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Volumn 271, Issue 5, 1997, Pages 728-750

Mapping of a second actin-tropomyosin and a second troponin C binding site within the C terminus of troponin I, and their importance in the Ca2+-dependent regulation of muscle contraction

Author keywords

Muscle regulation; TnI C terminus; TnI inhibition and release; Troponin C; Troponin I

Indexed keywords

ACTIN; ALANINE; CALCIUM ION; SYNTHETIC PEPTIDE; TROPOMYOSIN; TROPONIN C; TROPONIN I;

EID: 0031554903     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1200     Document Type: Article
Times cited : (184)

References (73)
  • 2
    • 0022501265 scopus 로고
    • Calmodulin and troponin C: A comparative study of the interaction of mastoparan and troponin I inhibitory peptide [104-115]
    • Cachia, P. J., Van Eyk, J., Ingraham, R. H., McCubbin, W. D., Kay, C. M. & Hodges, R. S. (1986). Calmodulin and troponin C: a comparative study of the interaction of mastoparan and troponin I inhibitory peptide [104-115]. Biochemistry, 25, 3553-3562.
    • (1986) Biochemistry , vol.25 , pp. 3553-3562
    • Cachia, P.J.1    Van Eyk, J.2    Ingraham, R.H.3    McCubbin, W.D.4    Kay, C.M.5    Hodges, R.S.6
  • 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. (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 troponin I peptide when bound to skeletal troponin C. J. Mol. Biol. 222, 405-421.
    • (1991) J. Mol. Biol. , vol.222 , pp. 405-421
    • Campbell, A.P.1    Sykes, B.D.2
  • 4
    • 0026213620 scopus 로고
    • Interaction of troponin I and troponin C: 19F NMR studies of the binding of the inhibitory troponin I peptide to turkey skeletal troponin C
    • Campbell, A. P., Cachia, P. J. & Sykes, B. D. (1991). Interaction of troponin I and troponin C: 19F NMR studies of the binding of the inhibitory troponin I peptide to turkey skeletal troponin C. Biochem. Cell Biol. 69, 674-681.
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 674-681
    • Campbell, A.P.1    Cachia, P.J.2    Sykes, B.D.3
  • 5
    • 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, 2961-2969.
    • (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
  • 6
    • 0020380464 scopus 로고
    • Photochemical cross-linking between rabbit skeletal troponin subunits
    • Chong, P. C. S. & Hodges, R. S. (1982). Photochemical cross-linking between rabbit skeletal troponin subunits. J. Biol. Chem. 257, 11667-11672.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11667-11672
    • Chong, P.C.S.1    Hodges, R.S.2
  • 7
    • 0020598375 scopus 로고
    • Inhibition of rabbit skeletal muscle acto-S1 ATPase by troponin T
    • Chong, P. C. S., Asselbergs, P. J. & Hodges, R. S. (1983). Inhibition of rabbit skeletal muscle acto-S1 ATPase by troponin T. FEBS Letters, 153, 372-376.
    • (1983) FEBS Letters , vol.153 , pp. 372-376
    • Chong, P.C.S.1    Asselbergs, P.J.2    Hodges, R.S.3
  • 8
    • 0015815403 scopus 로고
    • The amino acid sequence of rabbit skeletal muscle troponin C: Gene replication and homology with calcium-binding proteins from carp and hake muscle
    • Collins, J. H., Potter, J. D., Horn, M. J., Wilshire, G. & Jackman, N. (1973). The amino acid sequence of rabbit skeletal muscle troponin C: gene replication and homology with calcium-binding proteins from carp and hake muscle. FEBS Letters, 36, 268-272.
    • (1973) FEBS Letters , vol.36 , pp. 268-272
    • Collins, J.H.1    Potter, J.D.2    Horn, M.J.3    Wilshire, G.4    Jackman, N.5
  • 11
    • 0014396206 scopus 로고
    • Calcium ion and muscle contraction
    • Ebashi, S. & Endo, M. (1968). Calcium ion and muscle contraction. Prog. Biophys. Mol. Biol. 18, 123-183.
    • (1968) Prog. Biophys. Mol. Biol. , vol.18 , pp. 123-183
    • Ebashi, S.1    Endo, M.2
  • 13
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah, C. S. & Reinach, F. C. (1995). The troponin complex and regulation of muscle contraction (Review). FASEB J. 9, 755-767.
