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Volumn 87, Issue 8, 2011, Pages 486-508

Regulation of phosphorylase kinase by low concentrations of Ca ions upon muscle contraction: The connection between metabolism and muscle contraction and the connection between muscle physiology and Ca-dependent signal transduction

Author keywords

Ca dependent protein kinase; Cyclic AMP; Glycogenolysis; Low concentrations of Ca ions; Muscle contraction; Phosphorylase kinase; Signal transduction

Indexed keywords

CALCIUM; ION; PHOSPHORYLASE KINASE;

EID: 82355164581     PISSN: 03862208     EISSN: 13492896     Source Type: Journal    
DOI: 10.2183/pjab.87.486     Document Type: Article
Times cited : (16)

References (125)
  • 1
    • 0018337894 scopus 로고
    • Phosphorylation-dephosphorylation of enzymes
    • Krebs, E.G. and Beavo, J.A. (1979) Phosphorylation-dephosphorylation of enzymes. Annu. Rev. Biochem. 48, 923-959.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 923-959
    • Krebs, E.G.1    Beavo, J.A.2
  • 2
    • 0014396206 scopus 로고
    • Calcium ion and muscle contraction
    • Ebashi, S. and 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
  • 4
    • 84944488568 scopus 로고
    • Lactic acid in amphibian muscle
    • Fletcher, W.M. and Hopkins, F.G. (1907) Lactic acid in amphibian muscle. J. Physiol. 48, 247-309.
    • (1907) J. Physiol. , vol.48 , pp. 247-309
    • Fletcher, W.M.1    Hopkins, F.G.2
  • 5
    • 44349099512 scopus 로고
    • Über den Kohlenhydratumsatz isolierter Amphibien-muskeln und über die Beziehungen zwischen Kohlenhydratschwund und Milchsäurebildung im Muskel
    • Parnas, J.K. and Wagner, R. (1914) Über den Kohlenhydratumsatz isolierter Amphibien-muskeln und über die Beziehungen zwischen Kohlenhydratschwund und Milchsäurebildung im Muskel. Biochem. Z. 61, 387-427.
    • (1914) Biochem. Z. , vol.61 , pp. 387-427
    • Parnas, J.K.1    Wagner, R.2
  • 7
    • 0003907356 scopus 로고
    • Williams & Wilkins Company, Baltimore
    • Hill, A.V. (1926) Muscular Activity. Williams & Wilkins Company, Baltimore.
    • (1926) Muscular Activity
    • Hill, A.V.1
  • 8
    • 0000741837 scopus 로고
    • The inorganic phosphate and a labile form of organic phosphate in the gastrocunemius of the frog
    • Eggleton, P. and Eggleton, M.G. (1927) The inorganic phosphate and a labile form of organic phosphate in the gastrocunemius of the frog. Biochem. J. 21, 190-195.
    • (1927) Biochem. J. , vol.21 , pp. 190-195
    • Eggleton, P.1    Eggleton, M.G.2
  • 9
    • 0000847933 scopus 로고
    • The nature of the "inorganic phosphate" in involuntary muscle
    • Fiscke, C.H. and Subbarow, Y. (1927) The nature of the "inorganic phosphate" in involuntary muscle. Science 65, 401-403.
    • (1927) Science , vol.65 , pp. 401-403
    • Fiscke, C.H.1    Subbarow, Y.2
  • 11
    • 0000415398 scopus 로고
    • Über die Pyrophosphatfraktion im Muskel
    • Lohmann, K. (1929) Über die Pyrophosphatfraktion im Muskel. Naturwissensch. 17, 624-625.
    • (1929) Naturwissensch , vol.17 , pp. 624-625
    • Lohmann, K.1
  • 12
    • 84860887190 scopus 로고
    • Über die Konstitution der Adenosinphosphorsäure
    • Makino, K. (1935) Über die Konstitution der Adenosinphosphorsäure. Biochem. Z. 278, 161-163.
    • (1935) Biochem. Z. , vol.278 , pp. 161-163
    • Makino, K.1
  • 13
    • 84912377569 scopus 로고
    • The significance of the phenomenon "alactacid muscle contractions" for an interpretation of the chemistry of muscle contraction
    • This was originally published in Dane and translated into English. In Biological Phosphorylation: Development of Concepts. (1969) (ed. Kalker, H.M.). Prentice-Hall, Englewood Cliffs, N.J
    • Lundsgaard, E. (1932) The significance of the phenomenon "alactacid muscle contractions" for an interpretation of the chemistry of muscle contraction. Danske Hospitalstidende 74, 84-95. This was originally published in Dane and translated into English. In Biological Phosphorylation: Development of Concepts. (1969) (ed. Kalker, H.M.). Prentice-Hall, Englewood Cliffs, N.J., pp. 344-353.
    • (1932) Danske Hospitalstidende , vol.74 , pp. 344-353
    • Lundsgaard, E.1
  • 14
    • 0009502136 scopus 로고
    • Über die enzymatische Aufspaltung der Kreatinphosphorsäure; zugleich ein Beitrag zum Chemismus der Muskelkontraktion
    • Lohmann, K. (1934) Über die enzymatische Aufspaltung der Kreatinphosphorsäure; zugleich ein Beitrag zum Chemismus der Muskelkontraktion. Biochem. Z. 271, 264-277.
    • (1934) Biochem. Z. , vol.271 , pp. 264-277
    • Lohmann, K.1
  • 15
    • 2142645236 scopus 로고
    • Über der Verkettung der chemischen Vorgange im Muskel
    • Parnas, J.K., Ostern, P. and Mann, T. (1934) Über der Verkettung der chemischen Vorgange im Muskel. Biochem. Z. 272, 64-70.
    • (1934) Biochem. Z. , vol.272 , pp. 64-70
    • Parnas, J.K.1    Ostern, P.2    Mann, T.3
  • 16
    • 0002720053 scopus 로고
    • Metabolic generation and utilization of phosphate bond energy
    • Lipmann, F. (1941) Metabolic generation and utilization of phosphate bond energy. Adv. Enzymol. 1, 99-162.
