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Volumn 3, Issue 7, 2007, Pages 1195-1211

Sarcomere lattice geometry influences cooperative myosin binding in muscle

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ACTIVATION; GEOMETRY; MUSCLE; ORDINARY DIFFERENTIAL EQUATIONS; PROTEINS;

EID: 34547597323     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.0030115     Document Type: Article
Times cited : (86)

References (73)
  • 1
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley AF (1957) Muscle structure and theories of contraction. Prog Biophys Biophys Chem 7: 255-318.
    • (1957) Prog Biophys Biophys Chem , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 2
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn RW, Taylor EW (1971) Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10: 4617-4624.
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 3
    • 0018877621 scopus 로고
    • Cross-bridge model of muscle contraction: Quantitative analysis
    • Eisenberg E, Hill TL, Chen Y (1980) Cross-bridge model of muscle contraction: Quantitative analysis. Biophys J 29: 195-227.
    • (1980) Biophys J , vol.29 , pp. 195-227
    • Eisenberg, E.1    Hill, T.L.2    Chen, Y.3
  • 4
    • 0024307990 scopus 로고
    • A model of crossbridge action: The effects of ATP, ADP, and Pi
    • Pate E, Cooke R (1989) A model of crossbridge action: The effects of ATP, ADP, and Pi. J Muscle Res Cell Motil 10: 181-196.
    • (1989) J Muscle Res Cell Motil , vol.10 , pp. 181-196
    • Pate, E.1    Cooke, R.2
  • 5
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman LS (1996) Thin filament-mediated regulation of cardiac contraction. Ann Rev Physiol 58: 447-481.
    • (1996) Ann Rev Physiol , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 6
    • 0031834714 scopus 로고    scopus 로고
    • The effect of ATP analogs on posthydrolytic and force development steps in skinned skeletal muscle fibers
    • Regnier M, Homsher E (1998) The effect of ATP analogs on posthydrolytic and force development steps in skinned skeletal muscle fibers. Biophys J 74: 3059-3071.
    • (1998) Biophys J , vol.74 , pp. 3059-3071
    • Regnier, M.1    Homsher, E.2
  • 7
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon AM, Homsher E, Regnier M (2000) Regulation of contraction in striated muscle. Physiol Rev 80: 853-924.
    • (2000) Physiol Rev , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 8
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley AF, Simmons RM (1971) Proposed mechanism of force generation in striated muscle. Nature 233: 533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 9
    • 0019031856 scopus 로고
    • Theoretical model for the cooperative equilibrium binding of myosin subfragment 1 to the actin-troponin-tropomyosin complex
    • Hill TL, Eisenberg E, Greene L (1980) Theoretical model for the cooperative equilibrium binding of myosin subfragment 1 to the actin-troponin-tropomyosin complex. Proc Natl Acad Sci U S A 77: 3186-3190.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 3186-3190
    • Hill, T.L.1    Eisenberg, E.2    Greene, L.3
  • 10
    • 0028907268 scopus 로고
    • A cross-bridge model that is able to explain mechanical and energetic properties of shortening muscle
    • Piazzesi G, Lombardi V (1995) A cross-bridge model that is able to explain mechanical and energetic properties of shortening muscle. Biophys J 68: 1966-1979.
    • (1995) Biophys J , vol.68 , pp. 1966-1979
    • Piazzesi, G.1    Lombardi, V.2
  • 11
    • 0030687665 scopus 로고    scopus 로고
    • Models of calcium activation account for differences between skeletal and cardiac force redevelopment kinetics
    • Hancock WO, Huntsman LL, Gordon AM (1997) Models of calcium activation account for differences between skeletal and cardiac force redevelopment kinetics. J Muscle Res Cell Motil 18: 671-681.