    • (1995) FASEB J. , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 15
    • 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, F. C. (1990). Probing the calcium-induced conformational transition of troponin C with site-directed mutants. Nature, 345, 182-184.
    • (1990) Nature , vol.345 , pp. 182-184
    • Fujimori, K.1    Sorenson, M.2    Herzberg, O.3    Moult, J.4    Reinach, F.C.5
  • 16
    • 0028670746 scopus 로고
    • Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C
    • Gagne, S. M., Tsuda, S., Li, M. X., Chandra, M., Smillie, L. B. & Sykes, B. D. (1994). Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C. Protein Sci. 3, 1961-1974.
    • (1994) Protein Sci. , vol.3 , pp. 1961-1974
    • Gagne, S.M.1    Tsuda, S.2    Li, M.X.3    Chandra, M.4    Smillie, L.B.5    Sykes, B.D.6
  • 17
    • 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. (1995). Structures of the troponin C regulatory domains in the apo and calcium-saturated states. Nature Struct. Biol. 2, 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
  • 19
    • 0025271923 scopus 로고
    • Inhibition of mutant troponin C activity by an intra-domain disulphide bond
    • Grabarek, Z., Tan, R. Y., Wang, J., Tao, T. & Gergely, J. (1990). Inhibition of mutant troponin C activity by an intra-domain disulphide bond (see comments). Nature, 345, 132-135.
    • (1990) Nature , vol.345 , pp. 132-135
    • Grabarek, Z.1    Tan, R.Y.2    Wang, J.3    Tao, T.4    Gergely, J.5
  • 20
  • 21
    • 0015218120 scopus 로고
    • Reconstitution of troponin activity from three protein components
    • Greaser, M. L. & Gergely, J. (1971). Reconstitution of troponin activity from three protein components. J. Biol. Chem. 246, 4226-4233.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4226-4233
    • Greaser, M.L.1    Gergely, J.2
  • 22
    • 0015935352 scopus 로고
    • Purification and properties of the components from troponin
    • Greaser, M. L. & Gergely, J. (1973). Purification and properties of the components from troponin. J. Biol. Chem. 248, 2125-2133.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2125-2133
    • Greaser, M.L.1    Gergely, J.2
  • 24
    • 0019830545 scopus 로고
    • A new and convenient determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase
    • Heinonen, J. K. & Lahti, R. J. (1981). A new and convenient determination of inorganic orthophosphate and its application to the assay of inorganic pyrophosphatase. Anal. Biochem. 113, 313-317.
    • (1981) Anal. Biochem. , vol.113 , pp. 313-317
    • Heinonen, J.K.1    Lahti, R.J.2
  • 25
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution
    • Herzberg, O. & James, M. N. G. (1985). Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution. Nature, 313, 653-659.
    • (1985) Nature , vol.313 , pp. 653-659
    • Herzberg, O.1    James, M.N.G.2
  • 26
    • 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, 2638-2644.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2638-2644
    • Herzberg, O.1    Moult, J.2    James, M.N.3
  • 27
    • 0019887809 scopus 로고
    • Study of the structure of troponin-C by measuring the relative reactivities of lysine with acetic anhydride
    • Hichcock, S. E. (1981). Study of the structure of troponin-C by measuring the relative reactivities of lysine with acetic anhydride. J. Mol. Biol. 147, 153-173.
    • (1981) J. Mol. Biol. , vol.147 , pp. 153-173
    • Hichcock, S.E.1
  • 28
    • 0028962138 scopus 로고
    • An NMR and spin label study of the effects of binding calcium and troponin I inhibitory pep tide to cardiac troponin C
    • Howarth, J. W., Krudy, G. A., Lin, X., Putkey, J. A. & Rosevear, P. R. (1995). An NMR and spin label study of the effects of binding calcium and troponin I inhibitory pep tide to cardiac troponin C. Protein Sci. 4, 671-680.
    • (1995) Protein Sci. , vol.4 , pp. 671-680
    • Howarth, J.W.1    Krudy, G.A.2    Lin, X.3    Putkey, J.A.4    Rosevear, P.R.5
  • 29
    • 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, 5891-5898.
    • (1988) Biochemistry , vol.27 , pp. 5891-5898
    • Ingraham, R.H.1    Hodges, R.S.2
  • 30
    • 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. (1996). 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, 11026-11035.
