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Volumn 20, Issue 4, 1999, Pages 347-349

Unphosphorylated crossbridges and latch: Smooth muscle regulation revisited

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN LIGHT CHAIN;

EID: 0033132732     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1005557724418     Document Type: Article
Times cited : (8)

References (21)
  • 2
    • 0016795902 scopus 로고
    • Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity
    • Adelstein RS and Conti MA (1975) Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity. Nature 256: 597-598.
    • (1975) Nature , vol.256 , pp. 597-598
    • Adelstein, R.S.1    Conti, M.A.2
  • 3
    • 0025142344 scopus 로고
    • Cooperativity of actin-activated ATPase of gizzard heavy meromyosin in the presence of gizzard tropomyosin
    • Chacko S and Eisenberg E (1990) Cooperativity of actin-activated ATPase of gizzard heavy meromyosin in the presence of gizzard tropomyosin. J Biol Chem 265: 2105-2110.
    • (1990) J Biol Chem , vol.265 , pp. 2105-2110
    • Chacko, S.1    Eisenberg, E.2
  • 4
    • 0031041817 scopus 로고    scopus 로고
    • Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap
    • Guilford WH, Dupuis DE, Kennedy G, Wu JR, Patlak JB and Warshaw DM (1997) Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap. Biophys J 12: 1006-1021.
    • (1997) Biophys J , vol.12 , pp. 1006-1021
    • Guilford, W.H.1    Dupuis, D.E.2    Kennedy, G.3    Wu, J.R.4    Patlak, J.B.5    Warshaw, D.M.6
  • 5
    • 0032836236 scopus 로고    scopus 로고
    • Thin-filament linked regulation of smooth muscle myosin
    • Haeberle JR (1999) Thin-filament linked regulation of smooth muscle myosin. J Muscle Res Cell Motil 20: 363-370.
    • (1999) J Muscle Res Cell Motil , vol.20 , pp. 363-370
    • Haeberle, J.R.1
  • 6
    • 0028335358 scopus 로고
    • Calponin decreases the rate of cross-bridge cycling and increases maximum force production by smooth muscle myosin in an in vitro motility assay
    • Haeberle JR (1994) Calponin decreases the rate of cross-bridge cycling and increases maximum force production by smooth muscle myosin in an in vitro motility assay. J Biol Chem 269: 12424-12431.
    • (1994) J Biol Chem , vol.269 , pp. 12424-12431
    • Haeberle, J.R.1
  • 7
    • 0028952032 scopus 로고
    • Are actin filaments moving under unloaded conditions in the in vitro motility assay
    • Haeberle JR and Hemric ME (1995) Are actin filaments moving under unloaded conditions in the in vitro motility assay. Biophys J 68 (Suppl.) 306S-311S.
    • (1995) Biophys J , vol.68 , Issue.SUPPL.
    • Haeberle, J.R.1    Hemric, M.E.2
  • 8
    • 0026440112 scopus 로고
    • The effects of smooth muscle caldesmon on actin filament motility
    • Haeberle JR, Trybus KM, Hemric ME and Warshaw DM (1992) The effects of smooth muscle caldesmon on actin filament motility. J Biol Chem 267: 23001-23006.
    • (1992) J Biol Chem , vol.267 , pp. 23001-23006
    • Haeberle, J.R.1    Trybus, K.M.2    Hemric, M.E.3    Warshaw, D.M.4
  • 10
    • 0022636016 scopus 로고
    • Myoplasmic calcium, myosin phosphorylation, and regulation of the crossbridge cycle in swine arterial smooth muscle
    • Rembold CM and Murphy RA (1986) Myoplasmic calcium, myosin phosphorylation, and regulation of the crossbridge cycle in swine arterial smooth muscle. Circulation Res 58: 803-815.
    • (1986) Circulation Res , vol.58 , pp. 803-815
    • Rembold, C.M.1    Murphy, R.A.2
  • 11
    • 0029561337 scopus 로고
    • Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin
    • Rovner AS, Freyzon Y and Trybus KM (1995) Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin. J Biol Chem 270: 30260-30263.
    • (1995) J Biol Chem , vol.270 , pp. 30260-30263
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 12
    • 0022310829 scopus 로고
    • The mechanism of regulation of smooth muscle myosin by phosphorylation
    • Sellers JR and Adelstein RS (1985) The mechanism of regulation of smooth muscle myosin by phosphorylation. Curr Top Cell Regul 27: 51-62.
    • (1985) Curr Top Cell Regul , vol.27 , pp. 51-62
    • Sellers, J.R.1    Adelstein, R.S.2
  • 13
    • 77956930245 scopus 로고
    • Regulation of contractile activity
    • Boyer PD (ed.), Academic Press, Orlando. FL
    • Sellers JR and Adelstein RS (1987) Regulation of contractile activity. In: Boyer PD (ed.), The Enzymes (pp. 381-418). Academic Press, Orlando. FL.
    • (1987) The Enzymes , pp. 381-418
    • Sellers, J.R.1    Adelstein, R.S.2
  • 14
    • 0020356742 scopus 로고
    • The binding of smooth muscle heavy meromyosin to actin in the presence of ATP. Effect of phosphorylation
    • Sellers JR, Eisenberg E and Adelstein RS (1982) The binding of smooth muscle heavy meromyosin to actin in the presence of ATP. Effect of phosphorylation. J Biol Chem 257: 13880-13883.
    • (1982) J Biol Chem , vol.257 , pp. 13880-13883
    • Sellers, J.R.1    Eisenberg, E.2    Adelstein, R.S.3
  • 15
    • 0023832001 scopus 로고
    • Cross-bridge kinetics, cooperativity, and negatively strained cross-bridges in vertebrate smooth muscle. A laser-flash photolysis study
    • Somlyo AV, Goldman YE, Fujimori T, Bond M, Trentham DR and Somlyo AP (1988) Cross-bridge kinetics, cooperativity, and negatively strained cross-bridges 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.P.6
  • 16
    • 0024850616 scopus 로고
    • Filamentous smooth muscle myosin is regulated by phosphorylation
    • Trybus KM (1989) Filamentous smooth muscle myosin is regulated by phosphorylation. J Cell Biol 109: 2887-2894.
    • (1989) J Cell Biol , vol.109 , pp. 2887-2894
    • Trybus, K.M.1
  • 17
    • 0028085210 scopus 로고
    • Enhanced force generation by smooth muscle myosin in vitro
    • Vanburen P, Work SS and Warshaw DM (1994) Enhanced force generation by smooth muscle myosin in vitro. Proc Natl Acad Sci USA 91: 202-205.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 202-205
    • Vanburen, P.1    Work, S.S.2    Warshaw, D.M.3
  • 18
    • 0023037073 scopus 로고
    • Regulation of the actin-activated ATPase of aorta smooth muscle myosin
    • Wagner PD and Vu ND (1986) Regulation of the actin-activated ATPase of aorta smooth muscle myosin. J Biol Chem 261: 7778-7783.
    • (1986) J Biol Chem , vol.261 , pp. 7778-7783
    • Wagner, P.D.1    Vu, N.D.2
  • 19
    • 0023656764 scopus 로고
    • Actin-activation of unphosphorylated gizzard myosin
    • Wagner PD and Vu ND (1987) Actin-activation of unphosphorylated gizzard myosin. J Biol Chem 262: 15556-15562.
    • (1987) J Biol Chem , vol.262 , pp. 15556-15562
    • Wagner, P.D.1    Vu, N.D.2
  • 21
    • 0025335344 scopus 로고
    • Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro
    • Warshaw DM, Desrosiers JM, Work SS and Trybus KM (1990) Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro. J Cell Biol 111: 453-463.
    • (1990) J Cell Biol , vol.111 , pp. 453-463
    • Warshaw, D.M.1    Desrosiers, J.M.2    Work, S.S.3    Trybus, K.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.