메뉴 건너뛰기




Volumn 164, Issue 4, 1998, Pages 381-388

Regulation of the cross-bridge cycle: The effects of MgADP, LC17 isoforms and telokin

Author keywords

Caged compounds; Cross bridges; Myosin; Myosin light chains; Smooth muscle; Telokin

Indexed keywords

8 BROMO CYCLIC AMP; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; CALCIUM ION; CYCLIC AMP; CYCLIC GMP; FORSKOLIN; MYOSIN; MYOSIN LIGHT CHAIN; NUCLEOTIDE; PHOSPHOTRANSFERASE; TELOKIN; UNCLASSIFIED DRUG;

EID: 0032436266     PISSN: 00016772     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-201X.1998.tb10695.x     Document Type: Conference Paper
Times cited : (12)

References (63)
  • 2
    • 0020392227 scopus 로고
    • Mechanical characteristics of chemically skinned guinea-pig taenia coli
    • Arner, A. 1982. Mechanical characteristics of chemically skinned guinea-pig taenia coli. Pflug Arch 395, 277-284.
    • (1982) Pflug Arch , vol.395 , pp. 277-284
    • Arner, A.1
  • 3
    • 0022034172 scopus 로고
    • Effects of calcium and substrate on force-velocity relation and energy turnover in skinned smooth muscle of the guinea-pig
    • Arner, A. & Hellstrand, P. 1985. Effects of calcium and substrate on force-velocity relation and energy turnover in skinned smooth muscle of the guinea-pig. J Physiol 360, 347-365.
    • (1985) J Physiol , vol.360 , pp. 347-365
    • Arner, A.1    Hellstrand, P.2
  • 5
    • 0020730258 scopus 로고
    • Chemical energy usage during shortening and work production in mammalian smooth muscle
    • Butler, T.M., Siegman, M.J. & Mooers, S.U. 1983. Chemical energy usage during shortening and work production in mammalian smooth muscle. Am J Physiol 244, C234-C242.
    • (1983) Am J Physiol , vol.244
    • Butler, T.M.1    Siegman, M.J.2    Mooers, S.U.3
  • 6
    • 0028136286 scopus 로고
    • The creatine kinase system in smooth muscle
    • Clark, J.F. 1994. The creatine kinase system in smooth muscle. Mol Cell Biochem 133/134, 221-232.
    • (1994) Mol Cell Biochem , vol.133-134 , pp. 221-232
    • Clark, J.F.1
  • 7
    • 0019433353 scopus 로고
    • Myosin phosphorylation and the crossbriclge cycle in arterial smooth muscle
    • Dillon, P., Aksey, M., Driska, S. & Murphy, R.A. 1981. Myosin phosphorylation and the crossbriclge cycle in arterial smooth muscle. Science 211, 495-497.
    • (1981) Science , vol.211 , pp. 495-497
    • Dillon, P.1    Aksey, M.2    Driska, S.3    Murphy, R.A.4
  • 8
    • 0031137872 scopus 로고    scopus 로고
    • 2-terminal-inserted myosin II heavy chain is expressed in smooth muscle of small muscular arteries
    • 2-terminal-inserted myosin II heavy chain is expressed in smooth muscle of small muscular arteries. Am Physiol 272, C1532-1542.
    • (1997) Am Physiol , vol.272
    • DiSanto, M.E.1    Cox, R.H.2    Wang, Z.3    Chacko, S.4
  • 9
    • 0024536584 scopus 로고
    • Myosin dephosphorylation during rapid relaxation of hog carotid artery smooth muscle
    • Driska, S.P., Stein, P.G. & Porter, R. 1989. Myosin dephosphorylation during rapid relaxation of hog carotid artery smooth muscle. Am J Physiol 256, C315-C321.
