메뉴 건너뛰기




Volumn 48, Issue 3, 1998, Pages 173-179

Functional characterization of cardiac myosin isoforms

Author keywords

ATPase activity; Cardiac myosin; In vitro motility assay

Indexed keywords

MYOSIN;

EID: 0031902620     PISSN: 0021521X     EISSN: None     Source Type: Journal    
DOI: 10.2170/jjphysiol.48.173     Document Type: Review
Times cited : (16)

References (65)
  • 1
    • 0014132503 scopus 로고
    • Contractile state of cardiac muscle obtained from cats with experimentally produced ventricular hypertrophy and heart failure
    • Spaan JFJ, Buccino RA, Sonnenblick EH, and Braunwald E: Contractile state of cardiac muscle obtained from cats with experimentally produced ventricular hypertrophy and heart failure. Circ Res 21. 341-354, 1967
    • (1967) Circ Res , vol.21 , pp. 341-354
    • Spaan, J.F.J.1    Buccino, R.A.2    Sonnenblick, E.H.3    Braunwald, E.4
  • 2
    • 0017055413 scopus 로고
    • The myosin isozymes hypothesis in chronic heart overloading
    • Swyngheauw B, Léger JJ, and Schwartz K. The myosin isozymes hypothesis in chronic heart overloading. J Mol Cell Cardiol 8 915-924, 1976
    • (1976) J Mol Cell Cardiol , vol.8 , pp. 915-924
    • Swyngheauw, B.1    Léger, J.J.2    Schwartz, K.3
  • 3
    • 0016428808 scopus 로고
    • Effects of the thyroid state on the enzymatic characteristics of cardiac myosin
    • Yazaki Y and Raben MS: Effects of the thyroid state on the enzymatic characteristics of cardiac myosin. Circ Res 36 208-215, 1975
    • (1975) Circ Res , vol.36 , pp. 208-215
    • Yazaki, Y.1    Raben, M.S.2
  • 4
    • 0017759572 scopus 로고
    • Evidence for a new cardiac myosin species in thyrotoxic rabbit
    • Flink IL and Morkin E Evidence for a new cardiac myosin species in thyrotoxic rabbit. FEBS Lett 81 391-394, 1977
    • (1977) FEBS Lett , vol.81 , pp. 391-394
    • Flink, I.L.1    Morkin, E.2
  • 5
    • 0018773505 scopus 로고
    • Thyroid hormone stimulates synthesis of a cardiac myosin isozyme Comparison of the two-dimensional electrophoretic patterns of the cyanogen bromide peptides of cardiac myosin heavy chains from euthyroid and thyrotoxic rabbits
    • Flink IL, Rader JH, and Morkin E Thyroid hormone stimulates synthesis of a cardiac myosin isozyme Comparison of the two-dimensional electrophoretic patterns of the cyanogen bromide peptides of cardiac myosin heavy chains from euthyroid and thyrotoxic rabbits J Biol Chem 254 3105-3110, 1979
    • (1979) J Biol Chem , vol.254 , pp. 3105-3110
    • Flink, I.L.1    Rader, J.H.2    Morkin, E.3
  • 6
    • 0017900220 scopus 로고
    • Immunohistochemical evidence for myosin polymorphism in the chicken heart
    • Sartore S, Pierobon-Bormioli S, and Schiaffino S: Immunohistochemical evidence for myosin polymorphism in the chicken heart. Nature 274: 82-83, 1978
    • (1978) Nature , vol.274 , pp. 82-83
    • Sartore, S.1    Pierobon-Bormioli, S.2    Schiaffino, S.3
  • 7
    • 0018093539 scopus 로고
    • Electrophoretic analysis of multiple forms of rat cardiac myosin: Effects of hypophysectomy and thyroxine replacement
    • Hoh JFY, McGrath PA, and Hale PT. Electrophoretic analysis of multiple forms of rat cardiac myosin: effects of hypophysectomy and thyroxine replacement. J Mol Cell Cardiol 10: 1053-1076, 1978
    • (1978) J Mol Cell Cardiol , vol.10 , pp. 1053-1076
    • Hoh, J.F.Y.1    McGrath, P.A.2    Hale, P.T.3
  • 8
    • 0020356172 scopus 로고
    • Molecular cloning of mRNA sequences for cardiac α- and β-form myosin heavy chains, expression in ventricles of normal, hypothyroid, and thyrotoxic rabbits