    • (1997) J Muscle Res Cell Motil , vol.18 , pp. 671-681
    • Hancock, W.O.1    Huntsman, L.L.2    Gordon, A.M.3
  • 12
    • 0034123345 scopus 로고    scopus 로고
    • Different myofilament nearest-neighbor interactions have distinctive effects on contractile behavior
    • Razumova MV, Bukatina AE, Campbell KB (2000) Different myofilament nearest-neighbor interactions have distinctive effects on contractile behavior. Biophys J 78: 3120-3137.
    • (2000) Biophys J , vol.78 , pp. 3120-3137
    • Razumova, M.V.1    Bukatina, A.E.2    Campbell, K.B.3
  • 13
    • 0037305919 scopus 로고    scopus 로고
    • Ising model of cardiac thin filament activation with nearest-neighbor cooperative interactions
    • Rice JJ, Stolovitzky G, Tu Y, de Tombe PP (2003) Ising model of cardiac thin filament activation with nearest-neighbor cooperative interactions. Biophys J 84: 897-909.
    • (2003) Biophys J , vol.84 , pp. 897-909
    • Rice, J.J.1    Stolovitzky, G.2    Tu, Y.3    de Tombe, P.P.4
  • 14
    • 0029758343 scopus 로고    scopus 로고
    • On the theory of muscle contraction: Filament extensibility and the development of isometric force and stiffness
    • Mijailovich SM, Fredberg JJ, Butler JP (1996) On the theory of muscle contraction: Filament extensibility and the development of isometric force and stiffness. Biophys J 71: 1475-1484.
    • (1996) Biophys J , vol.71 , pp. 1475-1484
    • Mijailovich, S.M.1    Fredberg, J.J.2    Butler, J.P.3
  • 15
    • 0031953771 scopus 로고    scopus 로고
    • Compliant realignment of binding sites in muscle: Transient behavior and mechanical tuning
    • Daniel TL, Trimble AC, Chase PB (1998) Compliant realignment of binding sites in muscle: Transient behavior and mechanical tuning. Biophys J 74: 1611-1621.
    • (1998) Biophys J , vol.74 , pp. 1611-1621
    • Daniel, T.L.1    Trimble, A.C.2    Chase, P.B.3
  • 16
    • 0031642991 scopus 로고    scopus 로고
    • Elastically coupled molecular motors
    • Vilfan A, Frey E, Schwabl F (1998) Elastically coupled molecular motors. Eur Phys J B 3: 535-546.
    • (1998) Eur Phys J B , vol.3 , pp. 535-546
    • Vilfan, A.1    Frey, E.2    Schwabl, F.3
  • 18
    • 33845357154 scopus 로고    scopus 로고
    • Filament compliance effects can explain tension overshoots during force development
    • Campbell K (2006) Filament compliance effects can explain tension overshoots during force development. Biophys J 91: 4102-4109.
    • (2006) Biophys J , vol.91 , pp. 4102-4109
    • Campbell, K.1
  • 19
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • Isambert H, Venier P, Maggs AC, Fattoum A, Kassab R, et al. (1995) Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J Biol Chem 270: 11437-11444.
    • (1995) J Biol Chem , vol.270 , pp. 11437-11444
    • Isambert, H.1    Venier, P.2    Maggs, A.C.3    Fattoum, A.4    Kassab, R.5
  • 20
    • 0028081493 scopus 로고
    • X-ray diffraction measurements of the extensibility of the actin and myosin filaments in muscle
    • Huxley H, Stewart A, Sosa H, Irving T (1994) X-ray diffraction measurements of the extensibility of the actin and myosin filaments in muscle. Biophys J 67: 2411-2421.
    • (1994) Biophys J , vol.67 , pp. 2411-2421
    • Huxley, H.1    Stewart, A.2    Sosa, H.3    Irving, T.4
  • 21
    • 0028081494 scopus 로고
    • X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction
    • Wakabayashi K, Sugimoto Y, Tanaka H, Ueno Y, Takezawa Y, et al. (1994) X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction. Biophys J 67: 2422-2435.