    • (1989) Am J Physiol , vol.256
    • Driska, S.P.1    Stein, P.G.2    Porter, R.3
  • 10
    • 0018333803 scopus 로고
    • The velocity of unloaded shortening and its relation to sarcomere length and isometric force in verterbrate muscle fibres
    • Edman, K.A.P. 1979. The velocity of unloaded shortening and its relation to sarcomere length and isometric force in verterbrate muscle fibres. J Physiol 291, 143-159.
    • (1979) J Physiol , vol.291 , pp. 143-159
    • Edman, K.A.P.1
  • 11
    • 0028186819 scopus 로고
    • Progress in understanding the mechanism and function of cyclic GMP-dependent protein kinase
    • Francis, S.H. & Corbin, J.D. 1994. Progress in understanding the mechanism and function of cyclic GMP-dependent protein kinase. Adv Pharmacol 26, 115-170.
    • (1994) Adv Pharmacol , vol.26 , pp. 115-170
    • Francis, S.H.1    Corbin, J.D.2
  • 12
    • 0027787986 scopus 로고
    • Flash photolysis studies of relaxtion and crossbridge detachment: Higher sensitivity of tonic than phasic smooth muscle to MgADP
    • Fuglsang, A., Khromov, A., Torok, K., Somlyo, A.V. & Somlyo, A.P. 1993. Flash photolysis studies of relaxtion and crossbridge detachment: higher sensitivity of tonic than phasic smooth muscle to MgADP. J Mus Res Cell Motil 14, 666-673.
    • (1993) J Mus Res Cell Motil , vol.14 , pp. 666-673
    • Fuglsang, A.1    Khromov, A.2    Torok, K.3    Somlyo, A.V.4    Somlyo, A.P.5
  • 13
    • 0026343743 scopus 로고
    • The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin
    • Gallagher, P.J. & Herring, B.P. 1991. The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin. J Biol Chem 266, 23945-23952.
    • (1991) J Biol Chem , vol.266 , pp. 23945-23952
    • Gallagher, P.J.1    Herring, B.P.2
  • 15
    • 0024574354 scopus 로고
    • Cross-bridge dephosphorylation and relaxation of vascular smooth muscle
    • Hai, C. & Murphy, R.A. 1989. Cross-bridge dephosphorylation and relaxation of vascular smooth muscle. Am J Physiol 256, C282-C287.
    • (1989) Am J Physiol , vol.256
    • Hai, C.1    Murphy, R.A.2
  • 16
    • 0001068154 scopus 로고
    • Biochemistry of the contractile process in smooth muscle
    • L.R. Johnson (ed.) Raven Press, New York
    • Hartshorne, D.J. 1987. Biochemistry of the contractile process in smooth muscle. In: L.R. Johnson (ed.) Physiology of the Gastrointestinal Tract, 2nd edn, pp. 423-482. Raven Press, New York.
    • (1987) Physiology of the Gastrointestinal Tract, 2nd Edn , pp. 423-482
    • Hartshorne, D.J.1
  • 18
    • 0026771997 scopus 로고
    • Role of 17-kDa essential light chain isororms of aorta smooth muscle myosin
    • Hasegawa, Y. & Morita, F. 1992. Role of 17-kDa essential light chain isororms of aorta smooth muscle myosin. J Biochem 111, 804-809.
    • (1992) J Biochem , vol.111 , pp. 804-809
    • Hasegawa, Y.1    Morita, F.2
  • 19
    • 0022341592 scopus 로고
    • Phosphorylation of myosin light chain kinase from vascular smooth muscle by cAMP and cGMP dependent protein kinases
    • Hathaway, D.R., Konicki, M.V. & Coolican, S.A. 1985. Phosphorylation of myosin light chain kinase from vascular smooth muscle by cAMP and cGMP dependent protein kinases. J Mol Cell Cardiol 17, 841-850.