    • (1941) Adv. Enzymol. , vol.1 , pp. 99-162
    • Lipmann, F.1
  • 18
    • 0013114965 scopus 로고
    • Chemistry of muscle contraction. Adenosine triphosphate and phosphorylcreatine as energy supplies for single contractions of working muscle
    • Cain, D.F., Infante, A.A. and Davies, R.E. (1962) Chemistry of muscle contraction. Adenosine triphosphate and phosphorylcreatine as energy supplies for single contractions of working muscle. Nature 196, 214-217.
    • (1962) Nature , vol.196 , pp. 214-217
    • Cain, D.F.1    Infante, A.A.2    Davies, R.E.3
  • 20
    • 0000387962 scopus 로고
    • Glycogen formation in the liver from d- and l-lactic acid
    • Cori, C.F. and Cori, G.T. (1929) Glycogen formation in the liver from d- and l-lactic acid. J. Biol. Chem. 81, 389-403.
    • (1929) J. Biol. Chem. , vol.81 , pp. 389-403
    • Cori, C.F.1    Cori, G.T.2
  • 21
    • 44349193746 scopus 로고
    • Le méchanisme de la glycogénolyse
    • Parnas, J.K. and Ostern, P. (1936) Le méchanisme de la glycogénolyse. Bull. Soc. Chim. Biol. 18, 1471-1492.
    • (1936) Bull. Soc. Chim. Biol. , vol.18 , pp. 1471-1492
    • Parnas, J.K.1    Ostern, P.2
  • 22
    • 84860882917 scopus 로고
    • Le rôle de l'acide inosique dans la glycogénolyse musculaire
    • Parnas, J.K. and Mochnacha, I. (1936) Le rôle de l'acide inosique dans la glycogénolyse musculaire. Comptes Rendus Societe Biol. 123, 1173-1175.
    • (1936) Comptes Rendus Societe Biol , vol.123 , pp. 1173-1175
    • Parnas, J.K.1    Mochnacha, I.2
  • 23
    • 84964092503 scopus 로고
    • Mechanism of formation of hexose monophosphate in muscle and isolation of a new phosphate ester
    • Cori, C.F. and Cori, G.T. (1936) Mechanism of formation of hexose monophosphate in muscle and isolation of a new phosphate ester. Proc. Soc. Exp. Biol. Med. 34, 702-705.
    • (1936) Proc. Soc. Exp. Biol. Med. , vol.34 , pp. 702-705
    • Cori, C.F.1    Cori, G.T.2
  • 24
    • 0037776906 scopus 로고
    • The isolation of glucose-1-phosphoric acid
    • Cori, C.F., Colowick, S.P. and Cori, G.T. (1937) The isolation of glucose-1-phosphoric acid. J. Biol. Chem. 121, 465-477.
    • (1937) J. Biol. Chem. , vol.121 , pp. 465-477
    • Cori, C.F.1    Colowick, S.P.2    Cori, G.T.3
  • 25
    • 4043061238 scopus 로고
    • The enzymatic conversion of glucose-1-phosphoric ester to 6-ester in tissue extracts
    • Cori, C.F., Colowick, S.P. and Cori, G.T. (1938) The enzymatic conversion of glucose-1-phosphoric ester to 6-ester in tissue extracts. J. Biol. Chem. 124, 543-555.
    • (1938) J. Biol. Chem. , vol.124 , pp. 543-555
    • Cori, C.F.1    Colowick, S.P.2    Cori, G.T.3
  • 26
    • 0012353162 scopus 로고
    • Crystalline muscle phosphorylase
    • Green, A.A., Cori, G.T. and Cori, C.F. (1942) Crystalline muscle phosphorylase. J. Biol. Chem. 142, 447-448.
    • (1942) J. Biol. Chem. , vol.142 , pp. 447-448
    • Green, A.A.1    Cori, G.T.2    Cori, C.F.3
  • 27
    • 50449133481 scopus 로고
    • Enzymic conversion of phosphorylase a to phosphorylase b
    • Keller, P.J. and Cori, G.T. (1953) Enzymic conversion of phosphorylase a to phosphorylase b. Biochim. Biophys. Acta 12, 235-238.
    • (1953) Biochim. Biophys. Acta , vol.12 , pp. 235-238
    • Keller, P.J.1    Cori, G.T.2
  • 28
    • 82355161351 scopus 로고
    • Der Mechanismus der Zuckermobilizierung durch das Adrenalin
    • Lasser, E.J. (1920) Der Mechanismus der Zuckermobilizierung durch das Adrenalin. Biochem. Z. 102, 304-319.
    • (1920) Biochem. Z. , vol.102 , pp. 304-319
    • Lasser, E.J.1
  • 29
    • 0009223795 scopus 로고
    • The mechanism of epinephrine action
    • Cori, C.F. and Cori, G.T. (1928) The mechanism of epinephrine action. J. Biol. Chem. 79, 309-319.
    • (1928) J. Biol. Chem. , vol.79 , pp. 309-319
    • Cori, C.F.1    Cori, G.T.2
  • 30
    • 0009221644 scopus 로고
    • Effect of hyperglycemic-glycogenolytic factor and epinephrine on liver phosphorylase
    • Sutherland, E.W. and Cori, C.F. (1951) Effect of hyperglycemic-glycogenolytic factor and epinephrine on liver phosphorylase. J. Biol. Chem. 188, 531-543.
    • (1951) J. Biol. Chem. , vol.188 , pp. 531-543
    • Sutherland, E.W.1    Cori, C.F.2
  • 31
    • 84965091312 scopus 로고
    • The relationship of epinephrine and glucagons to liver phosphorylase. IV. Effect of epinephrine and glucagons on the reactivation of phosphorylase in liver homogenate
    • Rall, T.W., Sutherland, E.W. and Berthet, J. (1957) The relationship of epinephrine and glucagons to liver phosphorylase. IV. Effect of epinephrine and glucagons on the reactivation of phosphorylase in liver homogenate. J. Biol. Chem. 224, 463-475.
