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Volumn 296, Issue 5, 2009, Pages

Regulatory mechanism of smooth muscle contraction studied with gelsolin-treated strips of taenia caeci in guinea pig

Author keywords

Confocal fluorescence microscopy; Force development; Phalloidin; Phosphorylation of myosin regulatory light chain; Reduction in muscle cross sectional area; Thin filament linked regulation

Indexed keywords

ACTIN; CALDESMON; GELSOLIN; MYOSIN; MYOSIN LIGHT CHAIN; TROPOMYOSIN;

EID: 66149099239     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00565.2008     Document Type: Article
Times cited : (3)

References (62)
  • 1
    • 38049169183 scopus 로고    scopus 로고
    • 2+ regulation of smooth muscle thin filaments: Evidence for a cooperative switching mechanism
    • 2+ regulation of smooth muscle thin filaments: evidence for a cooperative switching mechanism. J Biol Chem 283: 47-56, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 47-56
    • Ansari, S.1    Alahyan, M.2    Marston, S.B.3    El-Mezgueldi, M.4
  • 2
    • 0028125196 scopus 로고
    • Lattice spacing changes accompanying isometric tension development in intact single muscle fibers
    • Bagni MA, Cecchi G, Griffiths PJ, Maeda Y, Rapp G, Ashley CC. Lattice spacing changes accompanying isometric tension development in intact single muscle fibers. Biophys J 67: 1965-1975, 1994. (Pubitemid 24342068)
    • (1994) Biophysical Journal , vol.67 , Issue.5 , pp. 1965-1975
    • Bagni, M.A.1    Cecchi, G.2    Griffiths, P.J.3    Maeda, Y.4    Rapp, G.5    Ashley, C.C.6
  • 3
    • 0035930613 scopus 로고    scopus 로고
    • Exchange of the Actin-bound Nucleotide in Intact Arterial Smooth Muscle
    • Bárány M, Barron JT, Gu L, Bárány K. Exchange of the actin-bound nucleotide in intact arterial smooth muscle. J Biol Chem 276: 48398-48403, 2001. (Pubitemid 37370751)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.51 , pp. 48398-48403
    • Barany, M.1    Barron, J.T.2    Gu, L.3    Barany, K.4
  • 4
    • 0026560945 scopus 로고
    • Relaxant effect of phalloidin on Triton-skinned microvascular and other smooth muscle preparations
    • Boels PJ, Pfitzer G. Relaxant effect of phalloidin on Triton-skinned microvascular and other smooth muscle preparations. J Muscle Res Cell Motil 13: 71-80, 1992.
    • (1992) J Muscle Res Cell Motil , vol.13 , pp. 71-80
    • Boels, P.J.1    Pfitzer, G.2
  • 5
    • 0021686984 scopus 로고
    • Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties
    • Bretscher A. Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties. J Biol Chem 259: 12873-12880, 1992.
    • (1992) J Biol Chem , vol.259 , pp. 12873-12880
    • Bretscher, A.1
  • 6
    • 0036135875 scopus 로고    scopus 로고
    • Pressure-induced actin polymerization in vascular smooth muscle as a mechanism underlying myogenic behavior
    • DOI 10.1096/cj.01-0104hyp
    • Cipolla MJ, Gokina NI, Osol G. Pressure-induced actin polymerization in vascular smooth muscle as a mechanism underlying myogenic behavior. FASEB J 16: 72-76, 2002. (Pubitemid 34027952)
    • (2002) FASEB Journal , vol.16 , Issue.1 , pp. 72-76
    • Cipolla, M.J.1    Gokina, N.I.2    Osol, G.3
  • 7
    • 0019433353 scopus 로고
    • Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle
    • Dillon PF, Aksoy MO, Driska SP, Murphy RA. Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle. Science 211: 495-497, 1981.
