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Volumn 516, Issue 3, 1999, Pages 805-824

Ca2+-independent phosphorylation of myosin in rat caudal artery and chicken gizzard myofilaments

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CYANOGINOSIN; MYOSIN; MYOSIN LIGHT CHAIN KINASE; SERINE; SYNTHETIC PEPTIDE; THREONINE; TRITON X 100; CALCIUM; CALMODULIN; CYCLOPEPTIDE; MYOSIN LIGHT CHAIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE; ALANYLLYSYLLYSYLLEUCYLALANYLLYSYLASPARTYLARGINYLMETHIONYLLYSYLLYSYLTYROSINYLMETHIONYLALANYLARGINYLARGINYLLYSYLLEUCYLGLUTAMINYLLYSYLALANYLGLYCYLHISTIDYLALANYLVALINE; CALCIUM INDEPENDENT KINASE; MICROCYSTIN LR; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

EID: 0033134836     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1469-7793.1999.0805u.x     Document Type: Article
Times cited : (133)

References (65)
  • 1
    • 0021115960 scopus 로고
    • Identification of the native form of chicken gizzard myosin light chain kinase with the aid of monoclonal antibodies
    • ADACHI, K., CARRUTHERS, C. A. & WALSH, M. P. (1983). Identification of the native form of chicken gizzard myosin light chain kinase with the aid of monoclonal antibodies. Biochemical and Biophysical Research Communications 115, 855-863.
    • (1983) Biochemical and Biophysical Research Communications , vol.115 , pp. 855-863
    • Adachi, K.1    Carruthers, C.A.2    Walsh, M.P.3
  • 2
    • 0028075454 scopus 로고
    • Identification and characterization of protein kinase Cζ-immunoreactive proteins
    • ALLEN, B. G., ANDREA, J. E. & WALSH, M. P. (1994). Identification and characterization of protein kinase Cζ-immunoreactive proteins. Journal of Biological Chemistry 269, 29288-29298.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 29288-29298
    • Allen, B.G.1    Andrea, J.E.2    Walsh, M.P.3
  • 4
    • 0030008340 scopus 로고    scopus 로고
    • Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences
    • BAYLEY, P. M., FINDLAY, W. A. & MARTIN, S. R. (1996). Target recognition by calmodulin: Dissecting the kinetics and affinity of interaction using short peptide sequences. Protein Science 5, 1215-1228.
    • (1996) Protein Science , vol.5 , pp. 1215-1228
    • Bayley, P.M.1    Findlay, W.A.2    Martin, S.R.3
  • 5
    • 0028822081 scopus 로고
    • Phosphorylation on threonine-18 of the regulatory light chain dissociates the ATPase and motor properties of smooth muscle myosin II
    • BRESNICK, A. R., WOLFF-LONG, V. L., BAUMANN, O. & POLLARD, T. D. (1995). Phosphorylation on threonine-18 of the regulatory light chain dissociates the ATPase and motor properties of smooth muscle myosin II. Biochemistry 34, 12576-12583.
    • (1995) Biochemistry , vol.34 , pp. 12576-12583
    • Bresnick, A.R.1    Wolff-Long, V.L.2    Baumann, O.3    Pollard, T.D.4
  • 10
    • 0026692912 scopus 로고
    • Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle
    • GONG, M. C., COHEN, P., KITAZAWA, T., IKEBE, M., MASUO, M., SOMLYO, A. P. & SOMLYO, A. V. (1992a). Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle. Journal of Biological Chemistry 267, 14662-14668.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 14662-14668
    • Gong, M.C.1    Cohen, P.2    Kitazawa, T.3    Ikebe, M.4    Masuo, M.5    Somlyo, A.P.6    Somlyo, A.V.7
  • 12
    • 0023841161 scopus 로고
    • Cross-bridge phosphorylation and regulation of latch state in smooth muscle
    • HAI, C.-M. & MURPHY, R. A. (1988). Cross-bridge phosphorylation and regulation of latch state in smooth muscle. American Journal of Physiology 254, C99-106.