    • Sinha AM, Umeda PK, Kavinsky CJ, Rajamanickam C, Hsu H-J, Jakovcic S, and Rabinowitz M. Molecular cloning of mRNA sequences for cardiac α- and β-form myosin heavy chains, expression in ventricles of normal, hypothyroid, and thyrotoxic rabbits. Proc Natl Acad Sci USA 79. 5847-5851, 1982
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5847-5851
    • Sinha, A.M.1    Umeda, P.K.2    Kavinsky, C.J.3    Rajamanickam, C.4    Hsu, H.-J.5    Jakovcic, S.6    Rabinowitz, M.7
  • 10
    • 0024785576 scopus 로고
    • Fulllength rat alpha and beta cardiac myosin heavy chain sequences, comparisons suggest a molecular basis for functional differences
    • McNally EM, Gianola KM, and Leinwand LA. Fulllength rat alpha and beta cardiac myosin heavy chain sequences, comparisons suggest a molecular basis for functional differences. J Mol Biol 210: 665-670, 1989
    • (1989) J Mol Biol , vol.210 , pp. 665-670
    • McNally, E.M.1    Gianola, K.M.2    Leinwand, L.A.3
  • 11
    • 0025718558 scopus 로고
    • Complete sequence of human cardiac α-myosin hevy chain gene and amino acid comparison to other myosins based on structural and functional differences
    • Matsuoka R, Beisel KW, Furutani M, Arai S, and Takao A Complete sequence of human cardiac α-myosin hevy chain gene and amino acid comparison to other myosins based on structural and functional differences. Am J Med Genet 41 537-547, 1991
    • (1991) Am J Med Genet , vol.41 , pp. 537-547
    • Matsuoka, R.1    Beisel, K.W.2    Furutani, M.3    Arai, S.4    Takao, A.5
  • 14
    • 0022542030 scopus 로고
    • Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles
    • Swyngheadauw B: Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles. Physiol Rev 66: 710-771, 1986
    • (1986) Physiol Rev , vol.66 , pp. 710-771
    • Swyngheadauw, B.1
  • 15
    • 0021153417 scopus 로고
    • Expression of the cardiac ventricular α- and β-myosin heavy chain genes is developmentally and hormonally regulated
    • Lompre A-M, Nadard-Ginard B, and Mahdavi V: Expression of the cardiac ventricular α- and β-myosin heavy chain genes is developmentally and hormonally regulated. J Biol Chem 259: 6437-6446, 1984
    • (1984) J Biol Chem , vol.259 , pp. 6437-6446
    • Lompre, A.-M.1    Nadard-Ginard, B.2    Mahdavi, V.3
  • 16
    • 0023712742 scopus 로고
    • Thyroid hormone receptor alpha isoforms generated by alternative splicing differentially activate myosin MHC gene transcription
    • Izumo S and Mahdavi V: Thyroid hormone receptor alpha isoforms generated by alternative splicing differentially activate myosin MHC gene transcription. Nature 334: 593-595, 1988
    • (1988) Nature , vol.334 , pp. 593-595
    • Izumo, S.1    Mahdavi, V.2
  • 21
    • 0019474454 scopus 로고
    • The adaptive changes in the isoenzyme pattern of myosin from hypertrophied rat myocardium as a result of pressure overload and physical training
    • Rupp H. The adaptive changes in the isoenzyme pattern of myosin from hypertrophied rat myocardium as a result of pressure overload and physical training Basic Res Cardiol 76. 79-88, 1981
    • (1981) Basic Res Cardiol , vol.76 , pp. 79-88
    • Rupp, H.1
  • 22
    • 0028118280 scopus 로고
    • Effect of chronic energy deprivation on cardiac thyroid hormone receptor and myosin isoform expression
    • Swoap SJ, Haddad F. Bodell P, and Baldwin KM: Effect of chronic energy deprivation on cardiac thyroid hormone receptor and myosin isoform expression. Am J Physiol 266: E254-E260, 1994
    • (1994) Am J Physiol , vol.266
    • Swoap, S.J.1    Haddad, F.2    Bodell, P.3    Baldwin, K.M.4
  • 23
    • 0023645820 scopus 로고
    • Influence of the Dwarf mouse mutation on skeletal and cardiac myosin isoforms Effect of one injection of thyroxine on skeletal and cardiac muscle phenotype