    • (1981) Science , vol.211 , pp. 495-497
    • Dillon, P.F.1    Aksoy, M.O.2    Driska, S.P.3    Murphy, R.A.4
  • 8
    • 0025609219 scopus 로고
    • The cytoskeletal and contractile apparatus of smooth muscle: Contraction bands and segmentation of the contractile elements
    • Draeger A, Amos WB, Ikebe M, Small JV. The cytoskeletal and contractile apparatus of smooth muscle: contraction bands and segmentation of the contractile elements. J Cell Biol 111: 2463-2473, 1990. (Pubitemid 120014530)
    • (1990) Journal of Cell Biology , vol.111 , Issue.6 , pp. 2463-2473
    • Draeger, A.1    Amos, W.B.2    Ikebe, M.3    Small, J.V.4
  • 9
    • 0029909623 scopus 로고    scopus 로고
    • Structural and functional reconstitution of thin filaments in the contractile apparatus of cardiac muscle
    • Fujita H, Yasuda K, Niitsu S, Funatsu T, Ishiwata S. Structural and functional reconstitution of thin filaments in the contractile apparatus of cardiac muscle. Biophys J 71: 2307-2318, 1996. (Pubitemid 26367697)
    • (1996) Biophysical Journal , vol.71 , Issue.5 , pp. 2307-2318
    • Fujita, H.1    Yasuda, K.2    Niitsu, S.3    Funatsu, T.4    Ishiwata, S.5
  • 10
    • 0036156643 scopus 로고    scopus 로고
    • Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins
    • Fujita H, Sasaki D, Ishiwata S, Kawai M. Elementary steps of the cross-bridge cycle in bovine myocardium with and without regulatory proteins. Biophys J 82: 915-928, 2002. (Pubitemid 34111232)
    • (2002) Biophysical Journal , vol.82 , Issue.2 , pp. 915-928
    • Fujita, H.1    Sasaki, D.2    Ishiwata, S.3    Kawai, M.4
  • 11
    • 0036713779 scopus 로고    scopus 로고
    • Microscopic analysis of polymerization dynamics with individual actin filaments
    • Fujiwara I, Takahashi S, Tadakuma H, Funatsu T, Ishiwata S. Microscopic analysis of polymerization dynamics with individual actin filaments. Nat Cell Biol 4: 666-673, 2002.
    • (2002) Nat Cell Biol , vol.4 , pp. 666-673
    • Fujiwara, I.1    Takahashi, S.2    Tadakuma, H.3    Funatsu, T.4    Ishiwata, S.5
  • 12
    • 0025062549 scopus 로고
    • Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin
    • DOI 10.1083/jcb.110.1.53
    • Funatsu T, Higuchi H, Ishiwata S. Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin. J Cell Biol 110: 53-62, 1990. (Pubitemid 20035877)
    • (1990) Journal of Cell Biology , vol.110 , Issue.1 , pp. 53-62
    • Funatsu, T.1    Higuchi, H.2    Ishiwata, S.3
  • 14
    • 0025075247 scopus 로고
    • The action of brevin, and F-actin severing protein, on the mechanical properties and ATPase activity of skinned smooth muscle
    • DOI 10.1007/BF01766667
    • Gailly P, Lejeune T, Capony JP, Gillis JM. The action of brevin, an F-actin severing protein, on the mechanical properties and ATPase activity of skinned smooth muscle. J Muscle Res Cell Motil 11: 293-301, 1990. (Pubitemid 20283769)
    • (1990) Journal of Muscle Research and Cell Motility , vol.11 , Issue.4 , pp. 293-301
    • Gailly, Ph.1    Lejeune, Th.2    Capony, J.P.3    Gillis, J.M.4
  • 15
    • 0027424574 scopus 로고
    • 2+-activated brevin on the mechanical properties of skinned smooth muscle
    • 2+-activated brevin on the mechanical properties of skinned smooth muscle. Adv Exp Med Biol 332: 205-212, 1993.
    • (1993) Adv Exp Med Biol , vol.332 , pp. 205-212
    • Gailly, P.1    Gillis, J.M.2    Capony, J.P.3
  • 16
    • 14244263335 scopus 로고    scopus 로고
    • Effect of caldesmon on the position and myosin-induced movement of smooth muscle tropomyosin bound to actin
    • DOI 10.1074/jbc.M410375200
    • Graceffa P, Mazurkie A. Effect of caldesmon on the position and myosin-induced movement of smooth muscle tropomyosin bound to actin. J Biol Chem 280: 4135-4143, 2005. (Pubitemid 40288578)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4135-4143
    • Graceffa, P.1    Mazurkie, A.2
  • 18
    • 0028258477 scopus 로고
    • Regulation of isotonic shortening velocity by second messengers in tracheal smooth muscle
    • Gunst SJ, al-Hassani HM, Adam LP. Regulation of isotonic shortening velocity by second messengers in tracheal smooth muscle. Am J Physiol Cell Physiol 266: C684-C691, 1994.