    • (1996) Biochemistry , vol.35 , pp. 11026-11035
    • Jha, P.K.1    Mao, C.2    Sarkar, S.3
  • 31
    • 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, J. H. (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, 13746-13751.
    • (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
  • 32
    • 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, J. H. (1994). Structure of the troponin complex. Implications of photocross-linking of troponin I to troponin C thiol mutants. J. Biol. Chem. 269, 5725-5729.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5725-5729
    • Kobayashi, T.1    Tao, T.2    Gergely, J.3    Collins, J.H.4
  • 33
    • 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. (1996). Interaction of a troponin I inhibitory peptide with both domains of troponin C. Biochim. Biophys. Acta, 1294, 25-30.
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 25-30
    • Kobayashi, T.1    Leavis, P.C.2    Collins, J.H.3
  • 34
    • 0015919772 scopus 로고
    • Carp musclebinding protein II. Structure determination and general description
    • Kretsinger, R. H. & Nockolds, C. E. (1973). Carp musclebinding protein II. Structure determination and general description. J. Biol. Chem. 248, 3313-3326.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 35
    • 0028016156 scopus 로고
    • NMR studies delineating spatial relationships within the cardiac troponin I-troponin C complex
    • Krudy, G. A., Kleerekoper, Q., Guo, X., Howarth, J. W., Solaro, R. J. & Rosevear, P. R. (1994). NMR studies delineating spatial relationships within the cardiac troponin I-troponin C complex. J. Biol. Chem. 269, 23731-23735.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23731-23735
    • Krudy, G.A.1    Kleerekoper, Q.2    Guo, X.3    Howarth, J.W.4    Solaro, R.J.5    Rosevear, P.R.6
  • 36
    • 0024428060 scopus 로고
    • Interactions of troponin I and its inhibitory fragment (residues 104-115) with troponin C and calmodulin
    • Lan, J., Albaugh, S. & Steiner, R. F. (1989). Interactions of troponin I and its inhibitory fragment (residues 104-115) with troponin C and calmodulin. Biochemistry, 28, 7380-7385.
    • (1989) Biochemistry , vol.28 , pp. 7380-7385
    • Lan, J.1    Albaugh, S.2    Steiner, R.F.3
  • 37
    • 0023643427 scopus 로고
    • Cross-linking of rabbit skeletal muscle troponin with the photoactive reagent 4-maleimidobenzophenone: Identification of residues in troponin I that are close to cysteine-98 of troponin C
    • Leszyk, J., Collins, J. H., Leavis, P. C. & Tao, T. (1987). Cross-linking of rabbit skeletal muscle troponin with the photoactive reagent 4-maleimidobenzophenone: identification of residues in troponin I that are close to cysteine-98 of troponin C. Biochemistry, 26, 7042-7047.
    • (1987) Biochemistry , vol.26 , pp. 7042-7047
    • Leszyk, J.1    Collins, J.H.2    Leavis, P.C.3    Tao, T.4
  • 38
    • 0023718224 scopus 로고
    • Cross-linking of rabbit skeletal muscle troponin subunits: Labeling of cysteine-98 of troponin C with 4-maleimidobenzophenone and analysis of products formed in the binary complex with troponin T and the ternary complex with troponins I and T
    • Leszyk, J., Collins, J. H., Leavis, P. C. & Tao, T. (1988). Cross-linking of rabbit skeletal muscle troponin subunits: labeling of cysteine-98 of troponin C with 4-maleimidobenzophenone and analysis of products formed in the binary complex with troponin T and the ternary complex with troponins I and T. Biochemistry, 27, 6983-6987.
    • (1988) Biochemistry , vol.27 , pp. 6983-6987
    • Leszyk, J.1    Collins, J.H.2    Leavis, P.C.3    Tao, T.4
  • 39
    • 0025019293 scopus 로고
    • Characterization of zero-length cross-links between rabbit skeletal muscle troponin C and troponin I: Evidence for direct interaction between the inhibitory region of troponin I and the NH2-terminal, regulatory domain of troponin C
    • Leszyk, J., Grabarek, Z., Gergely, J. & Collins, J. H. (1990). Characterization of zero-length cross-links between rabbit skeletal muscle troponin C and troponin I: evidence for direct interaction between the inhibitory region of troponin I and the NH2-terminal, regulatory domain of troponin C. Biochemistry, 29, 299-304.