    • Butler-Browne GS, Pruliere G, Cambon N, and Whalen RG: Influence of the Dwarf mouse mutation on skeletal and cardiac myosin isoforms Effect of one injection of thyroxine on skeletal and cardiac muscle phenotype. J Biol Chem 262: 15188-15193, 1987
    • (1987) J Biol Chem , vol.262 , pp. 15188-15193
    • Butler-Browne, G.S.1    Pruliere, G.2    Cambon, N.3    Whalen, R.G.4
  • 24
    • 0024347687 scopus 로고
    • Diabetes and thyroid-hormone-induced changes in cardiac function and their molecular basis
    • Dillmann WH: Diabetes and thyroid-hormone-induced changes in cardiac function and their molecular basis. Annu Rev Med 40: 373-394, 1989
    • (1989) Annu Rev Med , vol.40 , pp. 373-394
    • Dillmann, W.H.1
  • 25
    • 0025980291 scopus 로고
    • Activation of alpha-myosin heavy chain gene expression by cAMP in cultured fetal rat heart myocytes
    • Gupta MP, Gupta M, Stewart A, and Zak R: Activation of alpha-myosin heavy chain gene expression by cAMP in cultured fetal rat heart myocytes Biochem Biophys Res Commun 174: 1196-1203, 1991
    • (1991) Biochem Biophys Res Commun , vol.174 , pp. 1196-1203
    • Gupta, M.P.1    Gupta, M.2    Stewart, A.3    Zak, R.4
  • 26
    • 0017655064 scopus 로고
    • Actin-activated adenosine triphosphatase activity of native and N-ethylmaleimide-modified cardiac myosin from normal and thyrotoxic rabbits
    • Banerjee SK and Morkin E: Actin-activated adenosine triphosphatase activity of native and N-ethylmaleimide-modified cardiac myosin from normal and thyrotoxic rabbits. Circ Res 41: 630-634, 1977
    • (1977) Circ Res , vol.41 , pp. 630-634
    • Banerjee, S.K.1    Morkin, E.2
  • 27
    • 0019319641 scopus 로고
    • The ATPase acitivity of rat cardiac myosin isoenzymes
    • Pope B, Hoh JFY, and Weeds A: The ATPase acitivity of rat cardiac myosin isoenzymes. FEBS Lett 118: 205-208, 1980
    • (1980) FEBS Lett , vol.118 , pp. 205-208
    • Pope, B.1    Hoh, J.F.Y.2    Weeds, A.3
  • 28
    • 0014103605 scopus 로고
    • ATPase activity of myosin correlated with speed of muscle shortening
    • Barany M: ATPase activity of myosin correlated with speed of muscle shortening J Gen Physiol 50: 197-218, 1967
    • (1967) J Gen Physiol , vol.50 , pp. 197-218
    • Barany, M.1
  • 29
    • 0018341460 scopus 로고
    • Calcium-activated muscle from hypertrophied rabbit hearts Mechanical and correlated biochemical changes
    • Maughan D, Low E, Litten R III, Brayden J, and Alpert N: Calcium-activated muscle from hypertrophied rabbit hearts Mechanical and correlated biochemical changes Circ Res 44: 279-287, 1979
    • (1979) Circ Res , vol.44 , pp. 279-287
    • Maughan, D.1    Low, E.2    Litten III, R.3    Brayden, J.4    Alpert, N.5
  • 31
    • 0021244062 scopus 로고
    • Rabbit papillary muscle myosin isozymes and the velocity of muscle shortening
    • Pagani ED and Julian FJ: Rabbit papillary muscle myosin isozymes and the velocity of muscle shortening Circ Res 54: 586-594, 1984
    • (1984) Circ Res , vol.54 , pp. 586-594
    • Pagani, E.D.1    Julian, F.J.2
  • 32
    • 0029185812 scopus 로고
    • Crossbridge dynamics under various inotropic states in cardiac muscle: Evaluation by perturbation analysis
    • Saeki Y. Crossbridge dynamics under various inotropic states in cardiac muscle: evaluation by perturbation analysis. Jpn J Physiol 45: 687-705, 1995
    • (1995) Jpn J Physiol , vol.45 , pp. 687-705
    • Saeki, Y.1
  • 33
    • 0022764709 scopus 로고
    • Influence of V1 and V3 isomyosin on the mechanical behaviour of rat papillary muscle as studied by pseudorandom binary noise modulated length perturbations