    • (1994) Am J Physiol Cell Physiol , vol.266
    • Gunst, S.J.1    Al-Hassani, H.M.2    Adam, L.P.3
  • 20
    • 0032836236 scopus 로고    scopus 로고
    • Thin-filament linked regulation of smooth muscle myosin
    • Haeberle JR. Thin-filament linked regulation of smooth muscle myosin. J Muscle Res Cell Motil 20: 363-370, 1999.
    • (1999) J Muscle Res Cell Motil , vol.20 , pp. 363-370
    • Haeberle, J.R.1
  • 21
    • 0000975551 scopus 로고
    • Structural basis of the cross-striations in muscle
    • Hanson J, Huxley HE. Structural basis of the cross-striations in muscle. Nature 172: 530-532, 1953.
    • (1953) Nature , vol.172 , pp. 530-532
    • Hanson, J.1    Huxley, H.E.2
  • 22
    • 67649710091 scopus 로고    scopus 로고
    • Differential effects of an expected actin-tropomyosin binding region of heat shock protein 20 on the relaxation in skinned carotid artery and taenia cecum from guinea pig
    • In press
    • Hashimoto R, Yumoto M, Watanabe M, Konishi M, Haraoka J, Miki T. Differential effects of an expected actin-tropomyosin binding region of heat shock protein 20 on the relaxation in skinned carotid artery and taenia cecum from guinea pig. J Smooth Musc Res. In press.
    • J Smooth Musc Res
    • Hashimoto, R.1    Yumoto, M.2    Watanabe, M.3    Konishi, M.4    Haraoka, J.5    Miki, T.6
  • 24
    • 21044439541 scopus 로고    scopus 로고
    • 'Sarcomeres' of smooth muscle: Functional characteristics and ultrastructural evidence
    • DOI 10.1242/jcs.02368
    • Herrera AM, McParland BE, Bienkowska A, Tait R, Pare PD, Seow CY. "Sarcomeres" of smooth muscle: functional characteristics and ultrastructural evidence. J Cell Sci 118: 2381-2392, 2005. (Pubitemid 40873078)
    • (2005) Journal of Cell Science , vol.118 , Issue.11 , pp. 2381-2392
    • Herrera, A.M.1    McParland, B.E.2    Bienkowska, A.3    Tait, R.4    Pare, P.D.5    Seow, C.Y.6
  • 25
    • 0023851762 scopus 로고
    • Mechanism of contracture on cooling of caffeine-treated frog skeletal muscle fibres
    • Horiuti K. Mechanism of contracture on cooling of caffeine-treated frog skeletal muscle fibres. J Physiol 398: 131-148, 1988. (Pubitemid 18070002)
    • (1988) Journal of Physiology , vol.398 , pp. 131-148
    • Horiuti, K.1
  • 27
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction; interference microscopy of living muscle fibres
    • Huxley AF, Niedergerke R. Structural changes in muscle during contraction; interference microscopy of living muscle fibres. Nature 173: 971-973, 1954.
    • (1954) Nature , vol.173 , pp. 971-973
    • Huxley, A.F.1    Niedergerke, R.2
  • 28
    • 0033198486 scopus 로고    scopus 로고
    • F-actin stabilization increases tension cost during contraction of permeabilized airway smooth muscle in dogs
    • Jones KA, Perkins WJ, Lorenz RR, Prakash YS, Sieck GC, Warner DO. F-actin stabilization increases tension cost during contraction of permeabilized airway smooth muscle in dogs. J Physiol 519: 527-538, 1999.
    • (1999) J Physiol , vol.519 , pp. 527-538
    • Jones, K.A.1    Perkins, W.J.2    Lorenz, R.R.3    Prakash, Y.S.4    Sieck, G.C.5    Warner, D.O.6
  • 29
    • 33748291631 scopus 로고    scopus 로고
    • Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation
    • DOI 10.1007/s10974-006-9075-4
    • Kawai M, Ishiwata S. Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation. J Muscle Res Cell Motil 27: 455-468, 2006. (Pubitemid 44325624)
    • (2006) Journal of Muscle Research and Cell Motility , vol.27 , Issue.5-7 , pp. 455-468
    • Kawai, M.1    Ishiwata, S.2
  • 30
    • 0017229312 scopus 로고
    • Uni-directional growth of F-actin
    • Kondo H, Ishiwata S. Uni-directional growth of F-actin. J Biochem 79: 159-171, 1976.