    • (1957) J. Biol. Chem. , vol.224 , pp. 463-475
    • Rall, T.W.1    Sutherland, E.W.2    Berthet, J.3
  • 32
    • 0000413412 scopus 로고
    • Formation of a cyclic adenine ribonucleotide by tissue particles
    • Rall, T.W. and Sutherland, E.W. (1958) Formation of a cyclic adenine ribonucleotide by tissue particles. J. Biol. Chem. 232, 1065-1076.
    • (1958) J. Biol. Chem. , vol.232 , pp. 1065-1076
    • Rall, T.W.1    Sutherland, E.W.2
  • 33
    • 0001559662 scopus 로고
    • Fractionation and characterization of a cyclic nucleotide formed by tissue particles
    • Sutherland, E.W. and Rall, T.W. (1958) Fractionation and characterization of a cyclic nucleotide formed by tissue particles. J. Biol. Chem. 232, 1077-1091.
    • (1958) J. Biol. Chem. , vol.232 , pp. 1077-1091
    • Sutherland, E.W.1    Rall, T.W.2
  • 34
    • 0000626332 scopus 로고
    • The formation of a cyclic dianhydrodiadenylic acid (I) by the alkaline degradation of adenosine-5′-triphosphoric acid (II)
    • Cook, W.H., Lipkin, D. and Markham, R. (1957) The formation of a cyclic dianhydrodiadenylic acid (I) by the alkaline degradation of adenosine-5′-triphosphoric acid (II). J. Am. Chem. Soc. 79, 3607-3608.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 3607-3608
    • Cook, W.H.1    Lipkin, D.2    Markham, R.3
  • 36
    • 0001604424 scopus 로고
    • The relation of adenosine-3′, 5′-phosphate and phosphorylase to the actions of cathecolamines and other hormones
    • Sutherland, E.W. and Rall, T.W. (1960) The relation of adenosine-3′,5′-phosphate and phosphorylase to the actions of cathecolamines and other hormones. Pharmacol. Rev. 12, 265-299.
    • (1960) Pharmacol. Rev. , vol.12 , pp. 265-299
    • Sutherland, E.W.1    Rall, T.W.2
  • 37
    • 73849159943 scopus 로고
    • Adenyl cyclase. I. Distribution, preparation and properties
    • Sutherland, E.W., Rall, T.W. and Menon, T. (1962) Adenyl cyclase. I. Distribution, preparation and properties. J. Biol. Chem. 237, 1220-1227.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1220-1227
    • Sutherland, E.W.1    Rall, T.W.2    Menon, T.3
  • 40
    • 0000720406 scopus 로고
    • Myosin and adenosintriphosphatase
    • Engelhardt, W.A. and Lubimova, M.N. (1939) Myosin and adenosintriphosphatase. Nature 144, 668-669.
    • (1939) Nature , vol.144 , pp. 668-669
    • Engelhardt, W.A.1    Lubimova, M.N.2
  • 41
    • 0011231470 scopus 로고
    • 1951 (1st and 2nd ed., respectively). Academic Press Inc., New York
    • Szent-Györgyi, A. (1947 and 1951) Chemistry of Muscle Contraction (1st and 2nd ed., respectively). Academic Press Inc., New York.
    • (1947) Chemistry of Muscle Contraction
    • Szent-Györgyi, A.1
  • 42
    • 0011862810 scopus 로고
    • Proteins of the myofibril
    • (ed. Bourne, G.H.). Academic Press, New York
    • Ebashi, S. and Nonomura, Y. (1973) Proteins of the myofibril. In The Structure and Function of Muscle (ed. Bourne, G.H.). Academic Press, New York, Vol. 3, pp. 285-362.
    • (1973) The Structure and Function of Muscle , vol.3 , pp. 285-362
    • Ebashi, S.1    Nonomura, Y.2
  • 43
    • 0001740396 scopus 로고
    • The property and contraction process of isolated myofibrils
    • Natori, R. (1954) The property and contraction process of isolated myofibrils. Jikeikai Med. J. 1, 119-126.
    • (1954) Jikeikai Med. J. , vol.1 , pp. 119-126
    • Natori, R.1
  • 44
    • 79954419553 scopus 로고    scopus 로고
    • Reiji Natori, Setsuro Ebashi, and excitation-contraction coupling
    • Endo, M. (2011) Reiji Natori, Setsuro Ebashi, and excitation-contraction coupling. Prog. Biophys. Mol. Biol. 105, 129-133.
    • (2011) Prog. Biophys. Mol. Biol. , vol.105 , pp. 129-133
    • Endo, M.1
  • 45
    • 0002701488 scopus 로고
    • The action of calcium on muscle protoplasm
    • Heilbrunn, L.V. (1940) The action of calcium on muscle protoplasm. Physiol. Zool. 13, 88-94.
    • (1940) Physiol. Zool. , vol.13 , pp. 88-94
    • Heilbrunn, L.V.1
  • 46
    • 0001551928 scopus 로고
    • Disturbances initiated from naked surface of muscle protoplasm
    • Kamada, T. and Kinoshita, H. (1943) Disturbances initiated from naked surface of muscle protoplasm. Jpn. J. Zool. 10, 469-493.
    • (1943) Jpn. J. Zool. , vol.10 , pp. 469-493
    • Kamada, T.1    Kinoshita, H.2
  • 47
    • 0002925898 scopus 로고
    • The action of various cations on muscle protoplasm
    • Heilbrunn, L.V. and Wiercinski, F.J. (1947) The action of various cations on muscle protoplasm. J. Cell Comp. Physiol. 29, 15-32.
    • (1947) J. Cell Comp. Physiol. , vol.29 , pp. 15-32
    • Heilbrunn, L.V.1    Wiercinski, F.J.2
  • 48
    • 0040788031 scopus 로고
    • On the time required for diffusion and its relation to processes in muscle
    • Hill, A.V. (1948) On the time required for diffusion and its relation to processes in muscle. Proc. R. Soc. Lond. B 135, 446-453.
