메뉴 건너뛰기




Volumn 71, Issue 4, 1996, Pages 1891-1904

Calcium alone does not fully activate the thin filament for S1 binding to rigor myofibrils

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALCIUM ION; TROPOMYOSIN; TROPONIN;

EID: 0029840598     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79388-8     Document Type: Article
Times cited : (72)

References (55)
  • 1
    • 0021068068 scopus 로고
    • Kinetic model for the interaction of myosin subfragment 1 with regulated actin
    • Balazs, A. C., and I. R. Epstein, 1983. Kinetic model for the interaction of myosin subfragment 1 with regulated actin. Biophys. J. 44:145-151.
    • (1983) Biophys. J. , vol.44 , pp. 145-151
    • Balazs, A.C.1    Epstein, I.R.2
  • 2
    • 0023187156 scopus 로고
    • Co-operative interactions between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle
    • Brandt, P. W., M. S. Diamond, J. S. Rutchik, and F. H. Schachat. 1987. Co-operative interactions between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle. J. Mol. Biol. 195:885-896.
    • (1987) J. Mol. Biol. , vol.195 , pp. 885-896
    • Brandt, P.W.1    Diamond, M.S.2    Rutchik, J.S.3    Schachat, F.H.4
  • 3
    • 0015525066 scopus 로고
    • Cooperation within actin filament in vertebrate skeletal muscle
    • Bremel, R. D., and A. Weber. 1972. Cooperation within actin filament in vertebrate skeletal muscle. Nature New Biol. 238:97-101.
    • (1972) Nature New Biol. , vol.238 , pp. 97-101
    • Bremel, R.D.1    Weber, A.2
  • 4
    • 0024007477 scopus 로고
    • 2+ on crossbridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ on crossbridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc. Nail. Acad. Sci. USA. 85:3265-3269.
    • (1988) Proc. Nail. Acad. Sci. USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 5
    • 0027509324 scopus 로고
    • Subsarcomeric distribution of calcium in demembranated fibers of rabbit psoas
    • Cantino, M. E., T. StC. Allen, and A. M. Gordon. 1993. Subsarcomeric distribution of calcium in demembranated fibers of rabbit psoas. Biophys. J. 64:211-222.
    • (1993) Biophys. J. , vol.64 , pp. 211-222
    • Cantino, M.E.1    Allen, T.St.C.2    Gordon, A.M.3
  • 6
    • 0020681165 scopus 로고
    • Inorganic phosphate assay with malachite green: An improvement and evaluation
    • Carter, S. G., and D. W. Karl. 1982. Inorganic phosphate assay with malachite green: an improvement and evaluation. J. Biochem. Biophys. Methods. 7:7-13.
    • (1982) J. Biochem. Biophys. Methods , vol.7 , pp. 7-13
    • Carter, S.G.1    Karl, D.W.2
  • 7
    • 0027093717 scopus 로고
    • Actin mediated regulation of muscle contraction
    • Chalovich, J. M. 1992. Actin mediated regulation of muscle contraction. Pharmacol. Ther. 55:95-148.
    • (1992) Pharmacol. Ther. , vol.55 , pp. 95-148
    • Chalovich, J.M.1
  • 8
    • 0019519880 scopus 로고
    • Mechanism of action of troponin-tropomyosin. Inhibition of actomyosin ATPase activity without inhibition of myosin binding to actin
    • Chalovich, J. M., P. B. Chock, and E. Eisenberg. 1981. Mechanism of action of troponin-tropomyosin. Inhibition of actomyosin ATPase activity without inhibition of myosin binding to actin. J. Biol. Chem. 256:575-578.
    • (1981) J. Biol. Chem. , vol.256 , pp. 575-578
    • Chalovich, J.M.1    Chock, P.B.2    Eisenberg, E.3
  • 9
    • 0019977525 scopus 로고
    • Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin
    • Chalovich, J. M., and E. Eisenberg. 1982. Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin. J. Biol. Chem. 257:2432-2437.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2432-2437
    • Chalovich, J.M.1    Eisenberg, E.2
  • 10
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free or tree from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands
    • Fabiato, A. 1988. Computer programs for calculating total from specified free or tree from specified total ionic concentrations in aqueous solutions containing multiple metals and ligands. Methods Enzymol. 157:378-417.