    • Rossmanith GH, Hoh JFY, Kirman A, and Kwan LJ: Influence of V1 and V3 isomyosin on the mechanical behaviour of rat papillary muscle as studied by pseudorandom binary noise modulated length perturbations. J Muse Res Cell Motil 7: 307-319, 1986
    • (1986) J Muse Res Cell Motil , vol.7 , pp. 307-319
    • Rossmanith, G.H.1    Hoh, J.F.Y.2    Kirman, A.3    Kwan, L.J.4
  • 34
    • 0023236882 scopus 로고
    • Dynamic stiffness of Barium-contractured cardiac muscle with different speeds of contraction
    • Shibata T, Hunter WC, and Sagawa K: Dynamic stiffness of Barium-contractured cardiac muscle with different speeds of contraction. Circ Res 60: 770-779, 1987
    • (1987) Circ Res , vol.60 , pp. 770-779
    • Shibata, T.1    Hunter, W.C.2    Sagawa, K.3
  • 35
    • 33750822268 scopus 로고    scopus 로고
    • Right ventricular contractile protein function in rats with left ventricular myocardial infarction
    • de Tombe PP, Wannenburg T, Fan D, and Little WC: Right ventricular contractile protein function in rats with left ventricular myocardial infarction Am J Physiol 271: H73-H79, 1996
    • (1996) Am J Physiol , vol.271
    • De Tombe, P.P.1    Wannenburg, T.2    Fan, D.3    Little, W.C.4
  • 36
    • 0023258586 scopus 로고
    • Mechanical properties and ATPase activity in glycerinated cardiac muscle of hyperthyroid rabbit
    • Saeki Y, Kako C, Totsuka T, and Yanagisawa K Mechanical properties and ATPase activity in glycerinated cardiac muscle of hyperthyroid rabbit. Pflugers Arch 408: 578-583, 1987
    • (1987) Pflugers Arch , vol.408 , pp. 578-583
    • Saeki, Y.1    Kako, C.2    Totsuka, T.3    Yanagisawa, K.4
  • 37
    • 0019986514 scopus 로고
    • Energetic consequences of thyroid-modulated shifts in ventricular isomyosin distribution in the rat
    • Loiselle DS, Wendt IR, and Hoh JFY Energetic consequences of thyroid-modulated shifts in ventricular isomyosin distribution in the rat J Musc Res Cell Motil 3: 5-23, 1982
    • (1982) J Musc Res Cell Motil , vol.3 , pp. 5-23
    • Loiselle, D.S.1    Wendt, I.R.2    Hoh, J.F.Y.3
  • 38
    • 0020471098 scopus 로고
    • Heat, mechanics, and myosin ATPase in normal and hypertrophied heart muscle
    • Alpert NR and Mulieri LA: Heat, mechanics, and myosin ATPase in normal and hypertrophied heart muscle. Fed Proc 41: 192-198, 1982
    • (1982) Fed Proc , vol.41 , pp. 192-198
    • Alpert, N.R.1    Mulieri, L.A.2
  • 39
    • 0001825160 scopus 로고
    • Thermomechanical economy of hypertrophied hearts
    • ed. Alpert NR, Raven Press, New York
    • Alpert NR and Mulieri LA Thermomechanical economy of hypertrophied hearts In: Perspectives in Cardiovascular Research, ed. Alpert NR, Raven Press, New York, pp 619-630, 1983
    • (1983) Perspectives in Cardiovascular Research , pp. 619-630
    • Alpert, N.R.1    Mulieri, L.A.2
  • 40
    • 0025219047 scopus 로고
    • 2 consumption and systolic pressure-volume area or force-time integral
    • 2 consumption and systolic pressure-volume area or force-time integral. Circ Res 66: 999-1011, 1990
    • (1990) Circ Res , vol.66 , pp. 999-1011
    • Goto, Y.1    Slinker, B.K.2    LeWinter, M.M.3
  • 41
    • 0025854582 scopus 로고
    • Hyperthyroid dog left ventricle has the same oxygen consumption versus pressure-volume area (PVA) relation as euthyroid dog
    • Suga H, Tanaka N, Ohgoshi Y, Saeki Y, Nakanishi T. Futaki S, Yaku H, and Goto Y: Hyperthyroid dog left ventricle has the same oxygen consumption versus pressure-volume area (PVA) relation as euthyroid dog. Heart Vessels 6: 71-83, 1991
    • (1991) Heart Vessels , vol.6 , pp. 71-83
    • Suga, H.1    Tanaka, N.2    Ohgoshi, Y.3    Saeki, Y.4    Nakanishi, T.5    Futaki, S.6    Yaku, H.7    Goto, Y.8