    • (1976) J Biochem , vol.79 , pp. 159-171
    • Kondo, H.1    Ishiwata, S.2
  • 32
    • 2342418026 scopus 로고    scopus 로고
    • Contractile filament architecture and force transmission in swine airway smooth muscle
    • Kuo KH, Seow CY. Contractile filament architecture and force transmission in swine airway smooth muscle. J Cell Sci 117: 1503-1511, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 1503-1511
    • Kuo, K.H.1    Seow, C.Y.2
  • 34
    • 0034602971 scopus 로고    scopus 로고
    • Regulation of vascular smooth muscle tone by N-terminal region of caldesmon. Possible role of tethering actin to myosin
    • DOI 10.1074/jbc.275.5.3213
    • Lee YH, Gallant C, Guo H, Li Y, Wang CLA, Morgan KG. Regulation of vascular smooth muscle tone by N-terminal region of caldesmon: possible role of tethering actin to myosin. J Biol Chem 275: 3213-3220, 2000. (Pubitemid 30083021)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.5 , pp. 3213-3220
    • Lee, Y.-H.1    Gallant, C.2    Guo, H.3    Li, Y.4    Wang, C.-L.A.5    Morgan, K.G.6
  • 35
    • 0025851753 scopus 로고
    • Calponin and the composition of smooth muscle thin filaments
    • Lehman W. Calponin and the composition of smooth muscle thin filaments. J Muscle Res Cell Motil 12: 221-224, 1991.
    • (1991) J Muscle Res Cell Motil , vol.12 , pp. 221-224
    • Lehman, W.1
  • 36
    • 0026076130 scopus 로고
    • Functional interrelationship between calponin and caldesmon
    • Makuch R, Birukov K, Shirinsky V, Dabrowska R. Functional interrelationship between calponin and caldesmon. Biochem J 280: 33-38, 1991.
    • (1991) Biochem J , vol.280 , pp. 33-38
    • Makuch, R.1    Birukov, K.2    Shirinsky, V.3    Dabrowska, R.4
  • 37
    • 0029957346 scopus 로고    scopus 로고
    • The effects of caldesmon extraction on mechanical properties of shinned smooth muscle fihre preparations
    • DOI 10.1007/s004240050130
    • Malmqvist U, Arner A, Makuch R, Dabrowska R. The effects of caldesmon extraction on mechanical properties of skinned smooth muscle fibre preparations. Pflügers Arch 432: 241-247, 1996. (Pubitemid 26226107)
    • (1996) Pflugers Archiv European Journal of Physiology , vol.432 , Issue.2 , pp. 241-247
    • Malmqvist, U.1    Arner, A.2    Makuch, R.3    Dabrowska, R.4
  • 38
    • 0021646354 scopus 로고
    • 2+-regulated thin filaments and F-actin from sheep aorta smooth muscle
    • 2+-regulated thin filaments and F-actin from sheep aorta smooth muscle. J Muscle Res Cell Motil 5: 559-575, 1984.
    • (1984) J Muscle Res Cell Motil , vol.5 , pp. 559-575
    • Marston, S.B.1    Smith, C.W.J.2
  • 39
    • 0021358821 scopus 로고
    • Changes in the lateral filament spacing of skinned muscle fibres when cross-bridges attach
    • Matsubara I, Goldman YE, Simmons RM. Changes in the lateral filament spacing of skinned muscle fibres when cross-bridges attach. J Mol Biol 173: 15-33, 1984. (Pubitemid 14199547)
    • (1984) Journal of Molecular Biology , vol.173 , Issue.1 , pp. 15-33
    • Matsubara, I.1    Goldman, Y.E.2    Simmons, R.M.3
  • 40
    • 0033199069 scopus 로고    scopus 로고
    • Actin polymerization stimulated by contractile activation regulates force development in canine tracheal smooth muscle
    • DOI 10.1111/j.1469-7793.1999.0829n.x
    • Mehta D, Gunst SJ. Actin polymerization stimulated by contractile activation regulates force development in canine tracheal smooth muscle. J Physiol 519: 829-840, 1999. (Pubitemid 29462446)
    • (1999) Journal of Physiology , vol.519 , Issue.3 , pp. 829-840
    • Mehta, D.1    Gunst, S.J.2
  • 41
    • 0034921574 scopus 로고    scopus 로고
    • Signal transduction in smooth muscle. Cross-bridge regulation by thin filament-associated protein
    • Morgan KG, Gangopadhyay SS. Signal transduction in smooth muscle. Cross-bridge regulation by thin filament-associated protein. J Appl Physiol 91: 953-962, 2001.