    • (1988) Methods Enzymol. , vol.157 , pp. 378-417
    • Fabiato, A.1
  • 11
    • 0024402489 scopus 로고
    • Factors affecting polyacrylamide gel electrophoresis of high molecular weight myofibrillar proteins
    • Fritz, J. D., D. R. Swartz, and M. L. Greaser. 1989. Factors affecting polyacrylamide gel electrophoresis of high molecular weight myofibrillar proteins. Anal. Biochem. 180:205-210.
    • (1989) Anal. Biochem. , vol.180 , pp. 205-210
    • Fritz, J.D.1    Swartz, D.R.2    Greaser, M.L.3
  • 12
    • 0026082863 scopus 로고
    • The dynamics of actin and myosin association and the crossbridge model of muscle contraction
    • Geeves, M. A. 1991. The dynamics of actin and myosin association and the crossbridge model of muscle contraction. Biochem. J. 274:1-14.
    • (1991) Biochem. J. , vol.274 , pp. 1-14
    • Geeves, M.A.1
  • 13
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit
    • Geeves, M. A., and S. S. Lehrer. 1994. Dynamics of the muscle thin filament regulatory switch: the size of the cooperative unit. Biophys. J. 67:273-282.
    • (1994) Biophys. J. , vol.67 , pp. 273-282
    • Geeves, M.A.1    Lehrer, S.S.2
  • 14
    • 0019974315 scopus 로고
    • Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog
    • Godt, R. E., and B. D. Lindley. 1982. Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog. J. Gen. Physiol. 80:279-297.
    • (1982) J. Gen. Physiol. , vol.80 , pp. 279-297
    • Godt, R.E.1    Lindley, B.D.2
  • 15
    • 29744466425 scopus 로고
    • Determination of serum protein by means of the biuret reaction
    • Gornall, A. G., C. J. Bardawill, and M. M. David. 1949. Determination of serum protein by means of the biuret reaction. J. Biol. Chem. 177:751-766.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 17
    • 0019013686 scopus 로고
    • Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex
    • Greene, L. E., and E. Eisenberg. 1980. Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc. Natl. Acad. Sci. USA. 77:2616-2620.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2616-2620
    • Greene, L.E.1    Eisenberg, E.2
  • 18
    • 0023238920 scopus 로고
    • Regulation of actomyosin ATPase activity by troponin-tropomyosin: Effect of the binding of the myosin subfragment 1 (S1)-ATP complex
    • Greene, L. E., D. L. Williams, and E. Eisenberg. 1987. Regulation of actomyosin ATPase activity by troponin-tropomyosin: effect of the binding of the myosin subfragment 1 (S1)-ATP complex. Proc. Natl. Acad. Sci. USA. 84:3102-3106.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3102-3106
    • Greene, L.E.1    Williams, D.L.2    Eisenberg, E.3
  • 19
    • 0023645610 scopus 로고
    • 2+-specific regulatory sites in skinned rabbit psoas fibers
    • 2+-specific regulatory sites in skinned rabbit psoas fibers. J. Biol. Chem. 262:13627-13635.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13627-13635
    • Güth, K.1    Potter, J.D.2
  • 20
    • 0000733783 scopus 로고
    • X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle
    • Haselgrove, J. C. 1973. X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle. Cold Spring Harb. Symp. Quant. Biol. 37:341-352.
    • (1973) Cold Spring Harb. Symp. Quant. Biol. , vol.37 , pp. 341-352
    • Haselgrove, J.C.1
  • 21
    • 0028887715 scopus 로고
    • Characterization of the equilibrium between blocked and closed states of muscle thin filaments
    • Head, J. G., M. D. Ritchie, and M. A. Geeves. 1995. Characterization of the equilibrium between blocked and closed states of muscle thin filaments. Eur. J. Biochem. 227:694-699.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 694-699
    • Head, J.G.1    Ritchie, M.D.2    Geeves, M.A.3
  • 22
    • 0019031856 scopus 로고
    • Theoretical model for the cooperative equilibrium binding of myosin subfragment 1 to the actin-troponin-tropomyosin complex
    • Hill, T. L., E. Eisenberg, and L. E. Greene. 1980. Theoretical model for the cooperative equilibrium binding of myosin subfragment 1 to the actin-troponin-tropomyosin complex. Proc. Natl. Acad. Sci. USA. 77:3186-3190.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3186-3190
    • Hill, T.L.1    Eisenberg, E.2    Greene, L.E.3
  • 23
    • 0020669295 scopus 로고
    • Alternate model for the cooperative equilibrium binding of myosin subfragment-1-nucleotide complex to actin-troponin-tropomyosin
    • Hill, T. L., E. Eisenberg, and L. E. Greene. 1983. Alternate model for the cooperative equilibrium binding of myosin subfragment-1-nucleotide complex to actin-troponin-tropomyosin. Proc. Nail. Acad. Sci. USA. 80:60-64.