    • (1948) Proc. R. Soc. Lond. B , vol.135 , pp. 446-453
    • Hill, A.V.1
  • 49
    • 70449247729 scopus 로고
    • Local activation of striated fibers
    • Huxley, A.F. and Taylor, R.E. (1958) Local activation of striated fibers. J. Physiol. 144, 426-441.
    • (1958) J. Physiol. , vol.144 , pp. 426-441
    • Huxley, A.F.1    Taylor, R.E.2
  • 50
    • 22144479148 scopus 로고    scopus 로고
    • The membrane systems of muscle cells
    • (3rd ed, eds. Engel, A. and Franzini-Armstrong, C.). McGraw-Hill, New York
    • Franzini-Armstrong, C. (2004) The membrane systems of muscle cells. In Myology (3rd ed, eds. Engel, A. and Franzini-Armstrong, C.). McGraw-Hill, New York, Vol. I, pp. 232-256.
    • (2004) Myology , vol.1 , pp. 232-256
    • Franzini-Armstrong, C.1
  • 51
    • 0017364364 scopus 로고
    • Calcium release from the sarcoplasmic reticulum
    • Endo, M. (1977) Calcium release from the sarcoplasmic reticulum. Physiol. Rev. 57, 71-108.
    • (1977) Physiol. Rev. , vol.57 , pp. 71-108
    • Endo, M.1
  • 52
    • 40749160542 scopus 로고
    • Mechanism of relaxation in excited muscle fibers
    • Bozler, E. (1951) Mechanism of relaxation in excited muscle fibers. Am. J. Physiol. 167, 276-283.
    • (1951) Am. J. Physiol. , vol.167 , pp. 276-283
    • Bozler, E.1
  • 53
    • 0001438316 scopus 로고
    • A factor modifying muscle fiber syneresis
    • Marsh, B.B. (1951) A factor modifying muscle fiber syneresis. Nature 167, 1065-1066.
    • (1951) Nature , vol.167 , pp. 1065-1066
    • Marsh, B.B.1
  • 54
    • 0001164833 scopus 로고
    • Essential relaxing factor in muscle other than myokinase and creatine phosphokinase
    • Kumagai, H., Ebashi, S. and Takeda, F. (1955) Essential relaxing factor in muscle other than myokinase and creatine phosphokinase. Nature 176, 166.
    • (1955) Nature , vol.176 , pp. 166
    • Kumagai, H.1    Ebashi, S.2    Takeda, F.3
  • 55
    • 0039009663 scopus 로고
    • Kielly-Meyerhof's granules and the relaxation of glycerinated fibers
    • Igaku Shoin Ltd., Tokyo
    • Ebashi, S. (1957) Kielly-Meyerhof's granules and the relaxation of glycerinated fibers. In Conference on the chemistry of muscular contraction. Igaku Shoin Ltd., Tokyo, pp. 89-94.
    • (1957) Conference on the chemistry of muscular contraction , pp. 89-94
    • Ebashi, S.1
  • 56
    • 0001589275 scopus 로고
    • Relaxation in extracted muscle fibers
    • Bozler, E. (1954) Relaxation in extracted muscle fibers. J. Gen. Physiol. 38, 149-159.
    • (1954) J. Gen. Physiol. , vol.38 , pp. 149-159
    • Bozler, E.1
  • 57
    • 42649110198 scopus 로고
    • Relaxing effects of EDTA on glycerin treated fibers
    • Watanabe, S. (1955) Relaxing effects of EDTA on glycerin treated fibers. Arch. Biochem. Biophys. 54, 559-562.
    • (1955) Arch. Biochem. Biophys. , vol.54 , pp. 559-562
    • Watanabe, S.1
  • 58
    • 82355183274 scopus 로고
    • Roles of sarcoplamic reticulum and Ca ions on muscle contraction
    • (ed. Japan Biophys. Soc.). Yoshioka Shoten, Kyoto (in Japanese)
    • Ebashi, S. (1965) Roles of sarcoplamic reticulum and Ca ions on muscle contraction. In Molecular Functions of Living Body (ed. Japan Biophys. Soc.). Yoshioka Shoten, Kyoto, pp. 154-183 (in Japanese).
    • (1965) Molecular Functions of Living Body , pp. 154-183
    • Ebashi, S.1
  • 59
    • 0000882357 scopus 로고
    • Calcium binding and relaxation in the actomyosin system
    • Ebashi, S. (1960) Calcium binding and relaxation in the actomyosin system. J. Biochem. 48, 150-151.
    • (1960) J. Biochem. , vol.48 , pp. 150-151
    • Ebashi, S.1
  • 60
    • 84968965880 scopus 로고
    • Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle
    • Ebashi, S. and Lipmann, F. (1962) Adenosine triphosphate-linked concentration of calcium ions in a particulate fraction of rabbit muscle. J. Cell Biol. 14, 389-400.
    • (1962) J. Cell Biol. , vol.14 , pp. 389-400
    • Ebashi, S.1    Lipmann, F.2
  • 61
    • 0014358079 scopus 로고
    • The relationship between caffeine contracture of intact muscle and the effect of on caffeine on reticulum
    • Weber, A. and Herz, R. (1968) The relationship between caffeine contracture of intact muscle and the effect of on caffeine on reticulum. J. Gen. Physiol. 52, 750-759.
    • (1968) J. Gen. Physiol. , vol.52 , pp. 750-759
    • Weber, A.1    Herz, R.2
  • 62
    • 0019810179 scopus 로고
    • Calcium release and ionic changes in the sarcoplasmic reticulum of tetanized muscle: an electron-probe study
    • Somlyo, A.V., Gonzalez-Serratos, H., Shuman, H., McClellan, G. and Somlyo, A.P. (1981) Calcium release and ionic changes in the sarcoplasmic reticulum of tetanized muscle: an electron-probe study. J. Cell Biol. 90, 577-594.