    • (2001) J Appl Physiol , vol.91 , pp. 953-962
    • Morgan, K.G.1    Gangopadhyay, S.S.2
  • 42
    • 0028196621 scopus 로고
    • Actin isoform compartments in chicken gizzard smooth muscle cells
    • North AJ, Gimona M, Lando Z, Small JV. Actin isoform compartments in chicken gizzard smooth muscle cells. J Cell Sci 107: 445-455, 1994. (Pubitemid 24091852)
    • (1994) Journal of Cell Science , vol.107 , Issue.3 , pp. 445-455
    • North, A.J.1    Gimona, M.2    Lando, Z.3    Small, J.V.4
  • 43
    • 0034976775 scopus 로고    scopus 로고
    • Invited review: Regulation of myosin phosphorylation in smooth muscle
    • Pfitzer G. Signal transduction in smooth muscle. Regulation of myosin phosphorylation in smooth muscle. J Appl Physiol 91: 597-603, 2001. (Pubitemid 32574761)
    • (2001) Journal of Applied Physiology , vol.91 , Issue.1 , pp. 497-503
    • Pfitzer, G.1
  • 45
    • 48949118319 scopus 로고    scopus 로고
    • Calponins: Adaptable modular regulators of the actin cytoskeleton
    • Rozenblum GT, Gimona M. Calponins: adaptable modular regulators of the actin cytoskeleton. Int J Biochem Cell Biol 40: 1990-1995, 2008.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1990-1995
    • Rozenblum, G.T.1    Gimona, M.2
  • 47
    • 27744598463 scopus 로고    scopus 로고
    • Myosin filament assembly in an ever-changing myofilament lattice of smooth muscle
    • Seow CY. Myosin filament assembly in an ever-changing myofilament lattice of smooth muscle. Am J Physiol Cell Physiol 289: C1363-C1368, 2005.
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Seow, C.Y.1
  • 48
    • 0037227358 scopus 로고    scopus 로고
    • Inhibitors of actin filament polymerisation attenuate force but not global intracellular calcium in isolated pressurised resistance arteries
    • DOI 10.1159/000068940
    • Shaw L, Ahmed S, Austin C, Taggart MJ. Inhibitors of actin filament polymerization attenuate force but not global intracellular calcium in isolated pressurized resistance arteries. J Vasc Res 40: 1-10, 2003. (Pubitemid 36351191)
    • (2003) Journal of Vascular Research , vol.40 , Issue.1 , pp. 1-10
    • Shaw, L.1    Ahmed, S.2    Austin, C.3    Taggart, M.J.4
  • 50
    • 0032446186 scopus 로고    scopus 로고
    • The cytoskeleton of the vertebrate smooth muscle cell
    • DOI 10.1046/j.1365-201X.1998.00441.x
    • Small JV, Gimona M. The cytoskeleton of the vertebrate smooth muscle cell. Acta Physiol Scand 164: 341-348, 1998. (Pubitemid 29015653)
    • (1998) Acta Physiologica Scandinavica , vol.164 , Issue.4 , pp. 341-348
    • Small, J.V.1    Gimona, M.2
  • 51
    • 0022400733 scopus 로고
    • Caldesmon-induced inhibition of ATPase activity of actomyosin and contraction of skinned fibres of chicken gizzard smooth muscle
    • DOI 10.1016/0014-5793(85)80032-6
    • Szpacenko A, Wagner J, Dabrowska R, Rüegg JC. Caldesmon-induced inhibition of ATPase activity of actomyosin and contraction of skinned fibres of chicken gizzard smooth muscle. FEBS Lett 192:9-12, 1985. (Pubitemid 16230630)
    • (1985) FEBS Letters , vol.192 , Issue.1 , pp. 9-12
    • Szpacenko, A.1    Wagner, J.2    Dabrowska, R.3    Ruegg, J.C.4
  • 52
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA, Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246: 4866-4871, 1971.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 53
    • 0036401563 scopus 로고    scopus 로고
    • Use of actin isoform-specific antibodies to probe the domain structure in three smooth muscles
    • Stromer MH, Mayes MS, Bellin RM. Use of actin isoform-specific antibodies to probe the domain structure in three smooth muscles. Histochem Cell Biol 118: 291-299, 2002.