    • (1990) Biochemistry , vol.29 , pp. 299-304
    • Leszyk, J.1    Grabarek, Z.2    Gergely, J.3    Collins, J.H.4
  • 40
    • 0026741822 scopus 로고
    • Biologically important interactions between synthetic peptides of the N-terminal region of troponin I and troponin C
    • Ngai, S. M. & Hodges, R. S. (1992). Biologically important interactions between synthetic peptides of the N-terminal region of troponin I and troponin C. J. Biol. Chem. 267, 15715-15720.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15715-15720
    • Ngai, S.M.1    Hodges, R.S.2
  • 41
    • 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. (1994). Photochemical cross-linking between native rabbit skeletal troponin C and benzoylbenzoyl-troponin I inhibitory peptide, residues 104-115. J. Biol. Chem. 269, 2165-2172.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2165-2172
    • Ngai, S.M.1    Sonnichsen, F.D.2    Hodges, R.S.3
  • 42
    • 0019424237 scopus 로고
    • Fragments of rabbit striated muscle α-tropomyosin
    • Pato, M. O., Mak, A. S. & Smillie, L. B. (1981). Fragments of rabbit striated muscle α-tropomyosin. J. Biol. Chem. 256, 593-601.
    • (1981) J. Biol. Chem. , vol.256 , pp. 593-601
    • Pato, M.O.1    Mak, A.S.2    Smillie, L.B.3
  • 43
    • 0021875797 scopus 로고
    • The interaction of rabbit skeletal muscle troponin-T fragment with troponin-I
    • Pearlstone, J. R. & Smillie, L. B. (1985). The interaction of rabbit skeletal muscle troponin-T fragment with troponin-I. Canad. J. Biochem. Cell. Biol. 63, 212-218.
    • (1985) Canad. J. Biochem. Cell. Biol. , vol.63 , pp. 212-218
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 44
    • 0011121325 scopus 로고
    • 2+-specific fluorescence changes upon interaction of troponin-I inhibitory peptides with the N and C domains of troponin-C tryptophan mutants
    • 2+-specific fluorescence changes upon interaction of troponin-I inhibitory peptides with the N and C domains of troponin-C tryptophan mutants. Biophys. J. 68, A166.
    • (1995) Biophys. J. , vol.68
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 45
    • 0029060203 scopus 로고
    • Evidence for two-site binding of troponin I inhibitory peptides to the N and C domains of troponin C
    • Pearlstone, J. R. & Smillie, L. B. (1995b). Evidence for two-site binding of troponin I inhibitory peptides to the N and C domains of troponin C. Biochemistry, 34, 6932-6940.
    • (1995) Biochemistry , vol.34 , pp. 6932-6940
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 46
    • 0000907106 scopus 로고    scopus 로고
    • Interactions of structural C domain and regulatory N domain of troponin C with repeated sequence motif in troponin I
    • Pearlstone, J. R. & Smillie, L. B. (1997). Interactions of structural C domain and regulatory N domain of troponin C with repeated sequence motif in troponin I. Biophys. J. 72, A331.
    • (1997) Biophys. J. , vol.72
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 47
    • 0000810370 scopus 로고
    • Localization and mode of action of the inhibitory protein component of the troponin complex
    • Perry, S. V., Cole, H. A., Head, J. F. & Wilson, F. J. (1972). Localization and mode of action of the inhibitory protein component of the troponin complex. Cold Spring Harbor Symp. Quant. Biol. 37, 251-262.
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 251-262
    • Perry, S.V.1    Cole, H.A.2    Head, J.F.3    Wilson, F.J.4
  • 49
    • 0022625343 scopus 로고
    • Selective oxidation and reduction of methionine residues in peptides and proteins by oxygen exchange between sulfoxide and sulfide
    • Schechter, Y. (1986). Selective oxidation and reduction of methionine residues in peptides and proteins by oxygen exchange between sulfoxide and sulfide. J. Biol. Chem. 261, 66-70.
    • (1986) J. Biol. Chem. , vol.261 , pp. 66-70
    • Schechter, Y.1
  • 50
    • 0028113997 scopus 로고
    • Reversed-phase chromatography of synthetic amphipathic α-helical peptides as a model for ligand/receptor interactions: Effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains
    • Sereda, T. J., Mant, C. T., Sonnichsen, F. D. & Hodges, R. S. (1994). Reversed-phase chromatography of synthetic amphipathic α-helical peptides as a model for ligand/receptor interactions: effect of changing hydrophobic environment on the relative hydrophilicity/hydrophobicity of amino acid side-chains. J. Chromatog. 676, 139-153.