    • (1994) Biophys J , vol.67 , pp. 2422-2435
    • Wakabayashi, K.1    Sugimoto, Y.2    Tanaka, H.3    Ueno, Y.4    Takezawa, Y.5
  • 22
    • 0028607563 scopus 로고
    • Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation
    • Kojima H, Ishijima A, Yanagida T (1994) Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation. Proc Natl Acad Sci U S A 91: 12962-12966.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12962-12966
    • Kojima, H.1    Ishijima, A.2    Yanagida, T.3
  • 23
    • 0029162081 scopus 로고
    • Compliance of thin filaments in skinned fibers of rabbit skeletal muscle
    • Higuchi H, Yanagida T, Goldman YE (1995) Compliance of thin filaments in skinned fibers of rabbit skeletal muscle. Biophys J 69: 1000-1010.
    • (1995) Biophys J , vol.69 , pp. 1000-1010
    • Higuchi, H.1    Yanagida, T.2    Goldman, Y.E.3
  • 24
    • 11144353812 scopus 로고    scopus 로고
    • The myosin motor in muscle generates a smaller and slower working stroke at higher load
    • Reconditi M, Linari M, Lucii L, Stewart A, Sun YB, et al. (2004) The myosin motor in muscle generates a smaller and slower working stroke at higher load. Nature 428: 578-581.
    • (2004) Nature , vol.428 , pp. 578-581
    • Reconditi, M.1    Linari, M.2    Lucii, L.3    Stewart, A.4    Sun, Y.B.5
  • 25
    • 33645758327 scopus 로고    scopus 로고
    • Force generation in single conventional actomyosin complexes under high dynamic load
    • Takagi Y, Homsher EE, Goldman YE, Shuman H (2006) Force generation in single conventional actomyosin complexes under high dynamic load. Biophys J 90: 1295-1307.
    • (2006) Biophys J , vol.90 , pp. 1295-1307
    • Takagi, Y.1    Homsher, E.E.2    Goldman, Y.E.3    Shuman, H.4
  • 26
    • 0030950515 scopus 로고    scopus 로고
    • Strain-dependent modulation of phosphate transients in rabbit skeletal muscle fibers
    • Homsher E, Lacktis J, Regnier M (1997) Strain-dependent modulation of phosphate transients in rabbit skeletal muscle fibers. Biophys J 72: 1780-1791.
    • (1997) Biophys J , vol.72 , pp. 1780-1791
    • Homsher, E.1    Lacktis, J.2    Regnier, M.3
  • 27
    • 0035321086 scopus 로고    scopus 로고
    • Skeletal and cardiac muscle contractile activation: Tropomyosin rocks and rolls
    • Gordon AM, Regnier M, Homsher E (2001) Skeletal and cardiac muscle contractile activation: Tropomyosin "rocks and rolls." News Physiol Sci 16: 49-55.
    • (2001) News Physiol Sci , vol.16 , pp. 49-55
    • Gordon, A.M.1    Regnier, M.2    Homsher, E.3
  • 28
    • 0035006418 scopus 로고    scopus 로고
    • Influence of length on force and activation-dependent changes in troponin C structure in skinned cardiac and fast skeletal muscle
    • Martyn DA, Gordon AM (2001) Influence of length on force and activation-dependent changes in troponin C structure in skinned cardiac and fast skeletal muscle. Biophys J 80: 2798-2808.
    • (2001) Biophys J , vol.80 , pp. 2798-2808
    • Martyn, D.A.1    Gordon, A.M.2
  • 30
    • 34547608242 scopus 로고    scopus 로고
    • Simulating different nearest-neighbor interactions with a spatially explicit, calcium-regulated, compliant myofilament model
    • Tanner BCW, Regnier M, Chase PB, Daniel TL (2004) Simulating different nearest-neighbor interactions with a spatially explicit, calcium-regulated, compliant myofilament model. Biophys J 86: 566a.