    • (2002) Histochem Cell Biol , vol.118 , pp. 291-299
    • Stromer, M.H.1    Mayes, M.S.2    Bellin, R.M.3
  • 55
    • 0024239924 scopus 로고
    • A novel troponin T-like protein (calponin) in vascular smooth muscle: Interaction with tropomyosin paracrystals
    • Takahashi K, Abe M, Hiwada K, Kokubu T. A novel troponin T-like protein (calponin) in vascular smooth muscle: interaction with tropomyosin paracrystals. J Hypertens 6: S40-S43, 1988. (Pubitemid 19067264)
    • (1988) Journal of Hypertension , vol.6 , Issue.SUPPL. 4
    • Takahashi, K.1    Abe, M.2    Hiwada, K.3    Kokubu, T.4
  • 56
    • 0024850616 scopus 로고
    • Filamentous smooth muscle myosin is regulated by phosphorylation
    • Trybus KM. Filamentous smooth muscle myosin is regulated by phosphorylation. J Cell Biol 109, 2887-2894, 1989.
    • (1989) J Cell Biol , vol.109 , pp. 2887-2894
    • Trybus, K.M.1
  • 57
    • 0027934341 scopus 로고
    • Regulation of expressed truncated smooth muscle myosins. Role of the essential light chain and tail length
    • Trybus KM. Regulation of expressed truncated smooth muscle myosins. Role of the essential light chain and tail length. J Biol Chem 269: 20819-20822, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 20819-20822
    • Trybus, K.M.1
  • 58
    • 0035749892 scopus 로고    scopus 로고
    • Caldesmon and smooth-muscle regulation
    • Wang CLA. Caldesmon and smooth-muscle regulation. Cell Biochem Biophys 35: 275-288, 2001.
    • (2001) Cell Biochem Biophys , vol.35 , pp. 275-288
    • Wang, C.L.A.1
  • 59
    • 0027762277 scopus 로고
    • Effects of 2,3-butanedione monoxime on smooth-muscle contraction of guinea-pig portal vein
    • DOI 10.1007/BF00374873
    • Watanabe M. Effects of 2,3-butanedione monoxime on smooth-muscle contraction of guinea-pig portal vein. Pflügers Arch 425: 462-468, 1993. (Pubitemid 24017746)
    • (1993) Pflugers Archiv European Journal of Physiology , vol.425 , Issue.5-6 , pp. 462-468
    • Watanabe, M.1
  • 60
    • 0038352067 scopus 로고    scopus 로고
    • Troponin I inhibitory peptide suppresses the force generation in smooth muscle by directly interfering with cross-bridge formation
    • DOI 10.1016/S0006-291X(03)01170-7
    • Watanabe M, Yoshino Y, Morimoto S. Troponin I inhibitory peptide suppresses the force generation in smooth muscle by directly interfering with cross-bridge formation. Biochem Biophys Res Commun 307: 236-240, 2003. (Pubitemid 36818859)
    • (2003) Biochemical and Biophysical Research Communications , vol.307 , Issue.2 , pp. 236-240
    • Watanabe, M.1    Yoshino, Y.2    Morimoto, S.3
  • 61
    • 33646232946 scopus 로고    scopus 로고
    • Synthetic peptides of actin-tropomyosin binding region of troponin I and heat shock protein 20 modulate the relaxation process of skinned preparations of taenia caeci from guinea pig
    • Yoshino Y, Sakurai W, Morimoto S, Watanabe M. Synthetic peptides of actin-tropomyosin binding region of troponin I and heat shock protein 20 modulate the relaxation process of skinned preparations of taenia caeci from guinea pig. Jpn J Physiol 55: 373-378, 2005.
    • (2005) Jpn J Physiol , vol.55 , pp. 373-378
    • Yoshino, Y.1    Sakurai, W.2    Morimoto, S.3    Watanabe, M.4


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