    • (1994) J. Chromatog. , vol.676 , pp. 139-153
    • Sereda, T.J.1    Mant, C.T.2    Sonnichsen, F.D.3    Hodges, R.S.4
  • 51
    • 0025644197 scopus 로고
    • 2+-specific sites of skeletal muscle TnC are required for full activity
    • published erratum appears in J Biol. Chem. 1993, May 5;268(13):9936
    • 2+-specific sites of skeletal muscle TnC are required for full activity. J. Biol. Chem. 265, 21554-21560 (published erratum appears in J Biol. Chem. 1993, May 5;268(13):9936).
    • (1990) J. Biol. Chem. , vol.265 , pp. 21554-21560
    • Sheng, Z.1    Strauss, W.L.2    Francois, J.M.3    Potter, J.D.4
  • 52
    • 0026444089 scopus 로고
    • 2 terminus of fast skeletal muscle troponin I in its biological activity
    • published erratum appears in J. Biol. Chem. 1993 Feb. 5;268(4):3016
    • 2 terminus of fast skeletal muscle troponin I in its biological activity. J. Biol. Chem. 267, 25407-25413 (published erratum appears in J. Biol. Chem. 1993 Feb. 5;268(4):3016).
    • (1992) J. Biol. Chem. , vol.267 , pp. 25407-25413
    • Sheng, Z.1    Pan, B.S.2    Miller, T.E.3    Potter, J.D.4
  • 53
    • 0028891899 scopus 로고
    • NMR solution structure of calcium-saturated skeletal muscle troponin C
    • Slupsky, C. M. & Sykes, B. D. (1995). NMR solution structure of calcium-saturated skeletal muscle troponin C. Biochemistry, 34, 15953-15964.
    • (1995) Biochemistry , vol.34 , pp. 15953-15964
    • Slupsky, C.M.1    Sykes, B.D.2
  • 54
    • 0027008772 scopus 로고
    • A 1H NMR study of a ternary peptide complex that mimics the interaction between troponin C and troponin I
    • Slupsky, C. M., Shaw, G. S., Campbell, A. P. & Sykes, B. D. (1992). A 1H NMR study of a ternary peptide complex that mimics the interaction between troponin C and troponin I. Protein Sci. 1, 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
  • 55
    • 0029077856 scopus 로고
    • Solution secondary structure of calcium-saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy
    • Slupsky, C. M., Reinach, F. C., Smillie, L. B. & Sykes, B. D. (1995). Solution secondary structure of calcium-saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy. Protein Sci. 4, 1279-1290.
    • (1995) Protein Sci. , vol.4 , pp. 1279-1290
    • Slupsky, C.M.1    Reinach, F.C.2    Smillie, L.B.3    Sykes, B.D.4
  • 56
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. 1. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A. & Watts, S. (1971). The regulation of rabbit skeletal muscle contraction. 1. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246, 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watts, S.2
  • 58
    • 0026530360 scopus 로고
    • Interaction of troponin C and troponin C fragments with troponin I and the troponin I inhibitory peptide
    • Swenson, C. A. & Fredricksen, R. S. (1992). Interaction of troponin C and troponin C fragments with troponin I and the troponin I inhibitory peptide. Biochemistry, 31, 3420-3429.
    • (1992) Biochemistry , vol.31 , pp. 3420-3429
    • Swenson, C.A.1    Fredricksen, R.S.2
  • 59
    • 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. (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 Letters, 40, 253-257.
    • (1974) FEBS Letters , vol.40 , pp. 253-257
    • Syska, H.1    Perry, S.V.2    Trayer, I.P.3
  • 60
    • 0017280755 scopus 로고
    • The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit
    • Syska, H., Wilkinson, J. M., Grand, R. J. A. & Perry, S. V. (1976). The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit. Biochem. J. 153, 375-387.
    • (1976) Biochem. J. , vol.153 , pp. 375-387
    • Syska, H.1    Wilkinson, J.M.2    Grand, R.J.A.3    Perry, S.V.4
  • 61
    • 0018800925 scopus 로고
    • Synthesis and biological activity of an icosapeptide analog of the actomyosin ATPase inhibitory region of troponin I
    • Talbot, J. A. & Hodges, R. S. (1979). Synthesis and biological activity of an icosapeptide analog of the actomyosin ATPase inhibitory region of troponin I. J. Biol. Chem. 254, 3720-3723.