    • (1985) J Mol Cell Cardiol , vol.17 , pp. 841-850
    • Hathaway, D.R.1    Konicki, M.V.2    Coolican, S.A.3
  • 20
    • 0029746677 scopus 로고    scopus 로고
    • Telokin expression is mediated by a smooth muscle cell-specific promoter
    • Herring, B.P. & Smith, A.F. 1996. Telokin expression is mediated by a smooth muscle cell-specific promoter. Am J Physiol 270, 1656-1665.
    • (1996) Am J Physiol , vol.270 , pp. 1656-1665
    • Herring, B.P.1    Smith, A.F.2
  • 21
    • 0030938768 scopus 로고    scopus 로고
    • Telokin expression in AlO smooth muscle cells requires serum response factor
    • Herring, B.P. & Smith, A.F. 1997. Telokin expression in AlO smooth muscle cells requires serum response factor. Am J Physiol 272, C1394-C1404.
    • (1997) Am J Physiol , vol.272
    • Herring, B.P.1    Smith, A.F.2
  • 22
    • 0024421567 scopus 로고
    • Kinetics of contraction initiated by flash photolysis of caged adenosine triphosphate in tonic and phasic smooth muscles
    • Horiuti, K., Somlyo, A.V., Goldman, Y.E. & Somlyo, A.P. 1989. Kinetics of contraction initiated by flash photolysis of caged adenosine triphosphate in tonic and phasic smooth muscles, J Gen Physiol 94, 769-781.
    • (1989) J Gen Physiol , vol.94 , pp. 769-781
    • Horiuti, K.1    Somlyo, A.V.2    Goldman, Y.E.3    Somlyo, A.P.4
  • 23
    • 85038198982 scopus 로고    scopus 로고
    • Conformational changes in the alkali light chains of myosin induced by trifluoperazine and detected using electron paramagnetic resonance and circular dichroism spectroscopy
    • Huang, W., Wilson, G.J., Lam, H. & Hambly, B. 1997. Conformational changes in the alkali light chains of myosin induced by trifluoperazine and detected using electron paramagnetic resonance and circular dichroism spectroscopy. Biophys J 72, A182.
    • (1997) Biophys J , vol.72
    • Huang, W.1    Wilson, G.J.2    Lam, H.3    Hambly, B.4
  • 24
    • 0024330080 scopus 로고
    • Identification of turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase
    • Ito, M., Dabrowska, M., Guerriero, V. & Hartshorne, D.J. 1989. Identification of turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase. J Biol Chem 264, 13971-13974.
    • (1989) J Biol Chem , vol.264 , pp. 13971-13974
    • Ito, M.1    Dabrowska, M.2    Guerriero, V.3    Hartshorne, D.J.4
  • 25
    • 0026570943 scopus 로고
    • Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries
    • Jiang, H., Colbran, J.L., Francis, S.H. & Corbin, J.D. 1992. Direct evidence for cross-activation of cGMP-dependent protein kinase by cAMP in pig coronary arteries. J Biol Chem 267, 1015-1019.
    • (1992) J Biol Chem , vol.267 , pp. 1015-1019
    • Jiang, H.1    Colbran, J.L.2    Francis, S.H.3    Corbin, J.D.4
  • 26
    • 0021894617 scopus 로고
    • The function of myosin light chain kinase phosphorylation in smooth muscle
    • Kamm, K.E. & Stull, J.T. 1985. The function of myosin light chain kinase phosphorylation in smooth muscle. Ann Rev Pharmacol Toxicol 25, 593-620.
    • (1985) Ann Rev Pharmacol Toxicol , vol.25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 27
    • 0029876431 scopus 로고    scopus 로고
    • Roles of light chains in the activity and conformation of smooth muscle myosin
    • Katoh, T. & Morita, F. 1996. Roles of light chains in the activity and conformation of smooth muscle myosin. J Biol Chem 271, 9992-9996.