    • (1981) J. Cell Biol. , vol.90 , pp. 577-594
    • Somlyo, A.V.1    Gonzalez-Serratos, H.2    Shuman, H.3    McClellan, G.4    Somlyo, A.P.5
  • 63
    • 0001533582 scopus 로고
    • On the role of calcium in the activity of adenosine 5′-triphosphate hydrolysis by actomyosin
    • Weber, A. (1959) On the role of calcium in the activity of adenosine 5′-triphosphate hydrolysis by actomyosin. J. Biol. Chem. 234, 2764-2769.
    • (1959) J. Biol. Chem. , vol.234 , pp. 2764-2769
    • Weber, A.1
  • 64
    • 73049137785 scopus 로고
    • Calcium binding activity of vesicular relaxing factor
    • Ebashi, S. (1961) Calcium binding activity of vesicular relaxing factor. J. Biochem. 50, 236-244.
    • (1961) J. Biochem. , vol.50 , pp. 236-244
    • Ebashi, S.1
  • 65
    • 0025966656 scopus 로고
    • Myoplasmic calcium transients monitored with purpurate indicator dyes injected into frog skeletal muscle fibers
    • Konishi, M. and Baylor, S.M. (1991) Myoplasmic calcium transients monitored with purpurate indicator dyes injected into frog skeletal muscle fibers. J. Gen. Physiol. 97, 245-270.
    • (1991) J. Gen. Physiol. , vol.97 , pp. 245-270
    • Konishi, M.1    Baylor, S.M.2
  • 66
    • 0013790350 scopus 로고
    • A new protein factor promoting aggregation of tropomyosin
    • Ebashi, S. and Kodama, A. (1965) A new protein factor promoting aggregation of tropomyosin. J. Biochem. 58, 107-108.
    • (1965) J. Biochem. , vol.58 , pp. 107-108
    • Ebashi, S.1    Kodama, A.2
  • 68
    • 0345310756 scopus 로고
    • Localization of native tropomyosin in relation to striated patterns
    • Endo, M., Nonomura, Y., Masaki, T., Ohtsuki, I. and Ebashi, S. (1966) Localization of native tropomyosin in relation to striated patterns. J. Biochem. 60, 605-608.
    • (1966) J. Biochem. , vol.60 , pp. 605-608
    • Endo, M.1    Nonomura, Y.2    Masaki, T.3    Ohtsuki, I.4    Ebashi, S.5
  • 69
    • 0014409197 scopus 로고
    • Fractionation of troponin into two distinct proteins
    • Hartshorne, D.J. and Mueller, H. (1968) Fractionation of troponin into two distinct proteins. Biochem. Biophys. Res. Commun. 31, 647-653.
    • (1968) Biochem. Biophys. Res. Commun. , vol.31 , pp. 647-653
    • Hartshorne, D.J.1    Mueller, H.2
  • 70
    • 0014629135 scopus 로고
    • The relaxing protein system of striated muscle. Resolution of the troponin complex into inhibitory and calcium ion-sensitizing factors and their relationship to tropomyosin
    • Schaub, M.C. and Perry, S.V. (1969) The relaxing protein system of striated muscle. Resolution of the troponin complex into inhibitory and calcium ion-sensitizing factors and their relationship to tropomyosin. Biochem. J. 115, 993-1004.
    • (1969) Biochem. J. , vol.115 , pp. 993-1004
    • Schaub, M.C.1    Perry, S.V.2
  • 72
    • 2042464495 scopus 로고
    • Phosphorylase activity of skeletal muscle extracts
    • Krebs, E.G. and Fischer, E.H. (1955) Phosphorylase activity of skeletal muscle extracts. J. Biol. Chem. 216, 113-120.
    • (1955) J. Biol. Chem. , vol.216 , pp. 113-120
    • Krebs, E.G.1    Fischer, E.H.2
  • 73
    • 0000187410 scopus 로고
    • Conversion of phosphorylase b to phosphorylase a in muscle extracts
    • Fischer, E.H. and Krebs, E.G. (1955) Conversion of phosphorylase b to phosphorylase a in muscle extracts. J. Biol. Chem. 216, 121-132.
    • (1955) J. Biol. Chem. , vol.216 , pp. 121-132
    • Fischer, E.H.1    Krebs, E.G.2
  • 74
    • 0010291733 scopus 로고
    • The relationship of epinephrine and glucagons to liver phosphorylase. III. Reactivation of liver phosphorylation in slices and in extracts
    • Rall, T.W., Sutherland, E.W. and Wailait, W.D. (1956) The relationship of epinephrine and glucagons to liver phosphorylase. III. Reactivation of liver phosphorylation in slices and in extracts. J. Biol. Chem. 218, 483-495.
    • (1956) J. Biol. Chem. , vol.218 , pp. 483-495
    • Rall, T.W.1    Sutherland, E.W.2    Wailait, W.D.3
  • 75
    • 49749165001 scopus 로고
    • The phosphorylase b to a converting enzyme of skeletal muscle
    • Krebs, E.G. and Fischer, E.H. (1956) The phosphorylase b to a converting enzyme of skeletal muscle. Biochim. Biophys. Acta 20, 150-157.
    • (1956) Biochim. Biophys. Acta , vol.20 , pp. 150-157
    • Krebs, E.G.1    Fischer, E.H.2
  • 76
    • 0001010573 scopus 로고
    • The enzymatic phosphorylation of proteins
    • Burnet, G. and Kennedy, E.P. (1954) The enzymatic phosphorylation of proteins. J. Biol. Chem. 211, 969-980.
    • (1954) J. Biol. Chem. , vol.211 , pp. 969-980
    • Burnet, G.1    Kennedy, E.P.2
  • 77
    • 82355194655 scopus 로고
    • Regulation of enzyme activity in muscle during work
    • (ed. Gaebler, O.H.). Academic Press, New York
    • Cori, C.F. (1956) Regulation of enzyme activity in muscle during work. In Enzymes, Units of Biological Structure and Function (ed. Gaebler, O.H.). Academic Press, New York, pp. 573-583.