    • (2004) Biophys J , vol.86
    • Tanner, B.C.W.1    Regnier, M.2    Chase, P.B.3    Daniel, T.L.4
  • 31
    • 34547588959 scopus 로고    scopus 로고
    • A spatially-explicit model of actin and myosin interactions and Ca-based regulation in the cardiac myofilament
    • Rice JJ, de Tombe PP, Hussan J (2006) A spatially-explicit model of actin and myosin interactions and Ca-based regulation in the cardiac myofilament. Biophys J 90: 314a.
    • (2006) Biophys J , vol.90
    • Rice, J.J.1    de Tombe, P.P.2    Hussan, J.3
  • 32
    • 34547609081 scopus 로고    scopus 로고
    • Spatial and temporal characteristics of thin filament activation determine the magnitude and rate of force development in striated muscle
    • Tanner BCW, Daniel TL, Regnier M (2005) Spatial and temporal characteristics of thin filament activation determine the magnitude and rate of force development in striated muscle. Biophys J 88: 128a.
    • (2005) Biophys J , vol.88
    • Tanner, B.C.W.1    Daniel, T.L.2    Regnier, M.3
  • 33
    • 34547583935 scopus 로고    scopus 로고
    • Sarcomere lattice structure influences cooperative, calcium-activated muscle contraction in spatially-explicit model simulations
    • Tanner BCW, Daniel TL, Regnier M (2006) Sarcomere lattice structure influences cooperative, calcium-activated muscle contraction in spatially-explicit model simulations. Biophys J 90: 427a.
    • (2006) Biophys J , vol.90
    • Tanner, B.C.W.1    Daniel, T.L.2    Regnier, M.3
  • 35
    • 34047208553 scopus 로고    scopus 로고
    • Stiffness and fraction of myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas
    • Linari M, Caremani M, Piperio C, Brandt P, Lombardi V (2007) Stiffness and fraction of myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas. Biophys J 92: 2476-2490.
    • (2007) Biophys J , vol.92 , pp. 2476-2490
    • Linari, M.1    Caremani, M.2    Piperio, C.3    Brandt, P.4    Lombardi, V.5
  • 36
    • 0037112540 scopus 로고    scopus 로고
    • The size and the speed of the working stroke of muscle myosin and its dependence on the force
    • Piazzesi G, Lucii L, Lombardi V (2002) The size and the speed of the working stroke of muscle myosin and its dependence on the force. J Physiol 545: 145-151.
    • (2002) J Physiol , vol.545 , pp. 145-151
    • Piazzesi, G.1    Lucii, L.2    Lombardi, V.3
  • 38
    • 0029075829 scopus 로고
    • Unbinding force of a single motor molecule of muscle measured using optical tweezers
    • Nishizaka T, Miyata H, Yoshikawa H, Ishiwata S, Kinosita K (1995) Unbinding force of a single motor molecule of muscle measured using optical tweezers. Nature 377: 251-254.
    • (1995) Nature , vol.377 , pp. 251-254
    • Nishizaka, T.1    Miyata, H.2    Yoshikawa, H.3    Ishiwata, S.4    Kinosita, K.5
  • 39
    • 0030992359 scopus 로고    scopus 로고
    • Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin
    • Nakajima H, Kunioka Y, Nakano K, Shimizu K, Seto M, et al. (1997) Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin. Biochem Biophys Res Commun 234: 178-182.
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 178-182
    • Nakajima, H.1    Kunioka, Y.2    Nakano, K.3    Shimizu, K.4    Seto, M.5
  • 40
    • 0033884332 scopus 로고    scopus 로고
    • Characterization of single actomyosin rigor bonds: Load dependence of lifetime and mechanical properties
    • Nishizaka T, Seo R, Tadakuma H, Kinosita K, Ishiwata S (2000) Characterization of single actomyosin rigor bonds: Load dependence of lifetime and mechanical properties. Biophys J 79: 962-974.