  • 42
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction. Interference microscopy of living muscle fibers
    • Huxley AF and Niedergerke R: Structural changes in muscle during contraction. Interference microscopy of living muscle fibers Nature 173: 971-973, 1954
    • (1954) Nature , vol.173 , pp. 971-973
    • Huxley, A.F.1    Niedergerke, R.2
  • 43
    • 36949093311 scopus 로고
    • Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation
    • Huxley HE and Hanson J Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature 173: 973-976, 1954
    • (1954) Nature , vol.173 , pp. 973-976
    • Huxley, H.E.1    Hanson, J.2
  • 44
    • 0020586332 scopus 로고
    • Movement of myosin-coated fluorescent beads on actin cables in vitro
    • Sheetz MP and Spudich JA: Movement of myosin-coated fluorescent beads on actin cables in vitro Nature 303: 31-35, 1983
    • (1983) Nature , vol.303 , pp. 31-35
    • Sheetz, M.P.1    Spudich, J.A.2
  • 45
    • 0000542287 scopus 로고
    • Active sliding movement of latex beads coated with skeletal muscle myosin on Chara actin cables
    • Shimmen T and Yano M: Active sliding movement of latex beads coated with skeletal muscle myosin on Chara actin cables. Protoplasma 121. 132-137, 1984
    • (1984) Protoplasma , vol.121 , pp. 132-137
    • Shimmen, T.1    Yano, M.2
  • 47
    • 0027673796 scopus 로고
    • Scanning electron microscopy of the myosin-coated surface of polystyrene beads in a force-movement assay system for ATP-dependent actin-myosin sliding
    • Takahashi K, Oiwa K, Kawakami T, Tanaka H, and Sugi H Scanning electron microscopy of the myosin-coated surface of polystyrene beads in a force-movement assay system for ATP-dependent actin-myosin sliding. J Electron Microsc 42: 334-337, 1993
    • (1993) J Electron Microsc , vol.42 , pp. 334-337
    • Takahashi, K.1    Oiwa, K.2    Kawakami, T.3    Tanaka, H.4    Sugi, H.5
  • 48
    • 0027236561 scopus 로고
    • Dynamic interaction between cardiac myosin isoforms modifies velocity of actomyosin sliding in vitro
    • Sata M, Sugiura S, Yamashita H, Momomura S, and Serizawa T: Dynamic interaction between cardiac myosin isoforms modifies velocity of actomyosin sliding in vitro. Circ Res 73: 696-704, 1993
    • (1993) Circ Res , vol.73 , pp. 696-704
    • Sata, M.1    Sugiura, S.2    Yamashita, H.3    Momomura, S.4    Serizawa, T.5
  • 49
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron SJ and Spudich JA: Fluorescent actin filaments move on myosin fixed to a glass surface Proc Natl Acad Sci USA 83: 6272-6276, 1986
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 50
    • 0021719038 scopus 로고
    • ATP-dependent movement of myosin in vitro. Characterization of a quantitative assay
    • Sheetz MP, Chasan R, and Spudich JA: ATP-dependent movement of myosin in vitro. characterization of a quantitative assay. J Cell Biol 99. 1867-1871, 1984
    • (1984) J Cell Biol , vol.99 , pp. 1867-1871
    • Sheetz, M.P.1    Chasan, R.2    Spudich, J.A.3
  • 51
    • 0022341943 scopus 로고
    • Light chain phosphorylation regulates the movement of smooth muscle myosin on actin filament
    • Sellers JR, Spudich JA, and Sheetz MP. Light chain phosphorylation regulates the movement of smooth muscle myosin on actin filament. J Cell Biol 101. 1897-1902, 1985
    • (1985) J Cell Biol , vol.101 , pp. 1897-1902
    • Sellers, J.R.1    Spudich, J.A.2    Sheetz, M.P.3
  • 52
    • 0025335344 scopus 로고
    • Smooth muscle myosin cross-bridge interactions modulate actin filament velocity in vitro
    • Warshaw DM, Desrosiers JM, Work SS, and Trybus KM: Smooth muscle myosin cross-bridge interactions modulate actin filament velocity in vitro J Cell Biol 111: 453-463, 1990