    • (1956) Enzymes, Units of Biological Structure and Function , pp. 573-583
    • Cori, C.F.1
  • 78
    • 0004140523 scopus 로고
    • The effect of contraction and of epinephrine on the phosphorylase activity of frog sartorius muscle
    • Danforth, W.H., Helmreich, E. and Cori, C.F. (1962) The effect of contraction and of epinephrine on the phosphorylase activity of frog sartorius muscle. Proc. Natl. Acad. Sci. U.S.A. 48, 1191-1199.
    • (1962) Proc. Natl. Acad. Sci. U. S. A. , vol.48 , pp. 1191-1199
    • Danforth, W.H.1    Helmreich, E.2    Cori, C.F.3
  • 79
    • 0002101212 scopus 로고
    • The isolation and crystallization of rabbit skeletal muscle phosphorylase b
    • Fischer, E.H. and Krebs, E.W. (1958) The isolation and crystallization of rabbit skeletal muscle phosphorylase b. J. Biol. Chem. 231, 65-71.
    • (1958) J. Biol. Chem. , vol.231 , pp. 65-71
    • Fischer, E.H.1    Krebs, E.W.2
  • 80
    • 70449285205 scopus 로고
    • Factors affecting the activity of muscle phosphorylase b kinase
    • Krebs, E.W., Graves, D.J. and Fischer, E.H. (1959) Factors affecting the activity of muscle phosphorylase b kinase. J. Biol. Chem. 234, 2867-2873.
    • (1959) J. Biol. Chem. , vol.234 , pp. 2867-2873
    • Krebs, E.W.1    Graves, D.J.2    Fischer, E.H.3
  • 82
    • 0004020915 scopus 로고
    • Regulation of glycolysis in muscle. I. The conversion of phosphorylase b to phosphorylase a in frog sartorius muscle
    • Danforth, W.H. and Helmreich, E. (1964) Regulation of glycolysis in muscle. I. The conversion of phosphorylase b to phosphorylase a in frog sartorius muscle. J. Biol. Chem. 239, 3133-3138.
    • (1964) J. Biol. Chem. , vol.239 , pp. 3133-3138
    • Danforth, W.H.1    Helmreich, E.2
  • 83
    • 0000655087 scopus 로고
    • Potassium contractures in single muscle fibers
    • Hodgkin, A.L. and Horowicz, P. (1960) Potassium contractures in single muscle fibers. J. Physiol. 153, 386-403.
    • (1960) J. Physiol. , vol.153 , pp. 386-403
    • Hodgkin, A.L.1    Horowicz, P.2
  • 84
    • 0001105190 scopus 로고
    • Purification and properties of rabbit skeletal muscle phosphorylase b kinase
    • Krebs, E.W., Love, D., Bratvild, G.E., Trayer, K.A., Meyer, W. and Fischer, E.H. (1964) Purification and properties of rabbit skeletal muscle phosphorylase b kinase. Biochemistry 3, 1022-1033.
    • (1964) Biochemistry , vol.3 , pp. 1022-1033
    • Krebs, E.W.1    Love, D.2    Bratvild, G.E.3    Trayer, K.A.4    Meyer, W.5    Fischer, E.H.6
  • 85
    • 0014080718 scopus 로고
    • Reversible stimulation of muscle phosphorylase b kinase by low concentrations of calcium ions
    • Ozawa, E., Hosoi, K. and Ebashi, S. (1967) Reversible stimulation of muscle phosphorylase b kinase by low concentrations of calcium ions. J. Biochem. 61, 531-533.
    • (1967) J. Biochem. , vol.61 , pp. 531-533
    • Ozawa, E.1    Hosoi, K.2    Ebashi, S.3
  • 86
    • 0015289941 scopus 로고
    • Activation of phosphorylase b kinase by a minute amount of Ca ion
    • Ozawa, E. (1972) Activation of phosphorylase b kinase by a minute amount of Ca ion. J. Biochem. 71, 321-331.
    • (1972) J. Biochem. , vol.71 , pp. 321-331
    • Ozawa, E.1
  • 87
    • 0003025297 scopus 로고
    • The effect of potassium on the excitability and resting metabolism of frog's muscle
    • Solandt, D.Y. (1936) The effect of potassium on the excitability and resting metabolism of frog's muscle. J. Physiol. 86, 162-170.
    • (1936) J. Physiol. , vol.86 , pp. 162-170
    • Solandt, D.Y.1
  • 89
    • 0015912123 scopus 로고
    • The subunit structure of rabbitskeletal-muscle phosphorylase kinase, and molecular basis of its activation reactions
    • Cohen, P. (1973) The subunit structure of rabbitskeletal-muscle phosphorylase kinase, and molecular basis of its activation reactions. Eur. J. Biochem. 34, 1-14.
    • (1973) Eur. J. Biochem. , vol.34 , pp. 1-14
    • Cohen, P.1
  • 90
    • 0014959948 scopus 로고
    • Cell communication, calcium ion, and cyclic adenosin monophosphate
    • Rasmussen, H. (1970) Cell communication, calcium ion, and cyclic adenosin monophosphate. Science 170, 404-412.
    • (1970) Science , vol.170 , pp. 404-412
    • Rasmussen, H.1
  • 93
    • 0014300929 scopus 로고
    • 2+. II. Identification of the Kinase Activating Factor as a proteolytic enzyme
    • 2+. II. Identification of the Kinase Activating Factor as a proteolytic enzyme. Biochemistry 7, 2116-2122.
    • (1968) Biochemistry , vol.7 , pp. 2116-2122
    • Huston, R.B.1    Krebs, E.G.2
  • 94
    • 0014121449 scopus 로고
    • Requirement of Ca ion for the stimulating effect of cyclic 3′, 5′-AMP on muscle phosphorylase b kinase
    • Ozawa, E. and Ebashi, S. (1967) Requirement of Ca ion for the stimulating effect of cyclic 3′,5′-AMP on muscle phosphorylase b kinase. J. Biochem. 62, 285-286.