    • (2000) Biophys J , vol.79 , pp. 962-974
    • Nishizaka, T.1    Seo, R.2    Tadakuma, H.3    Kinosita, K.4    Ishiwata, S.5
  • 42
    • 0346057933 scopus 로고    scopus 로고
    • Interplay of troponin- and myosin-based pathways of calcium activation in skeletal and cardiac muscle: The use of W7 as an inhibitor of thin filament activation
    • Adhikari B, Wang K (2004) Interplay of troponin- and myosin-based pathways of calcium activation in skeletal and cardiac muscle: The use of W7 as an inhibitor of thin filament activation. Biophys J 86: 359-370.
    • (2004) Biophys J , vol.86 , pp. 359-370
    • Adhikari, B.1    Wang, K.2
  • 43
    • 0031920485 scopus 로고    scopus 로고
    • Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in skinned rabbit psoas fibers
    • Regnier M, Martyn DA, Chase PB (1998) Calcium regulation of tension redevelopment kinetics with 2-deoxy-ATP or low [ATP] in skinned rabbit psoas fibers. Biophys J 74: 2005-2015.
    • (1998) Biophys J , vol.74 , pp. 2005-2015
    • Regnier, M.1    Martyn, D.A.2    Chase, P.B.3
  • 45
    • 0024007477 scopus 로고    scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction. Proc Natl Acad Sci U S A 85: 3265-3269.
    • (1998) Proc Natl Acad Sci U S A , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 46
    • 0025061076 scopus 로고
    • Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: Implications for regulation of actin-myosin interaction
    • Sweeney HL, Stull JT (1990) Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: Implications for regulation of actin-myosin interaction. Proc Natl Acad Sci U S A 87: 414-418.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 414-418
    • Sweeney, H.L.1    Stull, J.T.2
  • 47
    • 0024312136 scopus 로고
    • Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers: Implications for twitch potentiation in intact muscle
    • Metzger JM, Greaser ML, Moss RL (1989) Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers: Implications for twitch potentiation in intact muscle. J Gen Physiol 93: 855-883.
    • (1989) J Gen Physiol , vol.93 , pp. 855-883
    • Metzger, J.M.1    Greaser, M.L.2    Moss, R.L.3
  • 48
    • 0026646783 scopus 로고
    • Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle
    • Metzger JM, Moss RL (1992) Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle. Biophys J 63: 460-468.
    • (1992) Biophys J , vol.63 , pp. 460-468
    • Metzger, J.M.1    Moss, R.L.2
  • 50
    • 34547584265 scopus 로고    scopus 로고
    • Development of 3-D lattice models for striated muscle contraction with extensible filaments
    • Mijailovich SM, Kojic M, Filipovic N, Smith DA (2005) Development of 3-D lattice models for striated muscle contraction with extensible filaments. Biophys J 88: 18a.
    • (2005) Biophys J , vol.88
    • Mijailovich, S.M.1    Kojic, M.2    Filipovic, N.3    Smith, D.A.4
  • 51
    • 0032808243 scopus 로고    scopus 로고
    • Tropomyosin positions in regulated thin filaments revealed by cryoelectron miscroscopy
    • Xu C, Craig R, Tobacman L, Horowitz R, Lehman W (1999) Tropomyosin positions in regulated thin filaments revealed by cryoelectron miscroscopy. Biophys J 77: 985-992.
    • (1999) Biophys J , vol.77 , pp. 985-992
    • Xu, C.1    Craig, R.2    Tobacman, L.3    Horowitz, R.4    Lehman, W.5
  • 54
    • 0030250140 scopus 로고    scopus 로고
    • Evolution of myosin filament arrangements on vertebrate skeletal muscle
    • Luther PK, Squire JM, Forey PL (1996) Evolution of myosin filament arrangements on vertebrate skeletal muscle. J Morphol 229: 325-335.