    • (1988) American Journal of Physiology , vol.254
    • Hai, C.-M.1    Murphy, R.A.2
  • 14
  • 15
    • 0020855158 scopus 로고
    • Selective purification of the 20,000-Da light chains of smooth muscle myosin
    • HATHAWAY, D. R. & HAEBERLE, J. R. (1983). Selective purification of the 20,000-Da light chains of smooth muscle myosin. Analytical Biochemistry 135, 37-43.
    • (1983) Analytical Biochemistry , vol.135 , pp. 37-43
    • Hathaway, D.R.1    Haeberle, J.R.2
  • 16
    • 0024788360 scopus 로고
    • Effects of okadaic acid on cytosolic calcium concentrations and on contractions of the porcine coronary artery
    • HIRANO, K., KANAIDE, H. & NAKAMURA, M. (1989). Effects of okadaic acid on cytosolic calcium concentrations and on contractions of the porcine coronary artery. British Journal of Pharmacology 98, 1261-1266.
    • (1989) British Journal of Pharmacology , vol.98 , pp. 1261-1266
    • Hirano, K.1    Kanaide, H.2    Nakamura, M.3
  • 17
    • 0018407218 scopus 로고
    • Chicken gizzard: Relation between calcium-activated phosphorylation and contraction
    • HOAR, P. E., KERRICK, W. G. L. & CASSIDY, P. S. (1979). Chicken gizzard: relation between calcium-activated phosphorylation and contraction. Science 204, 503-506.
    • (1979) Science , vol.204 , pp. 503-506
    • Hoar, P.E.1    Kerrick, W.G.L.2    Cassidy, P.S.3
  • 18
    • 0025732992 scopus 로고
    • A novel protein phosphatase inhibitor, tautomycin. Effect on smooth muscle
    • HORI, M., MAGAE, J., HAN, Y.-G., HARTSHORNE, D. J. & KARAKI, H. (1991). A novel protein phosphatase inhibitor, tautomycin. Effect on smooth muscle. FEBS Letters 285, 145-148.
    • (1991) FEBS Letters , vol.285 , pp. 145-148
    • Hori, M.1    Magae, J.2    Han, Y.-G.3    Hartshorne, D.J.4    Karaki, H.5
  • 19
    • 0029976102 scopus 로고    scopus 로고
    • Phosphorylation of the large subunit of myosin phosphatase and inhibition of phosphatase activity
    • ICHIKAWA, K., ITO, M. & HARTSHORNE, D. J. (1996). Phosphorylation of the large subunit of myosin phosphatase and inhibition of phosphatase activity. Journal of Biological Chemistry 271, 4733-4740.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 4733-4740
    • Ichikawa, K.1    Ito, M.2    Hartshorne, D.J.3
  • 20
    • 0030583303 scopus 로고    scopus 로고
    • Protein kinase C increases force and slows relaxation in smooth muscle: Evidence for regulation of the myosin light chain phosphatase
    • IKEBE, M. & BROZOVICH, F. V. (1996). Protein kinase C increases force and slows relaxation in smooth muscle: evidence for regulation of the myosin light chain phosphatase. Biochemical and Biophysical Research Communications 225, 370-376.
    • (1996) Biochemical and Biophysical Research Communications , vol.225 , pp. 370-376
    • Ikebe, M.1    Brozovich, F.V.2
  • 21
    • 0022410257 scopus 로고
    • Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase
    • IKEBE, M. & HARTSHORNE, D. J. (1985). Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase. Journal of Biological Chemistry 260, 10027-10031.
