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Volumn 103, Issue 3, 2012, Pages 501-510

Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; MYOSIN;

EID: 84864691712     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.06.031     Document Type: Article
Times cited : (96)

References (67)
  • 1
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • R.W. Lymn, and E.W. Taylor Mechanism of adenosine triphosphate hydrolysis by actomyosin Biochemistry 10 1971 4617 4624
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 2
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometre steps
    • DOI 10.1038/368113a0
    • J.T. Finer, R.M. Simmons, and J.A. Spudich Single myosin molecule mechanics: picoNewton forces and nanometer steps Nature 368 1994 113 119 (Pubitemid 24101520)
    • (1994) Nature , vol.368 , Issue.6467 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 4
    • 0028803118 scopus 로고
    • Movement and force produced by a single myosin head
    • J.E. Molloy, and J.E. Burns D.C. White Movement and force produced by a single myosin head Nature 378 1995 209 212
    • (1995) Nature , vol.378 , pp. 209-212
    • Molloy, J.E.1    Burns, J.E.2    White, D.C.3
  • 5
    • 0031041817 scopus 로고    scopus 로고
    • Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap
    • W.H. Guilford, and D.E. Dupuis D.M. Warshaw Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap Biophys. J. 72 1997 1006 1021 (Pubitemid 27113629)
    • (1997) Biophysical Journal , vol.72 , Issue.3 , pp. 1006-1021
    • Guilford, W.H.1    Dupuis, D.E.2    Kennedy, G.3    Wu, J.4    Patlak, J.B.5    Warshaw, D.M.6
  • 6
    • 33847769745 scopus 로고    scopus 로고
    • Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin
    • DOI 10.1529/biophysj.106.097618
    • N.M. Kad, and J.B. Patlak D.M. Warshaw Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin Biophys. J. 92 2007 1623 1631 (Pubitemid 46393473)
    • (2007) Biophysical Journal , vol.92 , Issue.5 , pp. 1623-1631
    • Kad, N.M.1    Patlak, J.B.2    Fagnant, P.M.3    Trybus, K.M.4    Warshaw, D.M.5
  • 7
    • 0242609969 scopus 로고    scopus 로고
    • Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers
    • DOI 10.1038/ncb1060
    • C. Veigel, and J.E. Molloy J. Kendrick-Jones Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers Nat. Cell Biol. 5 2003 980 986 (Pubitemid 37406911)
    • (2003) Nature Cell Biology , vol.5 , Issue.11 , pp. 980-986
    • Veigel, C.1    Molloy, J.E.2    Schmitz, S.3    Kendrick-Jones, J.4
  • 9
    • 0024991350 scopus 로고
    • Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • T.Q.P. Uyeda, S.J. Kron, and J.A. Spudich Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin J. Mol. Biol. 214 1990 699 710
    • (1990) J. Mol. Biol. , vol.214 , pp. 699-710
    • Uyeda, T.Q.P.1    Kron, S.J.2    Spudich, J.A.3
  • 10
    • 0036218298 scopus 로고    scopus 로고
    • The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules
    • J.E. Baker, and C. Brosseau D.M. Warshaw The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules Biophys. J. 82 2002 2134 2147 (Pubitemid 34280826)
    • (2002) Biophysical Journal , vol.82 , Issue.4 , pp. 2134-2147
    • Baker, J.E.1    Brosseau, C.2    Joel, P.B.3    Warshaw, D.M.4
  • 11
    • 0041707669 scopus 로고    scopus 로고
    • The unique properties of tonic smooth muscle emerge from intrinsic as well as intermolecular behaviors of myosin molecules
    • DOI 10.1074/jbc.M303583200
    • J.E. Baker, and C. Brosseau D.M. Warshaw The unique properties of tonic smooth muscle emerge from intrinsic as well as intermolecular behaviors of Myosin molecules J. Biol. Chem. 278 2003 28533 28539 (Pubitemid 36935757)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28533-28539
    • Baker, J.E.1    Brosseau, C.2    Fagnant, P.3    Warshaw, D.M.4
  • 12
    • 68849121787 scopus 로고    scopus 로고
    • The energetics of allosteric regulation of ADP release from myosin heads
    • D.R. Jackson Jr., and J.E. Baker The energetics of allosteric regulation of ADP release from myosin heads Phys. Chem. Chem. Phys. 11 2009 4808 4814