    • (1996) J Morphol , vol.229 , pp. 325-335
    • Luther, P.K.1    Squire, J.M.2    Forey, P.L.3
  • 55
    • 17644408404 scopus 로고    scopus 로고
    • Single particle analysis: A new approach to solving the 3D structure of myosin filaments
    • Al-Khayat HA, Morris EP, Squire JM (2004) Single particle analysis: A new approach to solving the 3D structure of myosin filaments. J Muscle Res Cell Motil 25: 635-644.
    • (2004) J Muscle Res Cell Motil , vol.25 , pp. 635-644
    • Al-Khayat, H.A.1    Morris, E.P.2    Squire, J.M.3
  • 56
    • 0031656226 scopus 로고    scopus 로고
    • The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer
    • Veigel C, Bartoo ML, White DC, Sparrow JC, Molloy JE (1998) The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer. Biophys J 75: 1424-1438.
    • (1998) Biophys J , vol.75 , pp. 1424-1438
    • Veigel, C.1    Bartoo, M.L.2    White, D.C.3    Sparrow, J.C.4    Molloy, J.E.5
  • 57
    • 0025123964 scopus 로고
    • The theory of sliding filament models for muscle contraction. III. Dynamics of the five-state model
    • Smith DA (1990) The theory of sliding filament models for muscle contraction. III. Dynamics of the five-state model. J Theor Biol 146: 433-466.
    • (1990) J Theor Biol , vol.146 , pp. 433-466
    • Smith, D.A.1
  • 58
    • 0034084354 scopus 로고    scopus 로고
    • The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle
    • Tesi C, Colomo F, Nencini S, Piroddi N, Poggesi C (2000) The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle. Biophys J 78: 3081-3092.
    • (2000) Biophys J , vol.78 , pp. 3081-3092
    • Tesi, C.1    Colomo, F.2    Nencini, S.3    Piroddi, N.4    Poggesi, C.5
  • 59
    • 0037095908 scopus 로고    scopus 로고
    • Characterization of the cross-bridge force-generating step using inorganic phosphate and BDM in myofibrils from rabbit skeletal muscles
    • Tesi C, Colomo F, Piroddi N, Poggesi C (2002) Characterization of the cross-bridge force-generating step using inorganic phosphate and BDM in myofibrils from rabbit skeletal muscles. J Physiol 541: 187-199.
    • (2002) J Physiol , vol.541 , pp. 187-199
    • Tesi, C.1    Colomo, F.2    Piroddi, N.3    Poggesi, C.4
  • 60
    • 0026694489 scopus 로고
    • Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres
    • Dantzig JA, Goldman YE, Millar NC, Lacktis J, Homsher E (1992) Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres. J Physiol 451: 247-278.
    • (1992) J Physiol , vol.451 , pp. 247-278
    • Dantzig, J.A.1    Goldman, Y.E.2    Millar, N.C.3    Lacktis, J.4    Homsher, E.5
  • 61
    • 0024392532 scopus 로고
    • Addition of phosphate to active muscle fibers probes actomyosin states within the powerstroke
    • Pate E, Cooke R (1989) Addition of phosphate to active muscle fibers probes actomyosin states within the powerstroke. Pflügers Archives 414: 73-81.
    • (1989) Pflügers Archives , vol.414 , pp. 73-81
    • Pate, E.1    Cooke, R.2
  • 62
    • 0031972659 scopus 로고    scopus 로고
    • Depletion of phosphate in active muscle fibers probes actomyosin states within the powerstroke
    • Pate E, Franks-Skiba K, Cooke R (1998) Depletion of phosphate in active muscle fibers probes actomyosin states within the powerstroke. Biophys J 74: 369-380.
    • (1998) Biophys J , vol.74 , pp. 369-380
    • Pate, E.1    Franks-Skiba, K.2    Cooke, R.3
  • 63
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop DF, Geeves MA (1993) Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament. Biophys J 65: 693-701.