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 10027-10031
    • Ikebe, M.1    Hartshorne, D.J.2
  • 22
    • 0022650773 scopus 로고
    • Identification, phosphorylation, and dephosphorylation of a second site for myosin light chain kinase on the 20,000-dalton light chain of smooth muscle myosin
    • IKEBE, M., HARTSHORNE, D. J. & ELZINGA, M. (1986). Identification, phosphorylation, and dephosphorylation of a second site for myosin light chain kinase on the 20,000-Dalton light chain of smooth muscle myosin. Journal of Biological Chemistry 261, 36-39.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 36-39
    • Ikebe, M.1    Hartshorne, D.J.2    Elzinga, M.3
  • 23
    • 0023655566 scopus 로고
    • Phosphorylation of the 20,000-dalton light chain of smooth muscle myosin by the calcium-activated, phospholipid-dependent protein kinase. Phosphorylation sites and effects of phosphorylation
    • IKEBE, M., HARTSHORNE, D. J. & ELZINGA, M. (1987). Phosphorylation of the 20,000-Dalton light chain of smooth muscle myosin by the calcium-activated, phospholipid-dependent protein kinase. Phosphorylation sites and effects of phosphorylation. Journal of Biological Chemistry 262, 9569-9573.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 9569-9573
    • Ikebe, M.1    Hartshorne, D.J.2    Elzinga, M.3
  • 24
    • 0023645699 scopus 로고
    • Proteolysis of smooth muscle myosin light chain kinase. Formation of inactive and calmodulin-indepemlent fragments
    • IKEBE, M., STEPINSKA, M., KEMP, B. E., MEANS, A. R. & HARTSHORNE, D. J. (1987). Proteolysis of smooth muscle myosin light chain kinase. Formation of inactive and calmodulin-indepemlent fragments. Journal of Biological Chemistry 262, 13828-13834.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 13828-13834
    • Ikebe, M.1    Stepinska, M.2    Kemp, B.E.3    Means, A.R.4    Hartshorne, D.J.5
  • 25
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • IKURA, M., CLORE, G. M., GRONENBORN, A. M., ZHU, G., KLEE, C. B. & BAX, A. (1992). Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 27
    • 0024512330 scopus 로고
    • Effects of modulators of myosin light-chain kinase activity in single smooth muscle cells
    • ITOH, T., IKEBE, M., KARGACIN, G. J., HARTSHORNE, D. J., KEMP, B. E. & FAY, F. S. (1989). Effects of modulators of myosin light-chain kinase activity in single smooth muscle cells. Nature 338, 164-167.
    • (1989) Nature , vol.338 , pp. 164-167
    • Itoh, T.1    Ikebe, M.2    Kargacin, G.J.3    Hartshorne, D.J.4    Kemp, B.E.5    Fay, F.S.6
  • 29
    • 0027203489 scopus 로고
    • Actin-binding peptide from smooth muscle myosin light chain kinase
    • KANOH, S., ITO, M., NIWA, E., KAWANO, Y. & HARTSHORNE, D. J. (1993). Actin-binding peptide from smooth muscle myosin light chain kinase. Biochemistry 32, 8902-8907.
    • (1993) Biochemistry , vol.32 , pp. 8902-8907
    • Kanoh, S.1    Ito, M.2    Niwa, E.3    Kawano, Y.4    Hartshorne, D.J.5
  • 30
    • 0025040785 scopus 로고
    • Peptide modulators of myosin light chain kinase affect smooth muscle cell contraction
    • KARGACIN, G. J., IKEBE, M. & FAY, F. S. (1990). Peptide modulators of myosin light chain kinase affect smooth muscle cell contraction. American Journal of Physiology 259, C315-324.