    • (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
  • 54
    • 0024994297 scopus 로고
    • Steady-state force-velocity relation in the ATP-dependent sliding movement of myosin-coated beads on actin cables in vitro studied with a centrifuge microscope
    • Oiwa K, Chaen S, Kamitsubo E, Shimmen T, and Sugi H: Steady-state force-velocity relation in the ATP-dependent sliding movement of myosin-coated beads on actin cables in vitro studied with a centrifuge microscope. Proc Natl Acad Sci USA 87: 7893-7897, 1990
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7893-7897
    • Oiwa, K.1    Chaen, S.2    Kamitsubo, E.3    Shimmen, T.4    Sugi, H.5
  • 55
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • Kishino A and Yanagida T: Force measurements by micromanipulation of a single actin filament by glass needles. Nature 334 74-76, 1988
    • (1988) Nature , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 58
    • 0022655537 scopus 로고
    • Observation of a single-beam gradient force optical trap for dielectric particles
    • Ashkin A, Dziedzic JM, Bjorkholm JE, and Chu S: Observation of a single-beam gradient force optical trap for dielectric particles. Optics Lett 11: 288-290, 1986
    • (1986) Optics Lett , vol.11 , pp. 288-290
    • Ashkin, A.1    Dziedzic, J.M.2    Bjorkholm, J.E.3    Chu, S.4
  • 59
    • 0023663919 scopus 로고
    • Optical trapping and manipulation of single cells using infrared laser beams
    • Ashkin A, Dziedzic JM, and Yamane T: Optical trapping and manipulation of single cells using infrared laser beams. Nature 330 769-771, 1987
    • (1987) Nature , vol.330 , pp. 769-771
    • Ashkin, A.1    Dziedzic, J.M.2    Yamane, T.3
  • 60
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied with optical tweezers
    • Block SM, Goldstein LS, and Schnapp BJ: Bead movement by single kinesin molecules studied with optical tweezers. Nature 348. 348-352, 1990
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.2    Schnapp, B.J.3
  • 61
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics. piconewton forces and nanometre steps
    • Finer JT, Simmons RM, and Spudich JA: Single myosin molecule mechanics. piconewton forces and nanometre steps Nature 368: 113-119, 1994
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 63
    • 0032104084 scopus 로고    scopus 로고
    • Comparison of unitary displacements and forces between two cardiac myosin isoforms by the optical trap technique. molecular basis for cardiac adaptation
    • Sugiura S. Kobayakawa N, Fujita H, Yamashita H, Momomura S, Chaen S, Omata M, and Sugi H: Comparison of unitary displacements and forces between two cardiac myosin isoforms by the optical trap technique. molecular basis for cardiac adaptation. Circ Res 82. 1029-1034, 1998
    • (1998) Circ Res , vol.82 , pp. 1029-1034
    • Sugiura, S.1    Kobayakawa, N.2    Fujita, H.3    Yamashita, H.4    Momomura, S.5    Chaen, S.6    Omata, M.7    Sugi, H.8
  • 64
    • 0031041817 scopus 로고    scopus 로고
    • Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacement in the laser trap
    • Guilford WH, Dupuis DE, Kennedy G, Wu J, Patlak JB, and Warshaw DM Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacement in the laser trap. Biophys J 72 1006-1021, 1997
    • (1997) Biophys J , vol.72 , 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
  • 65
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • Ishijima A, Kojima H, Funatsu T, Tokunaga M, Higuchi H, Tanaka H, and Yanagida T: Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92 161-171, 1998
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.