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 4808-4814
    • Jackson, Jr.D.R.1    Baker, J.E.2
  • 13
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • A.F. Huxley Muscle structure and theories of contraction Prog. Biophys. Biophys. Chem. 7 1957 255 318
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 14
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • A.F. Huxley, and R.M. Simmons Proposed mechanism of force generation in striated muscle Nature 233 1971 533 538
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 15
    • 0016180488 scopus 로고
    • Theoretical formalism for the sliding filament model of contraction of striated muscle. Part i
    • T.L. Hill Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I Prog. Biophys. Mol. Biol. 28 1974 267 340
    • (1974) Prog. Biophys. Mol. Biol. , vol.28 , pp. 267-340
    • Hill, T.L.1
  • 16
    • 0018877621 scopus 로고
    • Cross-bridge model of muscle contraction. Quantitative analysis
    • E. Eisenberg, T.L. Hill, and Y.-D. Chen Cross-bridge model of muscle contraction. Quantitative analysis Biophys. J. 29 1980 195 227 (Pubitemid 10161281)
    • (1980) Biophysical Journal , vol.29 , Issue.2 , pp. 195-227
    • Eisenberg, E.1    Hill, T.L.2    Chen, Y.3
  • 17
    • 0024307990 scopus 로고
    • A model of crossbridge action: The effects of ATP, ADP and P(i)
    • E. Pate, and R. Cooke A model of crossbridge action: the effects of ATP, ADP and Pi J. Muscle Res. Cell Motil. 10 1989 181 196 (Pubitemid 19177278)
    • (1989) Journal of Muscle Research and Cell Motility , vol.10 , Issue.3 , pp. 181-196
    • Pate, E.1    Cooke, R.2
  • 18
    • 0028907268 scopus 로고
    • A cross-bridge model that is able to explain mechanical and energetic properties of shortening muscle
    • G. Piazzesi, and V. Lombardi A cross-bridge model that is able to explain mechanical and energetic properties of shortening muscle Biophys. J. 68 1995 1966 1979
    • (1995) Biophys. J. , vol.68 , pp. 1966-1979
    • Piazzesi, G.1    Lombardi, V.2
  • 19
    • 69249172101 scopus 로고    scopus 로고
    • Drug effect unveils inter-head cooperativity and strain-dependent ADP release in fast skeletal actomyosin
    • N. Albet-Torres, and M.J. Bloemink A. Månsson Drug effect unveils inter-head cooperativity and strain-dependent ADP release in fast skeletal actomyosin J. Biol. Chem. 284 2009 22926 22937
    • (2009) J. Biol. Chem. , vol.284 , pp. 22926-22937
    • Albet-Torres, N.1    Bloemink, M.J.2    Månsson, A.3
  • 20
    • 77950660976 scopus 로고    scopus 로고
    • Actomyosin-ADP states, interhead cooperativity, and the force-velocity relation of skeletal muscle
    • A. Månsson Actomyosin-ADP states, interhead cooperativity, and the force-velocity relation of skeletal muscle Biophys. J. 98 2010 1237 1246
    • (2010) Biophys. J. , vol.98 , pp. 1237-1246
    • Månsson, A.1
  • 21
    • 0029113048 scopus 로고
    • Strain-dependent cross-bridge cycle for muscle
    • D.A. Smith, and M.A. Geeves Strain-dependent cross-bridge cycle for muscle Biophys. J. 69 1995 524 537
    • (1995) Biophys. J. , vol.69 , pp. 524-537
    • Smith, D.A.1    Geeves, M.A.2
  • 23
    • 22244450654 scopus 로고    scopus 로고
    • Dynamics of myosin-driven skeletal muscle contraction: I. Steady-state force generation
    • DOI 10.1529/biophysj.104.056846
    • G. Lan, and S.X. Sun Dynamics of myosin-driven skeletal muscle contraction: I. Steady-state force generation Biophys. J. 88 2005 4107 4117 (Pubitemid 40991122)
    • (2005) Biophysical Journal , vol.88 , Issue.6 , pp. 4107-4117
    • Lan, G.1    Sun, S.X.2
  • 24
    • 67650720444 scopus 로고    scopus 로고
    • A multisegmental cross-bridge kinetics model of the myofibril
    • U. Stoecker, and I.A. Telley J. Denoth A multisegmental cross-bridge kinetics model of the myofibril J. Theor. Biol. 259 2009 714 726
    • (2009) J. Theor. Biol. , vol.259 , pp. 714-726
    • Stoecker, U.1    Telley, I.A.2    Denoth, J.3
  • 25
    • 73449088381 scopus 로고    scopus 로고
    • Interactions between connected half-sarcomeres produce emergent mechanical behavior in a mathematical model of muscle