    • (1983) Proc. Nail. Acad. Sci. USA , vol.80 , pp. 60-64
    • Hill, T.L.1    Eisenberg, E.2    Greene, L.E.3
  • 24
    • 0000244537 scopus 로고
    • Structural changes in the actin and myosin containing filaments during contraction
    • Huxley, H. E. 1973. Structural changes in the actin and myosin containing filaments during contraction. Cold Spring Harb. Symp. Quant, Biol. 37:361-376.
    • (1973) Cold Spring Harb. Symp. Quant, Biol. , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 25
    • 0023651178 scopus 로고
    • Fluorescence probe studies on the state of tropomyosin in reconstituted muscle thin filaments
    • Ishii, Y., and S. S. Lehrer. 1987. Fluorescence probe studies on the state of tropomyosin in reconstituted muscle thin filaments. Biochemistry. 26:4922-4925.
    • (1987) Biochemistry , vol.26 , pp. 4922-4925
    • Ishii, Y.1    Lehrer, S.S.2
  • 26
    • 0023042009 scopus 로고
    • Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction
    • Kress, M., H. E. Huxley, A. R. Farqui, and J. Hendrix. 1986. Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction. J. Mol. Biol. 188:325-342.
    • (1986) J. Mol. Biol. , vol.188 , pp. 325-342
    • Kress, M.1    Huxley, H.E.2    Farqui, A.R.3    Hendrix, J.4
  • 27
    • 0021151109 scopus 로고
    • Thin filament proteins and thin filament linked regulation of vertebrate muscle contraction
    • Leavis, P. C., and J. Gergely. 1984. Thin filament proteins and thin filament linked regulation of vertebrate muscle contraction. CRC Crit. Rev. Biochem. 16:235-305.
    • (1984) CRC Crit. Rev. Biochem. , vol.16 , pp. 235-305
    • Leavis, P.C.1    Gergely, J.2
  • 28
    • 0028179144 scopus 로고
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature. 368:65-67.
    • (1994) Nature , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 30
    • 0020490904 scopus 로고
    • Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase
    • Lehrer, S. S., and E. P. Morris. 1982. Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase. J. Biol. Chem. 257:8073-8080.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8073-8080
    • Lehrer, S.S.1    Morris, E.P.2
  • 31
    • 0028940312 scopus 로고
    • An atomic model of the unregulated thin filament obtained by X-ray diffraction of oriented actin-tropomyosin gels
    • Lorenz, M., K. J. V. Poole, D. Popp, G. Rosenbaum, and K. C. Holmes. 1995. An atomic model of the unregulated thin filament obtained by X-ray diffraction of oriented actin-tropomyosin gels. J. Mol. Biol. 246:108-119.
    • (1995) J. Mol. Biol. , vol.246 , pp. 108-119
    • Lorenz, M.1    Poole, K.J.V.2    Popp, D.3    Rosenbaum, G.4    Holmes, K.C.5
  • 32
    • 0025990625 scopus 로고
    • Regulation of the actomyosin subfragment 1 interaction by troponin/tropomyosin
    • McKillop, D. F. A., and M. A. Geeves. 1991. Regulation of the actomyosin subfragment 1 interaction by troponin/tropomyosin. Biochem. J. 279:711-718.
    • (1991) Biochem. J. , vol.279 , pp. 711-718
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 33
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1 : Evidence for three states of the thin filament
    • McKillop, D. F. A., and M. A. Geeves. 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.A.1    Geeves, M.A.2
  • 34
    • 0000524425 scopus 로고
    • New method for quantitative determination of serum proteins separated by paper electrophoresis
    • Mejbaum-Katzenellenbogen, W., and W. Dobryszycka. 1959. New method for quantitative determination of serum proteins separated by paper electrophoresis. Clin. Chim. Acta. 4:515-522.
    • (1959) Clin. Chim. Acta , vol.4 , pp. 515-522
    • Mejbaum-Katzenellenbogen, W.1    Dobryszycka, W.2
  • 35
    • 0022500567 scopus 로고
    • Effects on shortening velocity of rabbit skeletal muscle due to variations in the level of thin filament activation
    • Moss, R. L. 1986. Effects on shortening velocity of rabbit skeletal muscle due to variations in the level of thin filament activation. J. Physiol. (Lond.). 377:487-505.