    • (1996) J Biol Chem , vol.271 , pp. 9992-9996
    • Katoh, T.1    Morita, F.2
  • 28
    • 0027258646 scopus 로고
    • An insert of 7 amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature
    • Kelley, C.A., Takahashi, M., Yu, J.H. & Adelstein, R.S. 1993. An insert of 7 amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature. J Biol Chem 268, 12848-12854.
    • (1993) J Biol Chem , vol.268 , pp. 12848-12854
    • Kelley, C.A.1    Takahashi, M.2    Yu, J.H.3    Adelstein, R.S.4
  • 29
    • 0023505706 scopus 로고
    • 2+-activated contractions in smooth muscle
    • A.P. Somlyo & N.L. Stephens (eds) Alan R. Liss, Inc., New York
    • 2+-activated contractions in smooth muscle. In: A.P. Somlyo & N.L. Stephens (eds) Regulation and Contraction of Smooth Muscle, pp. 437-448. Alan R. Liss, Inc., New York.
    • (1987) Regulation and Contraction of Smooth Muscle , pp. 437-448
    • Kerrick, W.G.1    Hoar, P.E.2
  • 30
    • 0031709567 scopus 로고    scopus 로고
    • MgADP promotes a catch-like state developed through force-calcium hysteresis in tonic smooth muscle
    • in press
    • Khromov, A.S., Somlyo, A.V. & Somlyo, A.P. 1998. MgADP promotes a catch-like state developed through force-calcium hysteresis in tonic smooth muscle. Biophys J (in press).
    • (1998) Biophys J
    • Khromov, A.S.1    Somlyo, A.V.2    Somlyo, A.P.3
  • 31
    • 0029930738 scopus 로고    scopus 로고
    • Nucleotide binding by actomyosm as a determinant of relaxation kinetics of rabbit phasic and tonic smooth muscle
    • Khromov, A., Somlyo, A.V. & Somlyo, A.P. 1996. Nucleotide binding by actomyosm as a determinant of relaxation kinetics of rabbit phasic and tonic smooth muscle. J Physiol 492, 669-673.
    • (1996) J Physiol , vol.492 , pp. 669-673
    • Khromov, A.1    Somlyo, A.V.2    Somlyo, A.P.3
  • 32
    • 0028857092 scopus 로고
    • The role of MgADP in force maintenance by dephosphorylated cross-bridges in smooth muscle: A flash photolysis study
    • Khromov, A.S., Somlyo, A.V., Trentham, D.R., Zimmermann, B. & Somlyo, A.P. 1995. The role of MgADP in force maintenance by dephosphorylated cross-bridges in smooth muscle: a flash photolysis study. Biophys J 69, 2611-2622.
    • (1995) Biophys J , vol.69 , pp. 2611-2622
    • Khromov, A.S.1    Somlyo, A.V.2    Trentham, D.R.3    Zimmermann, B.4    Somlyo, A.P.5
  • 33
    • 0029814390 scopus 로고    scopus 로고
    • Phosphorylation of the inositol 1,4,5-trisphosphate receptor: Cyclic GMP-dependent protein kinase mediates cAMP and cGMP dependent phosphorylation in the intact rat aorta
    • Komalavilas, P. & Lincoln, T.M. 1996. Phosphorylation of the inositol 1,4,5-trisphosphate receptor: cyclic GMP-dependent protein kinase mediates cAMP and cGMP dependent phosphorylation in the intact rat aorta. J Biol Chem 271, 21933-21938.
    • (1996) J Biol Chem , vol.271 , pp. 21933-21938
    • Komalavilas, P.1    Lincoln, T.M.2
  • 34
    • 18144450120 scopus 로고
    • Phosphagen and metabolite content during contraction in porcine carotid artery
    • Krisanda, J.M. & Paul, R.J. 1983. Phosphagen and metabolite content during contraction in porcine carotid artery. Am J Physiol 244, C385-C390.
