopus 로고
    • Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments
    • Tao T., Gong B.J., Leavis P.C. Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments. Science. 247:1990;1339-1341
    • (1990) Science , vol.247 , pp. 1339-1341
    • Tao, T.1    Gong, B.J.2    Leavis, P.C.3
  • 64
    • 0025088855 scopus 로고
    • Small-angle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase
    • Trewhella J., Blumenthal D.K., Rokop S.E., Seeger P.A. Small-angle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase. Biochemistry. 29:1990;9316-9324
    • (1990) Biochemistry , vol.29 , pp. 9316-9324
    • Trewhella, J.1    Blumenthal, D.K.2    Rokop, S.E.3    Seeger, P.A.4
  • 67
    • 0023042747 scopus 로고
    • Proximity relationship in the binary complex formed between troponin I and troponin C
    • Wang C.K., Cheung H.C. Proximity relationship in the binary complex formed between troponin I and troponin C. J. Mol. Biol. 191:1986;509-521
    • (1986) J. Mol. Biol. , vol.191 , pp. 509-521
    • Wang, C.K.1    Cheung, H.C.2
  • 68
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds A.G., Taylor R.S. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature. 257:1975;54-56
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 69
    • 0020013525 scopus 로고
    • Special instrumentation and techniques for kinetic studies of contractile systems
    • White H.D. Special instrumentation and techniques for kinetic studies of contractile systems. Methods Enzymol. 85:(part B):1982;698-708
    • (1982) Methods Enzymol. , vol.85 , Issue.PART B , pp. 698-708
    • White, H.D.1
  • 70
    • 0023696286 scopus 로고
    • Synthesis of a troponin C cDNA and expression of wild-type and mutant proteins in Escherichia coli
    • Xu G.Q., Hitchcock-DeGregori S.E. Synthesis of a troponin C cDNA and expression of wild-type and mutant proteins in Escherichia coli. J. Biol. Chem. 263:1988;13962-13969
    • (1988) J. Biol. Chem. , vol.263 , pp. 13962-13969
    • Xu, G.Q.1    Hitchcock-Degregori, S.E.2
  • 71
    • 0017207015 scopus 로고
    • 2O) on excitation-contraction coupling of skeletal muscle
    • 2O) on excitation-contraction coupling of skeletal muscle. Nippon Seirigaku Zasshi. 38:1976;298-300
    • (1976) Nippon Seirigaku Zasshi , vol.38 , pp. 298-300
    • Yagi, S.1    Endo, M.2


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