    • (1990) American Journal of Physiology , vol.259
    • Kargacin, G.J.1    Ikebe, M.2    Fay, F.S.3
  • 31
    • 0025360751 scopus 로고
    • The relationship between ATPase activity, isometric force, and myosin light-chain phosphorylation and thiophosphorylation in skinned smooth muscle fiber bundles from chicken gizzard
    • KENNEY, R. E., HOAR, P. E. & KERRICK, W. G. L. (1990). The relationship between ATPase activity, isometric force, and myosin light-chain phosphorylation and thiophosphorylation in skinned smooth muscle fiber bundles from chicken gizzard. Journal of Biological Chemistry 265, 8642-8649.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 8642-8649
    • Kenney, R.E.1    Hoar, P.E.2    Kerrick, W.G.L.3
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • LAEMMLI, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0031920581 scopus 로고    scopus 로고
    • Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle
    • LI, L., ETO, M., LEE, M. R., MORITA, F., YAZAWA, M. & KITAZAWA, T. (1998). Possible involvement of the novel CPI-17 protein in protein kinase C signal transduction of rabbit arterial smooth muscle. Journal of Physiology 508, 871-881.
    • (1998) Journal of Physiology , vol.508 , pp. 871-881
    • Li, L.1    Eto, M.2    Lee, M.R.3    Morita, F.4    Yazawa, M.5    Kitazawa, T.6
  • 36
    • 0030897992 scopus 로고    scopus 로고
    • Binding of myosin light chain kinase to cellular actin-myosin filaments
    • LIN, P., LUBY-PHELPS, K. & STULL, J. T. (1997). Binding of myosin light chain kinase to cellular actin-myosin filaments. Journal of Biological Chemistry 272, 7412-7420.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 7412-7420
    • Lin, P.1    Luby-Phelps, K.2    Stull, J.T.3
  • 37
    • 0025333146 scopus 로고
    • Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants
    • MACKINTOSH, C., BEATTIE, K. A., KLUMPP, S., COHEN, P. & CODD, G. A. (1990). Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants. FEBS Letters 264, 187-192.
    • (1990) FEBS Letters , vol.264 , pp. 187-192
    • Mackintosh, C.1    Beattie, K.A.2    Klumpp, S.3    Cohen, P.4    Codd, G.A.5
  • 38
    • 0029088182 scopus 로고
    • The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1
    • MACKINTOSH, R. W., DALBY, K. N., CAMPBELL, D. G., COHEN, P. T. W., COHEN, P. & MACKINTOSH, C. (1995). The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1. FEBS Letters 371, 236-240.
    • (1995) FEBS Letters , vol.371 , pp. 236-240
    • Mackintosh, R.W.1    Dalby, K.N.2    Campbell, D.G.3    Cohen, P.T.W.4    Cohen, P.5    Mackintosh, C.6
  • 39
    • 0028168041 scopus 로고
    • 2+-sensitizing effect of protein kinase C on vascular smooth muscle: Inhibition of myosin light chain phosphatase
    • 2+-sensitizing effect of protein kinase C on vascular smooth muscle: inhibition of myosin light chain phosphatase. Journal of General Physiology 104, 265-286.
    • (1994) Journal of General Physiology , vol.104 , pp. 265-286
    • Masuo, M.1    Reardon, S.2    Ikebe, M.3    Kitazawa, T.4
  • 41
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2·4Å structure of a calmodulin-peptide complex
    • MEADOR, W. E., MEANS, A. R. & QUIOCHO, F. A. (1992). Target enzyme recognition by calmodulin: 2·4Å structure of a calmodulin-peptide complex. Science 257, 1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 42
    • 0030708876 scopus 로고    scopus 로고
    • 1-adrenoceptor-mediated phosphorylation of myosin in rat-tail arterial smooth muscle
    • 1-Adrenoceptor-mediated phosphorylation of myosin in rat-tail arterial smooth muscle. Biochemical Journal 327, 669-674.
    • (1997) Biochemical Journal , vol.327 , pp. 669-674
    • Mita, M.1    Walsh, M.P.2
  • 43
    • 0021338840 scopus 로고
    • Isolation of the native form of chicken gizzard myosin light-chain kinase
    • NGAI, P. K., CARRUTHERS, C. A. & WALSH, M. P. (1984). Isolation of the native form of chicken gizzard myosin light-chain kinase. Biochemical Journal 218, 863-870.
