메뉴 건너뛰기




Volumn 85, Issue 4, 2003, Pages 2492-2506

Static and dynamic x-ray diffraction recordings from living mammalian and amphibian skeletal muscles

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 0141754066     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74672-4     Document Type: Article
Times cited : (34)

References (78)
  • 1
    • 0029094238 scopus 로고
    • Structural changes in actin-tropomyosin during muscle regulation: Computer modelling of low-angle X-ray diffraction data
    • Al-Khayat, H. A., N. Yagi, and J. M. Squire. 1995. Structural changes in actin-tropomyosin during muscle regulation: computer modelling of low-angle X-ray diffraction data. J. Mol. Biol. 252:611-632.
    • (1995) J. Mol. Biol. , vol.252 , pp. 611-632
    • Al-Khayat, H.A.1    Yagi, N.2    Squire, J.M.3
  • 3
    • 0017904793 scopus 로고
    • Calcium transients in isolated skeletal muscle fibres: Detection with aequorin
    • Blinks, J. R., R. Rüdel, and S. R. Taylor. 1978. Calcium transients in isolated skeletal muscle fibres: detection with aequorin. J. Physiol. 277:291-323.
    • (1978) J. Physiol. , vol.277 , pp. 291-323
    • Blinks, J.R.1    Rüdel, R.2    Taylor, S.R.3
  • 6
    • 0027509324 scopus 로고
    • Subsarcomeric distribution of calcium in demembranated fibers of rabbit psoas muscle
    • Cantino, M. E., T. S. C. Allen, and A. M. Gordon. 1993. Subsarcomeric distribution of calcium in demembranated fibers of rabbit psoas muscle. Biophys. J. 64:211-222.
    • (1993) Biophys. J. , vol.64 , pp. 211-222
    • Cantino, M.E.1    Allen, T.S.C.2    Gordon, A.M.3
  • 7
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia, C., and J. Janin. 1975. Principles of protein-protein recognition. Nature. 256:705-708.
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 9
    • 0020425131 scopus 로고
    • Orientation of spin labels attached to cross-bridges in contracting muscle fibres
    • Cooke, R., M. S. Crowder, and D. D. Thomas. 1982. Orientation of spin labels attached to cross-bridges in contracting muscle fibres. Nature. 300:776-778.
    • (1982) Nature , vol.300 , pp. 776-778
    • Cooke, R.1    Crowder, M.S.2    Thomas, D.D.3
  • 10
    • 0022405269 scopus 로고
    • The effects of ADP and phosphate on the contraction of muscle fibers
    • Cooke, R., and E. Pate. 1985. The effects of ADP and phosphate on the contraction of muscle fibers. Biophys. J. 48:789-798.
    • (1985) Biophys. J. , vol.48 , pp. 789-798
    • Cooke, R.1    Pate, E.2
  • 11
    • 0028212943 scopus 로고
    • Force-velocity relation for frog muscle fibres: Effects of moderate fatigue and of intracellular acidification
    • Curtin, N. A., and K. A. P. Edman. 1994. Force-velocity relation for frog muscle fibres: effects of moderate fatigue and of intracellular acidification. J. Physiol. 475:483-494.
    • (1994) J. Physiol. , vol.475 , pp. 483-494
    • Curtin, N.A.1    Edman, K.A.P.2
  • 12
    • 0018333803 scopus 로고
    • The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres
    • Edman, K. A. P. 1979. The velocity of unloaded shortening and its relation to sarcomere length and isometric force in vertebrate muscle fibres. J. Physiol. 291:143-159.
    • (1979) J. Physiol. , vol.291 , pp. 143-159
    • Edman, K.A.P.1
  • 13
    • 0025150667 scopus 로고
    • Myosin heads have a broad orientational distribution during isometric muscle contraction: Time-resolved EPR studies using caged ATP
    • Fajer, P. G., E. A. Fajer, and D. D. Thomas. 1990. Myosin heads have a broad orientational distribution during isometric muscle contraction: time-resolved EPR studies using caged ATP. Proc. Natl. Acad. Sci. USA. 87:5538-5542.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5538-5542
    • Fajer, P.G.1    Fajer, E.A.2    Thomas, D.D.3
  • 15
    • 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
  • 16
    • 0017508185 scopus 로고
    • Active and rigor muscle stiffness
    • Goldman, Y. E., and R. M. Simmons. 1977. Active and rigor muscle stiffness. J. Physiol. 269:55P-57P.
    • (1977) J. Physiol. , vol.269 , pp. 55-57
    • Goldman, Y.E.1    Simmons, R.M.2
  • 17
    • 0036214903 scopus 로고    scopus 로고