    • K.S. Campbell Interactions between connected half-sarcomeres produce emergent mechanical behavior in a mathematical model of muscle PLOS Comput. Biol. 5 2009 e1000560
    • (2009) PLOS Comput. Biol. , vol.5 , pp. 1000560
    • Campbell, K.S.1
  • 26
    • 68849120091 scopus 로고    scopus 로고
    • Hysteresis in cross-bridge models of muscle
    • S. Walcott, and S.X. Sun Hysteresis in cross-bridge models of muscle Phys. Chem. Chem. Phys. 11 2009 4871 4881
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 4871-4881
    • Walcott, S.1    Sun, S.X.2
  • 27
    • 34547597323 scopus 로고    scopus 로고
    • Sarcomere lattice geometry influences cooperative myosin binding in muscle
    • B.C.W. Tanner, T.L. Daniel, and M. Regnier Sarcomere lattice geometry influences cooperative myosin binding in muscle PLOS Comput. Biol. 3 2007 e115
    • (2007) PLOS Comput. Biol. , vol.3 , pp. 115
    • Tanner, B.C.W.1    Daniel, T.L.2    Regnier, M.3
  • 28
    • 79960333325 scopus 로고    scopus 로고
    • +-dependent regulation of the rate of myosin binding to actin: Solution data and the tropomyosin chain model
    • +-dependent regulation of the rate of myosin binding to actin: solution data and the tropomyosin chain model Biophys. J. 100 2011 2679 2687
    • (2011) Biophys. J. , vol.100 , pp. 2679-2687
    • Geeves, M.1    Griffiths, H.2    Smith, D.3
  • 29
    • 77953731159 scopus 로고    scopus 로고
    • Regulation of muscle force in the absence of actin-myosin-based cross-bridge interaction
    • T.R. Leonard, and W. Herzog Regulation of muscle force in the absence of actin-myosin-based cross-bridge interaction Am. J. Physiol. Cell Physiol. 299 2010 C14 C20
    • (2010) Am. J. Physiol. Cell Physiol. , vol.299
    • Leonard, T.R.1    Herzog, W.2
  • 30
    • 27744553633 scopus 로고    scopus 로고
    • Slip sliding away: Load-dependence of velocity generated by skeletal muscle myosin molecules in the laser trap
    • E.P. Debold, J.B. Patlak, and D.M. Warshaw Slip sliding away: load-dependence of velocity generated by skeletal muscle myosin molecules in the laser trap Biophys. J. 89 2005 L34 L36
    • (2005) Biophys. J. , vol.89
    • Debold, E.P.1    Patlak, J.B.2    Warshaw, D.M.3
  • 31
    • 0000682154 scopus 로고
    • The heat of shortening and the dynamic constants of muscle
    • A.V. Hill The heat of shortening and the dynamic constants of muscle Proc. R. Soc. Lond. B Biol. Sci. 126 1938 136 195
    • (1938) Proc. R. Soc. Lond. B Biol. Sci. , vol.126 , pp. 136-195
    • Hill, A.V.1
  • 33
    • 78349267968 scopus 로고    scopus 로고
    • Contractile performance of striated muscle
    • K.A.P. Edman Contractile performance of striated muscle Adv. Exp. Med. Biol. 682 2010 7 40
    • (2010) Adv. Exp. Med. Biol. , vol.682 , pp. 7-40
    • Edman, K.A.P.1
  • 34
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • G.I. Bell Models for the specific adhesion of cells to cells Science 200 1978 618 627
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 37
    • 52749093471 scopus 로고    scopus 로고
    • Effect of low pH on single skeletal muscle myosin mechanics and kinetics
    • E.P. Debold, S.E. Beck, and D.M. Warshaw Effect of low pH on single skeletal muscle myosin mechanics and kinetics Am. J. Physiol. Cell Physiol. 295 2008 C173 C179
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Debold, E.P.1    Beck, S.E.2    Warshaw, D.M.3
  • 43
    • 67650522936 scopus 로고    scopus 로고
    • Smooth muscle heavy meromyosin phosphorylated on one of its two heads supports force and motion
    • S. Walcott, and P.M. Fagnant D.M. Warshaw Smooth muscle heavy meromyosin phosphorylated on one of its two heads supports force and motion J. Biol. Chem. 284 2009 18244 18251
    • (2009) J. Biol. Chem. , vol.284 , pp. 18244-18251
    • Walcott, S.1    Fagnant, P.M.2    Warshaw, D.M.3
  • 44
    • 0027272935 scopus 로고
    • Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro
    • D.E. Harris, and D.M. Warshaw Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro J. Biol. Chem. 268 1993 14764 14768 (Pubitemid 23206617)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.20 , pp. 14764-14768