    • (1993) Biophys J , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 64
    • 17244378347 scopus 로고    scopus 로고
    • Thermodynamics of stoichiometric biochemical networks in living systems far from equilibrium
    • Qian H, Beard DA (2005) Thermodynamics of stoichiometric biochemical networks in living systems far from equilibrium. Biophys Chem 114: 213-220.
    • (2005) Biophys Chem , vol.114 , pp. 213-220
    • Qian, H.1    Beard, D.A.2
  • 65
    • 0021918919 scopus 로고
    • Kinetic studies of calcium and magnesium binding to troponin C
    • Rosenfeld SS, Taylor EW (1985) Kinetic studies of calcium and magnesium binding to troponin C. J Biol Chem 260: 242-251.
    • (1985) J Biol Chem , vol.260 , pp. 242-251
    • Rosenfeld, S.S.1    Taylor, E.W.2
  • 66
    • 0030052282 scopus 로고    scopus 로고
    • Kinetic studies of calcium binding to the regulatory site of troponin C from cardiac muscle
    • Dong W, Rosenfeld SS, Wang CK, Gordon AM, Cheung HC (1996) Kinetic studies of calcium binding to the regulatory site of troponin C from cardiac muscle. J Biol Chem 271: 688-694.
    • (1996) J Biol Chem , vol.271 , pp. 688-694
    • Dong, W.1    Rosenfeld, S.S.2    Wang, C.K.3    Gordon, A.M.4    Cheung, H.C.5
  • 69
    • 0032734506 scopus 로고    scopus 로고
    • Kinetics of thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz- 2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: Implications for regulation of muscle contraction
    • Brenner B, Chalovich JM (1999) Kinetics of thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz- 2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: Implications for regulation of muscle contraction. Biophys J 77: 2692-2708.
    • (1999) Biophys J , vol.77 , pp. 2692-2708
    • Brenner, B.1    Chalovich, J.M.2
  • 70
    • 0036655688 scopus 로고    scopus 로고
    • Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin c using NMR spectroscopy
    • Li M, Saude E, Wang X, Pearlstone J, Smillie L, et al. (2002) Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin c using NMR spectroscopy. Eur Biophys J 31: 245-256.
    • (2002) Eur Biophys J , vol.31 , pp. 245-256
    • Li, M.1    Saude, E.2    Wang, X.3    Pearlstone, J.4    Smillie, L.5
  • 71
    • 0031799047 scopus 로고    scopus 로고
    • Determinants of relaxation rate in skinned frog skeletal muscle fibers
    • Wahr PA, Johnson JD, Rall JA (1998) Determinants of relaxation rate in skinned frog skeletal muscle fibers. Am J Physiol 274: C1608-C1615.
    • (1998) Am J Physiol , vol.274
    • Wahr, P.A.1    Johnson, J.D.2    Rall, J.A.3
  • 72
    • 23744475805 scopus 로고    scopus 로고
    • Different effects of cardiac versus skeletal muscle regulatory proteins on in vitro measures of actin filament speed and force
    • Clemmens EW, Entezari M, Martyn DA, Regnier M (2005) Different effects of cardiac versus skeletal muscle regulatory proteins on in vitro measures of actin filament speed and force. J Physiol 566: 737-746.
    • (2005) J Physiol , vol.566 , pp. 737-746
    • Clemmens, E.W.1    Entezari, M.2    Martyn, D.A.3    Regnier, M.4
  • 73
    • 13844272490 scopus 로고    scopus 로고
    • 2+ versus crossbridge contribution to force in rabbit skeletal fibres
    • 2+ versus crossbridge contribution to force in rabbit skeletal fibres. J Physiol 562: 873-884.
    • (2005) J Physiol , vol.562 , pp. 873-884
    • Moreno-Gonzalez, A.1    Fredlund, J.2    Regnier, M.3


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