    • (1984) Biochemical Journal , vol.218 , pp. 863-870
    • Ngai, P.K.1    Carruthers, C.A.2    Walsh, M.P.3
  • 45
    • 0023155843 scopus 로고
    • Direct activation by okadaic acid of the contractile elements in the smooth muscle of guinea-pig taenia coli
    • OZAKI, H., KOHAMA, K., NONOMURA, Y., SHIBATA, S. & KARAKI, H. (1987). Direct activation by okadaic acid of the contractile elements in the smooth muscle of guinea-pig taenia coli. Naunyn-Schmiedeberg's Archives of Pharmacology 335, 356-358.
    • (1987) Naunyn-Schmiedeberg's Archives of Pharmacology , vol.335 , pp. 356-358
    • Ozaki, H.1    Kohama, K.2    Nonomura, Y.3    Shibata, S.4    Karaki, H.5
  • 46
    • 0028847677 scopus 로고
    • Embryonic chicken gizzard: Expression of the smooth muscle regulatory proteins caldesmon and myosin light chain kinase
    • PAUL, E. R., NGAI, P. K., WALSH, M. P. & GRÖSCHEL-STEWART, U. (1995). Embryonic chicken gizzard: expression of the smooth muscle regulatory proteins caldesmon and myosin light chain kinase. Cell and Tissue Research 279, 331-337.
    • (1995) Cell and Tissue Research , vol.279 , pp. 331-337
    • Paul, E.R.1    Ngai, P.K.2    Walsh, M.P.3    Gröschel-Stewart, U.4
  • 47
    • 0023710193 scopus 로고
    • Autoregulation of enzymes by pseudosubstrate prototypes: Myosin light chain kinase
    • PEARSON, R. B., WETTENHALL, R. E. H., MEANS, A. R., HARTSHORNE, D. J. & KEMP, B. E. (1988). Autoregulation of enzymes by pseudosubstrate prototypes: myosin light chain kinase. Science 241, 970-972.
    • (1988) Science , vol.241 , pp. 970-972
    • Pearson, R.B.1    Wettenhall, R.E.H.2    Means, A.R.3    Hartshorne, D.J.4    Kemp, B.E.5
  • 48
    • 0019817451 scopus 로고
    • Phosphorylation of smooth muscle myosin: Evidence for cooperativity between the myosin heads
    • PERSECHINI, A. & HARTSHORNE, D. J. (1981). Phosphorylation of smooth muscle myosin: evidence for cooperativity between the myosin heads. Science 213, 1381-1385.
    • (1981) Science , vol.213 , pp. 1381-1385
    • Persechini, A.1    Hartshorne, D.J.2
  • 49
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • RHOADS, A. R. & FRIEDBERG, F. (1997). Sequence motifs for calmodulin recognition. FASEB Journal 11, 331-340.
    • (1997) FASEB Journal , vol.11 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 51
    • 0028955180 scopus 로고
    • The variable coupling between force and myosin light chain phosphorylation in triton-skinned chicken gizzard fibre bundles: Role of myosin light chain phosphatase
    • SCHMIDT, U. S., TROSCHKA, M. & PFITZER, G. (1995). The variable coupling between force and myosin light chain phosphorylation in Triton-skinned chicken gizzard fibre bundles: role of myosin light chain phosphatase. Pflügers Archiv 429, 708-715.
    • (1995) Pflügers Archiv , vol.429 , pp. 708-715
    • Schmidt, U.S.1    Troschka, M.2    Pfitzer, G.3
  • 52
    • 0024024871 scopus 로고
    • Autophosphorylation of smooth-muscle caldesmon
    • SCOTT-WOO, G. C. & WALSH, M. P. (1988). Autophosphorylation of smooth-muscle caldesmon. Biochemical Journal 252, 463-472.