    • (1983) Am J Physiol , vol.244
    • Krisanda, J.M.1    Paul, R.J.2
  • 35
    • 0021321488 scopus 로고
    • Increased phosphorylation of myosin light chain kinase after an increase in cyclic AMP in intact smooth muscle
    • de Lanerolle, P., Nishikawa, M., Yost, D.A. & Adelstein, R.S. 1984. Increased phosphorylation of myosin light chain kinase after an increase in cyclic AMP in intact smooth muscle. Science 223, 1415-1417.
    • (1984) Science , vol.223 , pp. 1415-1417
    • Lanerolle, P.1    Nishikawa, M.2    Yost, D.A.3    Adelstein, R.S.4
  • 36
    • 0031057516 scopus 로고    scopus 로고
    • 2+-desensitization in vascular smooth muscle by activating the myosin light chain phosphatase
    • 2+-desensitization in vascular smooth muscle by activating the myosin light chain phosphatase. J Biol Chem 272, 5063-5068.
    • (1997) J Biol Chem , vol.272 , pp. 5063-5068
    • Lee, M.W.1    Ti, L.2    Kitazawa, T.3
  • 37
    • 0025817957 scopus 로고
    • Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle
    • Malmqvist, U. & Arner, A. 1991. Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening velocity in smooth muscle. Pflug Arch 418, 523-530.
    • (1991) Pflug Arch , vol.418 , pp. 523-530
    • Malmqvist, U.1    Arner, A.2
  • 38
    • 0030832240 scopus 로고    scopus 로고
    • Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed
    • Malmqvist, U., Trybus, K.M., Yagi, S., Carmichael, J. & Fay, F.S. 1997. Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed. Proc Natl Acad Sci USA 94, 7655-7660.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7655-7660
    • Malmqvist, U.1    Trybus, K.M.2    Yagi, S.3    Carmichael, J.4    Fay, F.S.5
  • 39
    • 0032553296 scopus 로고    scopus 로고
    • Myosin essential light chain isoforms modulate the velocity of shortening propelled by non phosphorylated cross bridges
    • in press
    • Matthew, J.D., Khromov, A.S., Trybus, K.M., Somlyo, A.P. & Somlyo, A.V. 1998. Myosin essential light chain isoforms modulate the velocity of shortening propelled by non phosphorylated cross bridges, J Biol Chem (in press).
    • (1998) J Biol Chem
    • Matthew, J.D.1    Khromov, A.S.2    Trybus, K.M.3    Somlyo, A.P.4    Somlyo, A.V.5
  • 40
    • 0027963629 scopus 로고
    • Correlation between high temperature dependence of smooth muscle myosinlight chain phosphatase activity and muscle relaxation rate
    • Mitsui, T., Kitazawa, T. & Ikebe, M 1994. Correlation between high temperature dependence of smooth muscle myosinlight chain phosphatase activity and muscle relaxation rate. J Biol Chem 269, 5842-5848.
    • (1994) J Biol Chem , vol.269 , pp. 5842-5848
    • Mitsui, T.1    Kitazawa, T.2    Ikebe, M.3
  • 41
    • 17344389756 scopus 로고
    • 2+-dependent stress maintenance in skinned swine carotid media
    • 2+-dependent stress maintenance in skinned swine carotid media. Am J Physiol 251, C892-C903.
    • (1986) Am J Physiol , vol.251
    • Moreland, R.S.1    Murphy, R.A.2
  • 42
    • 0023645308 scopus 로고
    • Nonmuscle and smooth muscle light chain mRNAs are generated from a single gene by tissue specific alternative RNA splicing
    • Nabeshima, Y., Nameshima, Y., Nonomura, Y. & Fujii-Kuriyama, Y. 1987. Nonmuscle and smooth muscle light chain mRNAs are generated from a single gene by tissue specific alternative RNA splicing. J Biol Chem 262, 10608-10612.