    • (1967) J. Biochem. , vol.62 , pp. 285-286
    • Ozawa, E.1    Ebashi, S.2
  • 95
    • 0014409394 scopus 로고
    • An adenosine 3′, 5′-monophosphate-dependent protein kinase from rabbit skeletal muscle
    • Walsh, D.A., Perkins, J.P. and Krebs, E.G. (1968) An adenosine 3′,5′-monophosphate-dependent protein kinase from rabbit skeletal muscle. J. Biol. Chem. 243, 3763-3765.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3763-3765
    • Walsh, D.A.1    Perkins, J.P.2    Krebs, E.G.3
  • 96
    • 0015618464 scopus 로고
    • Activation of phosphorylase kinase from brain by small amounts of calcium ion
    • Ozawa, E. (1973) Activation of phosphorylase kinase from brain by small amounts of calcium ion. J. Neurochem. 20, 1487-1488.
    • (1973) J. Neurochem. , vol.20 , pp. 1487-1488
    • Ozawa, E.1
  • 97
    • 82355183270 scopus 로고
    • Introduction
    • (eds. Hidaka, H. and Kakiuchi, S.). Kodansha Scientific, Tokyo (in Japanese)
    • Hidaka, H. and Kakiuchi, S. (1981) Introduction. In Calmodulin (eds. Hidaka, H. and Kakiuchi, S.). Kodansha Scientific, Tokyo, pp. 1-7 (in Japanese).
    • (1981) Calmodulin , pp. 1-7
    • Hidaka, H.1    Kakiuchi, S.2
  • 98
    • 79954631768 scopus 로고
    • Stimulation of activity of cyclic 3′, 5′-nucleotide phosphodiestrase by calcium ion
    • Kakiuchi, S. and Yamazaki, R. (1970) Stimulation of activity of cyclic 3′,5′-nucleotide phosphodiestrase by calcium ion. Proc. Jpn. Acad. 46, 387-392.
    • (1970) Proc. Jpn. Acad. , vol.46 , pp. 387-392
    • Kakiuchi, S.1    Yamazaki, R.2
  • 99
    • 0015935052 scopus 로고
    • Purification and properties of the protein activator of bovine heart cyclic adenosine 3′,5′-monophosphate phosphodiestrase
    • Teo, T.S., Wang, T.H. and Wang, H. (1973) Purification and properties of the protein activator of bovine heart cyclic adenosine 3′,5′-monophosphate phosphodiestrase. J. Biol. Chem. 248, 588-595.
    • (1973) J. Biol. Chem. , vol.248 , pp. 588-595
    • Teo, T.S.1    Wang, T.H.2    Wang, H.3
  • 101
    • 0014934492 scopus 로고
    • Cyclic 3′-5′-nucleotide phosphodiestrase
    • Cheung, W.Y. (1970) Cyclic 3′-5′-nucleotide phosphodiestrase. Biochem. Biophys. Res. Commun. 38, 533-538.
    • (1970) Biochem. Biophys. Res. Commun. , vol.38 , pp. 533-538
    • Cheung, W.Y.1
  • 104
    • 0015578069 scopus 로고
    • Studies on the subunit structure of rabbit skeletal muscle phosphorylase kinase
    • Hayakawa, T., Perkins, J.P. and Krebs, E.G. (1973) Studies on the subunit structure of rabbit skeletal muscle phosphorylase kinase. Biochemistry 12, 574-580.
    • (1973) Biochemistry , vol.12 , pp. 574-580
    • Hayakawa, T.1    Perkins, J.P.2    Krebs, E.G.3
  • 105
    • 0019320864 scopus 로고
    • Isolation and properties of the catalytically active γ subunit of phosphorylase b kinase
    • Skuster, J.R., Chan, K.F.J. and Graves, D.J. (1980) Isolation and properties of the catalytically active γ subunit of phosphorylase b kinase. J. Biol. Chem. 255, 2203-2210.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2203-2210
    • Skuster, J.R.1    Chan, K.F.J.2    Graves, D.J.3
  • 106
    • 0018198417 scopus 로고
    • 2+-sependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase
    • 2+-sependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. FEBS Lett. 92, 287-293.
    • (1978) FEBS Lett. , vol.92 , pp. 287-293
    • Cohen, P.1    Burchell, A.2    Foulkes, G.3    Cohen, P.T.W.4
  • 107
    • 0019137715 scopus 로고
    • Phosphorylase kinase from rabbit skeletal muscle: Identification of the calmodulin-binding subunits
    • Picton, C., Klee, C.B. and Cohen, P. (1980) Phosphorylase kinase from rabbit skeletal muscle: Identification of the calmodulin-binding subunits. Eur. J. Biochem. 111, 553-561.
    • (1980) Eur. J. Biochem. , vol.111 , pp. 553-561
    • Picton, C.1    Klee, C.B.2    Cohen, P.3
  • 108
    • 0017745032 scopus 로고
    • Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues
    • Takai, Y., Kishimoto, A., Inoue, M. and Nishizuka, Y. (1977) Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. J. Biol. Chem. 252, 7603-7609.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7603-7609
    • Takai, Y.1    Kishimoto, A.2    Inoue, M.3    Nishizuka, Y.4
  • 109
    • 0018800888 scopus 로고
    • Calciumdependent activation of a multifunctional protein kinase by membrane phospholipids
    • Takai, Y., Kishimoto, A., Iwasa, Y., Kawahara, Y., Mori, T. and Nishizuka, Y. (1979) Calciumdependent activation of a multifunctional protein kinase by membrane phospholipids. J. Biol. Chem. 254, 3692-3695.