    • (1979) J. Biol. Chem. , vol.254 , pp. 3720-3723
    • Talbot, J.A.1    Hodges, R.S.2
  • 62
    • 0019474543 scopus 로고
    • Synthetic studies on the inhibitory region of rabbit skeletal troponin I
    • Talbot, J. A. & Hodges, R. S. (1981). Synthetic studies on the inhibitory region of rabbit skeletal troponin I. J. Biol. Chem. 256, 2798-2802.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2798-2802
    • Talbot, J.A.1    Hodges, R.S.2
  • 63
    • 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, 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
  • 64
    • 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. (1990). Calcium-induced movement of troponin-I relative to actin in skeletal muscle thin filaments. Science, 247, 1339-1341.
    • (1990) Science , vol.247 , pp. 1339-1341
    • Tao, T.1    Gong, B.J.2    Leavis, P.C.3
  • 65
    • 0026474696 scopus 로고
    • 2+-dependent interaction between troponin C and troponin I inhibitory peptide (96-116)
    • 2+-dependent interaction between troponin C and troponin I inhibitory peptide (96-116). J. Biochem. 112, 665-670.
    • (1992) J. Biochem. , vol.112 , pp. 665-670
    • Tsuda, S.1    Aimoto, S.2    Hikichi, K.3
  • 66
    • 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, J. E. & Hodges, R. S. (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, 1726-1732.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1726-1732
    • Van Eyk, J.E.1    Hodges, R.S.2
  • 67
    • 0027191849 scopus 로고
    • A synthetic peptide mimics troponin I function in the calcium-dependent regulation of muscle contraction
    • Van Eyk, J. E., Strauss, J. D., Hodges, R. S. & Ruegg, J. C. (1993). A synthetic peptide mimics troponin I function in the calcium-dependent regulation of muscle contraction. FEBS Letters, 323, 223-228.
    • (1993) FEBS Letters , vol.323 , pp. 223-228
    • Van Eyk, J.E.1    Strauss, J.D.2    Hodges, R.S.3    Ruegg, J.C.4
  • 69
    • 0025714052 scopus 로고
    • Ca2(+)-dependent interactions between the C-helix of troponin-C and troponin-I. Photocross-linking and fluorescence studies using a recombinant troponin-C
    • Wang, Z. Y., Sarkar, S., Gergely, J. & Tao, T. (1990). Ca2(+)-dependent interactions between the C-helix of troponin-C and troponin-I. Photocross-linking and fluorescence studies using a recombinant troponin-C. J. Biol. Chem. 265, 4953-4957.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4953-4957
    • Wang, Z.Y.1    Sarkar, S.2    Gergely, J.3    Tao, T.4
  • 70
    • 0016752124 scopus 로고
    • Seperation of sub-fragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds, A. G. & Taylor, R. S. (1975). Seperation of sub-fragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature, 257, 54-56.
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 71
    • 0018139861 scopus 로고
    • Characterization of a region region of the primary sequence of troponin C involved in calcium ion-dependent interaction with troponin I
    • Weeks, R. A. & Perry, S. V. (1978). Characterization of a region region of the primary sequence of troponin C involved in calcium ion-dependent interaction with troponin I. Biochem. J. 173, 449-457.
    • (1978) Biochem. J. , vol.173 , pp. 449-457
    • Weeks, R.A.1    Perry, S.V.2
  • 72
    • 0014209728 scopus 로고
    • Proteolytic separation of an enzymatic active subfragment from the myosin-subfragment S-1
    • Yagi, K., Yazawa, Y. & TUsutumu, Y. (1967). Proteolytic separation of an enzymatic active subfragment from the myosin-subfragment S-1. Biochem. Biophys. Res. Commun. 29, 331-336.
    • (1967) Biochem. Biophys. Res. Commun. , vol.29 , pp. 331-336
    • Yagi, K.1    Yazawa, Y.2    Tusutumu, Y.3
  • 73
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • Zot, A. S. & Potter, J. D. (1987). Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction (Review). Annu. Rev. Biaphys. Biophys. Chem. 16, 535-559.
    • (1987) Annu. Rev. Biaphys. Biophys. Chem. , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2


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