    • (1988) Biochemical Journal , vol.252 , pp. 463-472
    • Scott-Woo, G.C.1    Walsh, M.P.2
  • 54
    • 0028152923 scopus 로고
    • Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle
    • SHIRAZI, A., IIZUKA, K., FADDEN, P., MOSSE, C., SOMLYO, A. P., SOMLYO, A. V. & HAYSTEAD, T. A. J. (1994). Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle. Journal of Biological Chemistry 269, 31598-31606.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 31598-31606
    • Shirazi, A.1    Iizuka, K.2    Fadden, P.3    Mosse, C.4    Somlyo, A.P.5    Somlyo, A.V.6    Haystead, T.A.J.7
  • 55
    • 0024323715 scopus 로고
    • Phosphatase inhibition with okadaic acid does not alter the relationship between force and myosin light chain phosphorylation in permeabilized smooth muscle
    • SIEGMAN, M. J., BUTLER, T. M. & MOOERS, S. U. (1989). Phosphatase inhibition with okadaic acid does not alter the relationship between force and myosin light chain phosphorylation in permeabilized smooth muscle. Biochemical and Biophysical Research Communications 161, 838-842.
    • (1989) Biochemical and Biophysical Research Communications , vol.161 , pp. 838-842
    • Siegman, M.J.1    Butler, T.M.2    Mooers, S.U.3
  • 56
    • 0016821897 scopus 로고
    • Preparation and properties of vertebrate smooth-muscle myofibrils and actomyosin
    • SOBIESZEK, A. & BREMEL, R. D. (1975). Preparation and properties of vertebrate smooth-muscle myofibrils and actomyosin. European Journal of Biochemistry 55, 49-60.
    • (1975) European Journal of Biochemistry , vol.55 , pp. 49-60
    • Sobieszek, A.1    Bremel, R.D.2
  • 57
    • 84988058290 scopus 로고
    • Urea-glycerol-acrylamide gel electrophoresis of acidic low molecular weight muscle proteins: Rapid determination of myosin light chain phosphorylation in myosin, actomyosin and whole muscle samples
    • SOBIESZEK, A. & JERTSCHIN, P. (1986). Urea-glycerol-acrylamide gel electrophoresis of acidic low molecular weight muscle proteins: rapid determination of myosin light chain phosphorylation in myosin, actomyosin and whole muscle samples. Electrophoresis 7, 417-425.
    • (1986) Electrophoresis , vol.7 , pp. 417-425
    • Sobieszek, A.1    Jertschin, P.2
  • 58
    • 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
  • 59
    • 0027310995 scopus 로고
    • Effects of calyculin A on tension and myosin phosphorylation in skinned smooth muscle of the rabbit mesenteric artery
    • SUZUKI, A. & ITOH, T. (1993). Effects of calyculin A on tension and myosin phosphorylation in skinned smooth muscle of the rabbit mesenteric artery. British Journal of Pharmacology 109, 703-712.
    • (1993) British Journal of Pharmacology , vol.109 , pp. 703-712
    • Suzuki, A.1    Itoh, T.2
  • 60
    • 0028914008 scopus 로고
    • Autophosphorylation of smooth muscle myosin light chain kinase at its regulatory domain
    • TOKUI, T., ANDO, S. & IKEBE, M. (1995). Autophosphorylation of smooth muscle myosin light chain kinase at its regulatory domain. Biochemistry 34, 5173-5179.
    • (1995) Biochemistry , vol.34 , pp. 5173-5179
    • Tokui, T.1    Ando, S.2    Ikebe, M.3
  • 62
    • 0024576739 scopus 로고
    • Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay
    • UMEMOTO, S., BENGUR, A. R. & SELLERS, J. R. (1989). Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay. Journal of Biological Chemistry 264, 1431-1436.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 1431-1436
    • Umemoto, S.1    Bengur, A.R.2    Sellers, J.R.3
  • 65
    • 0025348420 scopus 로고
    • Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation
    • WINDER, S. J. & WALSH, M. P. (1990). Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation. Journal of Biological Chemistry 265, 10148-10155.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 10148-10155
    • Winder, S.J.1    Walsh, M.P.2


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