    • (1987) J Biol Chem , vol.262 , pp. 10608-10612
    • Nabeshima, Y.1    Nameshima, Y.2    Nonomura, Y.3    Fujii-Kuriyama, Y.4
  • 43
    • 0024433914 scopus 로고
    • Direct regulation of smooth muscle contractile elements by second messengers
    • Nishimura, J. & van Breemen, C. 1989. Direct regulation of smooth muscle contractile elements by second messengers. Biochem Biophys Res Comm 163, 929-935.
    • (1989) Biochem Biophys Res Comm , vol.163 , pp. 929-935
    • Nishimura, J.1    Van Breemen, C.2
  • 44
    • 0025997465 scopus 로고
    • ++ sensitivity of permeabilized rabbit mesenteric artery: Possible involvement of a second Ca regulatory system in smooth muscle contraction
    • ++ sensitivity of permeabilized rabbit mesenteric artery: possible involvement of a second Ca regulatory system in smooth muscle contraction. J Pharmacol Exp Ther 258, 397-402.
    • (1991) J Pharmacol Exp Ther , vol.258 , pp. 397-402
    • Nishimura, J.1    Van Breemen, C.V.2
  • 45
    • 0027408994 scopus 로고
    • The effects of MgADP on crossbridge kinetics: A laser flash photolysis study of guinea-pig smooth muscle
    • Nishiye, E., Somlyo, A.V., Torok, K. & Somlyo, A.P. 1993. The effects of MgADP on crossbridge kinetics: A laser flash photolysis study of guinea-pig smooth muscle. J Physiol 460, 247-271.
    • (1993) J Physiol , vol.460 , pp. 247-271
    • Nishiye, E.1    Somlyo, A.V.2    Torok, K.3    Somlyo, A.P.4
  • 46
    • 0022553832 scopus 로고
    • Cyclic GMP-dependent protein kinase relaxes skinned fibers from guinea pig taenia coli
    • Pfitzer, G., Merkel, L., Rüegg, J.C. & Hofmann, F. 1986. Cyclic GMP-dependent protein kinase relaxes skinned fibers from guinea pig taenia coli. Pflug Arch 407, 87-91.
    • (1986) Pflug Arch , vol.407 , pp. 87-91
    • Pfitzer, G.1    Merkel, L.2    Rüegg, J.C.3    Hofmann, F.4
  • 49
    • 0019137357 scopus 로고
    • Chemical energetics of force development, force maintenance, and relaxation in mammalian smooth muscle
    • Siegman, M.J., Butler, T.M., Mooers, S.U. & Davies, R.E. 1980. Chemical energetics of force development, force maintenance, and relaxation in mammalian smooth muscle. J Gen Physiol 76, 609-629.
    • (1980) J Gen Physiol , vol.76 , pp. 609-629
    • Siegman, M.J.1    Butler, T.M.2    Mooers, S.U.3    Davies, R.E.4
  • 50
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • Siemankowski, R.F., Wiseman, M.O. & White, H.D. 1985. ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci USA 82, 658-662.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 658-662
    • Siemankowski, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 52
    • 0030936358 scopus 로고    scopus 로고
    • Purification and characterization of a smooth muscle myosin light chain kinase-phosphatase complex
    • Sobieszek, A., Borkowski, J. & Babiychuk, V.S. 1997. Purification and characterization of a smooth muscle myosin light chain kinase-phosphatase complex. J Biol Chem 272, 7034-7041.
    • (1997) J Biol Chem , vol.272 , pp. 7034-7041
    • Sobieszek, A.1    Borkowski, J.2    Babiychuk, V.S.3
  • 53
    • 0023832001 scopus 로고
    • Crossbridge kinetics, cooperactivity and negatively strained crossbridges in vertebrate smooth muscle: A laser flash photolysis study
    • Somlyo, A.V., Goldman, Y.E., Fujimori, T., Bond, M., Trentham, D.R. & Somlyo, A.F. 1988. Crossbridge kinetics, cooperactivity and negatively strained crossbridges in vertebrate smooth muscle: A laser flash photolysis study. J Gen Physiol 91, 165-192.