    • Harris, D.E.1    Warshaw, D.M.2
  • 45
    • 79958801934 scopus 로고    scopus 로고
    • Phosphate enhances myosin-powered actin filament velocity under acidic conditions in a motility assay
    • E.P. Debold, and M.A. Turner S. Walcott Phosphate enhances myosin-powered actin filament velocity under acidic conditions in a motility assay Am. J. Physiol. Regul. Integr. Comp. Physiol. 300 2011 R1401 R1408
    • (2011) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.300
    • Debold, E.P.1    Turner, M.A.2    Walcott, S.3
  • 46
    • 77958197530 scopus 로고    scopus 로고
    • Modeling smooth muscle myosin's two heads: Long-lived enzymatic roles and phosphorylation-dependent equilibria
    • S. Walcott, and D.M. Warshaw Modeling smooth muscle myosin's two heads: long-lived enzymatic roles and phosphorylation-dependent equilibria Biophys. J. 99 2010 1129 1138
    • (2010) Biophys. J. , vol.99 , pp. 1129-1138
    • Walcott, S.1    Warshaw, D.M.2
  • 47
    • 77955289401 scopus 로고    scopus 로고
    • Nonlinear elasticity and an 8-nm working stroke of single myosin molecules in myofilaments
    • M. Kaya, and H. Higuchi Nonlinear elasticity and an 8-nm working stroke of single myosin molecules in myofilaments Science 329 2010 686 689
    • (2010) Science , vol.329 , pp. 686-689
    • Kaya, M.1    Higuchi, H.2
  • 48
    • 44049094435 scopus 로고    scopus 로고
    • Single-molecule measurement of the stiffness of the rigor myosin head
    • A. Lewalle, and W. Steffen J. Sleep Single-molecule measurement of the stiffness of the rigor myosin head Biophys. J. 94 2008 2160 2169
    • (2008) Biophys. J. , vol.94 , pp. 2160-2169
    • Lewalle, A.1    Steffen, W.2    Sleep, J.3
  • 49
    • 0031656226 scopus 로고    scopus 로고
    • The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer
    • C. Veigel, and M.L. Bartoo J.E. Molloy The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer Biophys. J. 75 1998 1424 1438 (Pubitemid 28397612)
    • (1998) Biophysical Journal , vol.75 , Issue.3 , pp. 1424-1438
    • Veigel, C.1    Bartoo, M.L.2    White, D.C.S.3    Sparrow, J.C.4    Molloy, J.E.5
  • 50
    • 0042929817 scopus 로고    scopus 로고
    • Actin sliding on reconstituted myosin filaments containing only one myosin heavy chain isoform
    • DOI 10.1023/A:1024871825135
    • T. Scholz, and B. Brenner Actin sliding on reconstituted myosin filaments containing only one myosin heavy chain isoform J. Muscle Res. Cell Motil. 24 2003 77 86 (Pubitemid 37011531)
    • (2003) Journal of Muscle Research and Cell Motility , vol.24 , Issue.1 , pp. 77-86
    • Scholz, T.1    Brenner, B.2
  • 51
    • 84857671126 scopus 로고    scopus 로고
    • An integrated in vitro and in situ study of kinetics of myosin II from frog skeletal muscle
    • R. Elangovan, and M. Capitanio G. Piazzesi An integrated in vitro and in situ study of kinetics of myosin II from frog skeletal muscle J. Physiol. 590 2012 1227 1242
    • (2012) J. Physiol. , vol.590 , pp. 1227-1242
    • Elangovan, R.1    Capitanio, M.2    Piazzesi, G.3
  • 52
    • 0032539594 scopus 로고    scopus 로고
    • Interaction of actin and ADP with the head domain of smooth muscle myosin: Implications for strain-dependent ADP release in smooth muscle
    • DOI 10.1021/bi9722406
    • C.R. Cremo, and M.A. Geeves Interaction of actin and ADP with the head domain of smooth muscle myosin: implications for strain-dependent ADP release in smooth muscle Biochemistry 37 1998 1969 1978 (Pubitemid 28099821)
    • (1998) Biochemistry , vol.37 , Issue.7 , pp. 1969-1978
    • Cremo, C.R.1    Geeves, M.A.2
  • 53
    • 69249101145 scopus 로고
    • A mathematical method for the unique determination of cross-bridge properties from steady-state mechanical and energetic experiments on macroscopic muscle
    • H.M. Lacker, and C.S. Peskin A mathematical method for the unique determination of cross-bridge properties from steady-state mechanical and energetic experiments on macroscopic muscle Lect. Math Life Sci. 16 1986 121 153