    • (1986) J. Physiol. (Lond.) , vol.377 , pp. 487-505
    • Moss, R.L.1
  • 36
    • 0019888840 scopus 로고
    • Cooperativity of the calcium switch of regulated aclomyosin system
    • Murray, J. M., and A. Weber. 1980. Cooperativity of the calcium switch of regulated aclomyosin system. Mol. Cell. Biochem. 35:11-15.
    • (1980) Mol. Cell. Biochem. , vol.35 , pp. 11-15
    • Murray, J.M.1    Weber, A.2
  • 37
    • 0019435182 scopus 로고
    • Myosin subfragment 1 binding to relaxed actin filaments and steric model of relaxation
    • Murray, J. M., A. Weber, and M. K. Knox. 1981. Myosin subfragment 1 binding to relaxed actin filaments and steric model of relaxation. Biochemistry. 20:641-649.
    • (1981) Biochemistry , vol.20 , pp. 641-649
    • Murray, J.M.1    Weber, A.2    Knox, M.K.3
  • 38
    • 0020024384 scopus 로고
    • Studies on the co-operative properties of tropomyosin-actin and tropomyosin-troponin-actin complexes by the use of N-ethylmaleimide-treated and untreated species of myosin subfragment I
    • Nagashima, H., and S. Asakura. 1982. Studies on the co-operative properties of tropomyosin-actin and tropomyosin-troponin-actin complexes by the use of N-ethylmaleimide-treated and untreated species of myosin subfragment I. J. Mol. Biol. 155:409-428.
    • (1982) J. Mol. Biol. , vol.155 , pp. 409-428
    • Nagashima, H.1    Asakura, S.2
  • 39
    • 0024349096 scopus 로고
    • Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle
    • Pan, B.-S., A.-M. Gordon, and Z. Luo. 1989. Removal of tropomyosin overlap modifies cooperative binding of myosin S-1 to reconstituted thin filaments of rabbit striated muscle. J. Biol. Chem. 264:8495-8498.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8495-8498
    • Pan, B.-S.1    Gordon, A.-M.2    Luo, Z.3
  • 40
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J. D., and J. A. Spudich. 1982. Purification of muscle actin. Methods Enzymol. 85:164-181.
    • (1982) Methods Enzymol. , vol.85 , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 41
    • 0015935349 scopus 로고
    • The role of tropomyosin in muscle regulation: Analysis of the X-ray diffraction patterns from relaxed and contracting muscles
    • Parry, D. A. D., and J. M. Squire. 1973. The role of tropomyosin in muscle regulation: analysis of the X-ray diffraction patterns from relaxed and contracting muscles. J. Mol. Biol. 75:33-55.
    • (1973) J. Mol. Biol. , vol.75 , pp. 33-55
    • Parry, D.A.D.1    Squire, J.M.2
  • 42
    • 0027447838 scopus 로고
    • Calcium ions and the structure of muscle actin filament. An X-ray diffraction study
    • Popp, D., and Y. Maéda. 1993. Calcium ions and the structure of muscle actin filament. An X-ray diffraction study. J. Mol. Biol. 229:279-285.
    • (1993) J. Mol. Biol. , vol.229 , pp. 279-285
    • Popp, D.1    Maéda, Y.2
  • 43
    • 0028256424 scopus 로고
    • The three-dimensional structure of a molecular motor
    • Rayment, I., and H. M. Holden. 1994. The three-dimensional structure of a molecular motor. Trends Biochem. Sci. 19:129-134.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 129-134
    • Rayment, I.1    Holden, H.M.2
  • 44
    • 0023664678 scopus 로고
    • The mechanism of regulation of actomyosin subfragment 1 ATPase
    • Rosenfeld, S. S., and E. W. Taylor. 1987. The mechanism of regulation of actomyosin subfragment 1 ATPase. J. Biol. Chem. 262:9984-9993.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9984-9993
    • Rosenfeld, S.S.1    Taylor, E.W.2
  • 45
    • 0028229830 scopus 로고
    • The actomyosin interaction - Shedding light on structural events: "Plus ça change, plus c'est la même chose."
    • Squire, J. M. 1994. The actomyosin interaction - shedding light on structural events: "Plus ça change, plus c'est la même chose." J. Muscle Re. Cell Motil. 15:227-231.