    • (1988) J Gen Physiol , vol.91 , pp. 165-192
    • Somlyo, A.V.1    Goldman, Y.E.2    Fujimori, T.3    Bond, M.4    Trentham, D.R.5    Somlyo, A.F.6
  • 55
    • 0005483362 scopus 로고
    • Active state and catch-like state in rabbit main pulmonary artery
    • Somlyo, A.V. & Somlyo, A.P. 1967. Active state and catch-like state in rabbit main pulmonary artery. J Gen Physiol 50, 168-169.
    • (1967) J Gen Physiol , vol.50 , pp. 168-169
    • Somlyo, A.V.1    Somlyo, A.P.2
  • 56
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo, A.P. & Somlyo, A.V. 1994. Signal transduction and regulation in smooth muscle. Nature 372, 231-236.
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 58
    • 0028220979 scopus 로고
    • Coupling of ATPase activity and motility in smooth muscle myosin is mediated by the regulatory light chain
    • Trybus, K.M., Waller, G.S. & Chatman, T.A. 1994. Coupling of ATPase activity and motility in smooth muscle myosin is mediated by the regulatory light chain. J Cell Biol 124, 963-969.
    • (1994) J Cell Biol , vol.124 , pp. 963-969
    • Trybus, K.M.1    Waller, G.S.2    Chatman, T.A.3
  • 60
    • 0027223294 scopus 로고
    • Identification of a novel smooth muscle myosin heavy chain of cDNA: Isoform diversity in the S1 head region
    • White, S., Martin, A.E. & Periasamy, M. 1993. Identification of a novel smooth muscle myosin heavy chain of cDNA: isoform diversity in the S1 head region. Am J Physiol 264, C1252-C1258.
    • (1993) Am J Physiol , vol.264
    • White, S.1    Martin, A.E.2    Periasamy, M.3
  • 61
    • 0032080256 scopus 로고    scopus 로고
    • Acceleration of regulatory myosin light chain dephosphorylation and relaxation of smooth muscle-by telokin and cyclic nucleotide-activated kinase
    • Wu, X., Haystead, T.A.J., Nakamoto, R.K., Somlyo, A.V. & Somlyo, A.P. 1998. Acceleration of regulatory myosin light chain dephosphorylation and relaxation of smooth muscle-by telokin and cyclic nucleotide-activated kinase. J Biol Chem 273, 11362-11369.
    • (1998) J Biol Chem , vol.273 , pp. 11362-11369
    • Wu, X.1    Haystead, T.A.J.2    Nakamoto, R.K.3    Somlyo, A.V.4    Somlyo, A.P.5
  • 62
    • 0029892621 scopus 로고    scopus 로고
    • Cyclic GMP-dependent stimulation reverses G-protein-coupled inhibition of smooth muscle myosin light chain phosphatase
    • Wu, X., Somlyo, A.V. & Somlyo, A.P. 1996. Cyclic GMP-dependent stimulation reverses G-protein-coupled inhibition of smooth muscle myosin light chain phosphatase. Biochem Biophys Res Comm 220, 658-663.
    • (1996) Biochem Biophys Res Comm , vol.220 , pp. 658-663
    • Wu, X.1    Somlyo, A.V.2    Somlyo, A.P.3
  • 63
    • 0028793840 scopus 로고
    • Restoration of phosphorylation-dependent regulation to the skeletal muscle myosin regulatory light chain
    • Yang, Z. & Sweeney, H.L. 1995. Restoration of phosphorylation-dependent regulation to the skeletal muscle myosin regulatory light chain. J Biol Chem 270, 24646-24649.
    • (1995) J Biol Chem , vol.270 , pp. 24646-24649
    • Yang, Z.1    Sweeney, H.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.