    • (1986) Lect. Math Life Sci. , vol.16 , pp. 121-153
    • Lacker, H.M.1    Peskin, C.S.2
  • 54
    • 70449122578 scopus 로고    scopus 로고
    • Binding site models of friction due to the formation and rupture of bonds: State-function formalism, force-velocity relations, response to slip velocity transients, and slip stability
    • M. Srinivasan, and S. Walcott Binding site models of friction due to the formation and rupture of bonds: state-function formalism, force-velocity relations, response to slip velocity transients, and slip stability Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 80 2009 046124
    • (2009) Phys. Rev. e Stat. Nonlin. Soft Matter Phys. , vol.80 , pp. 046124
    • Srinivasan, M.1    Walcott, S.2
  • 55
    • 0025874034 scopus 로고
    • Sliding distance between actin and myosin filaments per ATP molecule hydrolysed in skinned muscle fibres
    • H. Higuchi, and Y.E. Goldman Sliding distance between actin and myosin filaments per ATP molecule hydrolyzed in skinned muscle fibers Nature 352 1991 352 354 (Pubitemid 21912359)
    • (1991) Nature , vol.352 , Issue.6333 , pp. 352-354
    • Higuchi, H.1    Goldman, Y.E.2
  • 56
    • 77957977698 scopus 로고    scopus 로고
    • Coupling between motor proteins determines dynamic behaviors of motor protein assemblies
    • J.W. Driver, and A.R. Rogers M.R. Diehl Coupling between motor proteins determines dynamic behaviors of motor protein assemblies Phys. Chem. Chem. Phys. 12 2010 10398 10405
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 10398-10405
    • Driver, J.W.1    Rogers, A.R.2    Diehl, M.R.3
  • 57
    • 80052447606 scopus 로고    scopus 로고
    • Productive cooperation among processive motors depends inversely on their mechanochemical efficiency
    • J.W. Driver, and D.K. Jamison M.R. Diehl Productive cooperation among processive motors depends inversely on their mechanochemical efficiency Biophys. J. 101 2011 386 395
    • (2011) Biophys. J. , vol.101 , pp. 386-395
    • Driver, J.W.1    Jamison, D.K.2    Diehl, M.R.3
  • 59
    • 0025775887 scopus 로고
    • Simulation of stochastic processes in motile crossbridge systems
    • E. Pate, and R. Cooke Simulation of stochastic processes in motile crossbridge systems J. Muscle Res. Cell Motil. 12 1991 376 393
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 376-393
    • Pate, E.1    Cooke, R.2
  • 62
    • 33645998737 scopus 로고    scopus 로고
    • Phosphorylation of a single head of smooth muscle myosin activates the whole molecule
    • A.S. Rovner, P.M. Fagnant, and K.M. Trybus Phosphorylation of a single head of smooth muscle myosin activates the whole molecule Biochemistry 45 2006 5280 5289
    • (2006) Biochemistry , vol.45 , pp. 5280-5289
    • Rovner, A.S.1    Fagnant, P.M.2    Trybus, K.M.3
  • 64
    • 0020562586 scopus 로고
    • Assembly and kinetic properties of myosin light chain isozymes from fast skeletal muscle
    • S.C. Pastra-Landis, T. Huiatt, and S. Lowey Assembly and kinetic properties of myosin light chain isozymes from fast skeletal muscle J. Mol. Biol. 170 1983 403 422 (Pubitemid 13012674)
    • (1983) Journal of Molecular Biology , vol.170 , Issue.2 , pp. 403-422
    • Pastra Landis, S.C.1    Huiatt, T.2    Lowey, S.3
  • 65
    • 0019317330 scopus 로고
    • Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles
    • S.B. Marston, and E.W. Taylor Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles J. Mol. Biol. 139 1980 573 600
    • (1980) J. Mol. Biol. , vol.139 , pp. 573-600
    • Marston, S.B.1    Taylor, E.W.2
  • 66
    • 0020356742 scopus 로고
    • The binding of smooth muscle heavy meromyosin to actin in the presence of ATP. Effect of phosphorylation
    • J.R. Sellers, E. Eisenberg, and R.S. Adelstein The binding of smooth muscle heavy meromyosin to actin in the presence of ATP. Effect of phosphorylation J. Biol. Chem. 257 1982 13880 13883 (Pubitemid 13139714)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.23 , pp. 13880-13883
    • Sellers, J.R.1    Eisenberg, E.2    Adelstein, R.S.3


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