    • (1994) J. Muscle Re. Cell Motil. , vol.15 , pp. 227-231
    • Squire, J.M.1
  • 46
    • 0025605176 scopus 로고
    • Regulation of binding of subfragment 1 in isolated rigor myofibrils
    • Swartz, D. R., M. L. Greaser, and B. B. Marsh. 1990. Regulation of binding of subfragment 1 in isolated rigor myofibrils. J. Cell Biol. 111:2989-3001.
    • (1990) J. Cell Biol. , vol.111 , pp. 2989-3001
    • Swartz, D.R.1    Greaser, M.L.2    Marsh, B.B.3
  • 47
    • 43949172570 scopus 로고
    • Structural studies of rigor bovine myofibrils using fluorescence microscopy. II. Influence of sarcomere length on the binding of myosin subfragment-1, alpha-actinin and G-actin to rigor myofibrils
    • Swartz, D. R., M. L. Greaser, and B. B. Marsh. 1993. Structural studies of rigor bovine myofibrils using fluorescence microscopy. II. Influence of sarcomere length on the binding of myosin subfragment-1, alpha-actinin and G-actin to rigor myofibrils. Meat Sci. 33:157-190.
    • (1993) Meat Sci. , vol.33 , pp. 157-190
    • Swartz, D.R.1    Greaser, M.L.2    Marsh, B.B.3
  • 48
    • 0026774946 scopus 로고
    • 2+-sensitive mechanical properties of skinned skeletal muscle fibers
    • 2+-sensitive mechanical properties of skinned skeletal muscle fibers. J. Bioll. Chem. 267:20497-20506.
    • (1992) J. Bioll. Chem. , vol.267 , pp. 20497-20506
    • Swartz, D.R.1    Moss, R.L.2
  • 49
    • 0019128230 scopus 로고
    • Kinetic studies of the cooperative binding of subfragment 1 to regulated actin
    • Trybus, K. M., and E. W. Taylor. 1980. Kinetic studies of the cooperative binding of subfragment 1 to regulated actin. Proc. Natl. Acad. Sci. USA. 77:7209-7213.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7209-7213
    • Trybus, K.M.1    Taylor, E.W.2
  • 50
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility
    • Weeds, A. G., and B. Pope. 1977. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111:129-157.
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 51
    • 0023747148 scopus 로고
    • Cooperative turning on of myosin subfragment 1 adenosine triphosphatase activity by the troponin-tropomyosin-actin complex
    • Williams, D. L., L. E. Greene, and E. Eisenberg. 1988. Cooperative turning on of myosin subfragment 1 adenosine triphosphatase activity by the troponin-tropomyosin-actin complex. Biochemistry. 27:6987-6993.
    • (1988) Biochemistry , vol.27 , pp. 6987-6993
    • Williams, D.L.1    Greene, L.E.2    Eisenberg, E.3
  • 52
    • 0021112289 scopus 로고
    • Quantitative determination of myosin and actin in rabbit skeletal muscle
    • Yates, L. D., and M. L. Greaser. 1983. Quantitative determination of myosin and actin in rabbit skeletal muscle. J. Mol. Biol. 168:123-141.
    • (1983) J. Mol. Biol. , vol.168 , pp. 123-141
    • Yates, L.D.1    Greaser, M.L.2
  • 53
    • 0024491838 scopus 로고
    • Image fidelity: Characterizing the imaging transfer function
    • Young, I. T. 1989. Image fidelity: characterizing the imaging transfer function. Methods Cell Biol. 30:1-45.
    • (1989) Methods Cell Biol. , vol.30 , pp. 1-45
    • Young, I.T.1
  • 54
    • 0023654087 scopus 로고
    • 2+ dependence of ATPase and tension development of fast skeletal muscle
    • 2+ dependence of ATPase and tension development of fast skeletal muscle. J. Biol. Chem. 262:1966-1969.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1966-1969
    • Zot, A.S.1    Potter, J.D.2
  • 55
    • 0024399874 scopus 로고
    • Reciprocal coupling between troponin C and myosin crossbridge attachment
    • Zot, A. S., and J. D. Potter. 1989. Reciprocal coupling between troponin C and myosin crossbridge attachment. Biochemistry. 28:6751-6756.
    • (1989) Biochemistry , vol.28 , pp. 6751-6756
    • Zot, A.S.1    Potter, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.