    • (1979) J. Biol. Chem. , vol.254 , pp. 3692-3695
    • Takai, Y.1    Kishimoto, A.2    Iwasa, Y.3    Kawahara, Y.4    Mori, T.5    Nishizuka, Y.6
  • 110
    • 0018803639 scopus 로고
    • Unsaturated diacetylglycerol as a possible messenger for the activation of calcium-activated, phospholipids-dependent protein kinase system
    • Takai, Y., Kishimoto, A., Kikkawa, U., Mori, T. and Nishizuka, Y. (1979) Unsaturated diacetylglycerol as a possible messenger for the activation of calcium-activated, phospholipids-dependent protein kinase system. Biochem. Biophys. Res. Commun. 91, 1218-1224.
    • (1979) Biochem. Biophys. Res. Commun. , vol.91 , pp. 1218-1224
    • Takai, Y.1    Kishimoto, A.2    Kikkawa, U.3    Mori, T.4    Nishizuka, Y.5
  • 111
    • 0003409119 scopus 로고    scopus 로고
    • 2nd ed. Kluwer Academic/Plenum Pub., New York
    • Dekker, L.V. (2004) Protein kinase C. 2nd ed. Kluwer Academic/Plenum Pub., New York.
    • (2004) Protein kinase C
    • Dekker, L.V.1
  • 112
    • 0001070415 scopus 로고
    • A neutral, Ca-activated proteinase from the soluble fraction of rat brain
    • Guroff, G. (1964) A neutral, Ca-activated proteinase from the soluble fraction of rat brain. J. Biol. Chem. 239, 149-155.
    • (1964) J. Biol. Chem. , vol.239 , pp. 149-155
    • Guroff, G.1
  • 113
    • 0018234999 scopus 로고
    • Calciuminduced interaction of microtubule formation in brain extracts
    • Sandoval, I.V. and Weber, K. (1978) Calciuminduced interaction of microtubule formation in brain extracts. Eur. J. Biochem. 92, 463-470.
    • (1978) Eur. J. Biochem. , vol.92 , pp. 463-470
    • Sandoval, I.V.1    Weber, K.2
  • 115
    • 0021749729 scopus 로고
    • Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease for a thiol protease and a calcium-binding protein?
    • Ohno, S., Emori, Y., Imajoh, S., Kawasaki, H., Kisaragi, M. and Suzuki, K. (1984) Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease for a thiol protease and a calcium-binding protein? Nature 312, 566-570.
    • (1984) Nature , vol.312 , pp. 566-570
    • Ohno, S.1    Emori, Y.2    Imajoh, S.3    Kawasaki, H.4    Kisaragi, M.5    Suzuki, K.6
  • 116
    • 79959301027 scopus 로고    scopus 로고
    • Calpain chronicle-an enzyme family under multidisciplinary characterization
    • Sorimachi, H., Hata, S. and Ono, Y. (2011) Calpain chronicle-an enzyme family under multidisciplinary characterization. Proc. Jpn. Acad., Ser. B 87, 287-327.
    • (2011) Proc. Jpn. Acad., Ser. B , vol.87 , pp. 287-327
    • Sorimachi, H.1    Hata, S.2    Ono, Y.3
  • 117
    • 77958557373 scopus 로고    scopus 로고
    • Our trails and trials in the subsarcolemmal cytoskeleton network and muscular dystrophy researches in the dystrophin era
    • Ozawa, E. (2010) Our trails and trials in the subsarcolemmal cytoskeleton network and muscular dystrophy researches in the dystrophin era. Proc. Jpn. Acad., Ser. B 86, 798-820.
    • (2010) Proc. Jpn. Acad., Ser. B , vol.86 , pp. 798-820
    • Ozawa, E.1
  • 121
    • 0019026208 scopus 로고
    • Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent kinase and phosphorylase kinase
    • Embi, N., Rylatt, D.B. and Cohen, P. (1980) Glycogen synthase kinase-3 from rabbit skeletal muscle. Separation from cyclic-AMP-dependent kinase and phosphorylase kinase. Eur. J. Biochem. 107, 519-527.
    • (1980) Eur. J. Biochem. , vol.107 , pp. 519-527
    • Embi, N.1    Rylatt, D.B.2    Cohen, P.3
  • 122
    • 13844260647 scopus 로고    scopus 로고
    • Malignant hyperthermia
    • (eds. Engel, A.G. and Franzini-Armstrong, C.). McGraw Hill, New York
    • Wedel, D. and McLennan, D.H. (2004) Malignant hyperthermia. In Myology (eds. Engel, A.G. and Franzini-Armstrong, C.). McGraw Hill, New York, pp. 1663-1676.
    • (2004) Myology , pp. 1663-1676
    • Wedel, D.1    McLennan, D.H.2
  • 123
    • 70349686734 scopus 로고    scopus 로고
    • Calcium-induced calcium release in skeletal muscle
    • Endo, M. (2009) Calcium-induced calcium release in skeletal muscle. Physiol. Rev. 89, 1153-1176.
    • (2009) Physiol. Rev. , vol.89 , pp. 1153-1176
    • Endo, M.1
  • 124
    • 15444360946 scopus 로고
    • Malignant hyperpyrexia. Effect of halothane on single skinned fibers
    • Takagi, A., Sugita, H., Toyokura, Y. and Endo, M. (1976) Malignant hyperpyrexia. Effect of halothane on single skinned fibers. Proc. Jpn. Acad. 52, 603-606.
    • (1976) Proc. Jpn. Acad. , vol.52 , pp. 603-606
    • Takagi, A.1    Sugita, H.2    Toyokura, Y.3    Endo, M.4
  • 125
    • 16444386608 scopus 로고    scopus 로고
    • Non lysosomal glycogenosis
    • (3rd ed., eds. Engel, A. and Franzini-Armstrong, C.). McGraw-Hill, New York
    • DiMauro, S., Hays, A.P. and Tsujino, S. (2004) Non lysosomal glycogenosis. In Myology (3rd ed., eds. Engel, A. and Franzini-Armstrong, C.). McGraw-Hill, New York, Vol. II, pp. 1535-1558.
    • (2004) Myology , vol.2 , pp. 1535-1558
    • DiMauro, S.1    Hays, A.P.2    Tsujino, S.3


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