    • A model of cross-bridge attachment to actin in the A.M.ATP state based on X-ray diffraction from permeabilized rabbit psoas muscle
    • Gu, J., S. Xu, and L. C. Yu. 2002. A model of cross-bridge attachment to actin in the A.M.ATP state based on X-ray diffraction from permeabilized rabbit psoas muscle. Biophys. J. 82:2123-2133.
    • (2002) Biophys. J. , vol.82 , pp. 2123-2133
    • Gu, J.1    Xu, S.2    Yu, L.C.3
  • 18
    • 0016610095 scopus 로고
    • X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle
    • Haselgrove, J. C. 1975. X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle. J. Mol. Biol. 92:113-143.
    • (1975) J. Mol. Biol. , vol.92 , pp. 113-143
    • Haselgrove, J.C.1
  • 19
    • 0015801643 scopus 로고
    • X-ray evidence for radial crossbridge movement and for the sliding filament model in actively contracting skeletal muscle
    • Haselgrove, J. C., and H. E. Huxley. 1973. X-ray evidence for radial crossbridge movement and for the sliding filament model in actively contracting skeletal muscle. J. Mol. Biol. 77:549-568.
    • (1973) J. Mol. Biol. , vol.77 , pp. 549-568
    • Haselgrove, J.C.1    Huxley, H.E.2
  • 20
    • 0030969083 scopus 로고    scopus 로고
    • ATPase kinetics on activation of rabbit and frog permeabilized isometric muscle fibres: A real time phosphate assay
    • He, Z.-H., R. K. Chillingworth, M. Brune, J. E. T. Corrie, D. R. Trentham, M. R. Webb, and M. A. Ferenczi. 1997. ATPase kinetics on activation of rabbit and frog permeabilized isometric muscle fibres: a real time phosphate assay. J. Physiol. 501:125-148.
    • (1997) J. Physiol. , vol.501 , pp. 125-148
    • He, Z.-H.1    Chillingworth, R.K.2    Brune, M.3    Corrie, J.E.T.4    Trentham, D.R.5    Webb, M.R.6    Ferenczi, M.A.7
  • 21
    • 0000682154 scopus 로고
    • The heat of shortening and the dynamic constants of muscle
    • Hill, A. V. 1938. The heat of shortening and the dynamic constants of muscle. Proc. R. Soc. Lond. B Biol. Sci. 126:136-195.
    • (1938) Proc. R. Soc. Lond. B Biol. Sci. , vol.126 , pp. 136-195
    • Hill, A.V.1
  • 23
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • Huxley, H. E. 1969. The mechanism of muscular contraction. Science. 164:1356-1365.
    • (1969) Science , vol.164 , pp. 1356-1365
    • Huxley, H.E.1
  • 24
    • 0011992718 scopus 로고
    • The movement of myosin cross-bridges during contraction
    • S. Ebashi, K. Maruyama, and M. Endo, editors. Japan Science Society Press, Tokyo
    • Huxley, H. E. 1980. The movement of myosin cross-bridges during contraction. In Muscle Contraction: Its Regulatory Mechanisms. S. Ebashi, K. Maruyama, and M. Endo, editors. Japan Science Society Press, Tokyo. 33-43.
    • (1980) Muscle Contraction: Its Regulatory Mechanisms , pp. 33-43
    • Huxley, H.E.1
  • 25
    • 85010249552 scopus 로고
    • The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor
    • Huxley, H. E., and W. Brown. 1967. The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. Mol. Biol. 30:383-434.
    • (1967) J. Mol. Biol. , vol.30 , pp. 383-434
    • Huxley, H.E.1    Brown, W.2
  • 26
    • 0021794822 scopus 로고
    • Crossbridge behaviour during muscle contraction
    • Huxley, H. E., and M. Kress. 1985. Crossbridge behaviour during muscle contraction. J. Muscle Res. Cell Motil. 6:153-161.
    • (1985) J. Muscle Res. Cell Motil. , vol.6 , pp. 153-161
    • Huxley, H.E.1    Kress, M.2
  • 29
    • 0028876663 scopus 로고
    • Effect of stretch and release on equatorial X-ray diffraction during a twitch contraction of frog skeletal muscle
    • Iwamoto, H., T. Kobayashi, Y. Amemiya, and K. Wakabayashi. 1995. Effect of stretch and release on equatorial X-ray diffraction during a twitch contraction of frog skeletal muscle. Biophys. J. 68:227-234.
    • (1995) Biophys. J. , vol.68 , pp. 227-234
    • Iwamoto, H.1    Kobayashi, T.2    Amemiya, Y.3    Wakabayashi, K.4
  • 30
    • 0035951287 scopus 로고    scopus 로고
    • X-ray diffraction evidence for the lack of stereospecific protein interactions in highly activated actomyosin complex
    • Iwamoto, H., K. Oiwa, T. Suzuki, and T. Fujisawa. 2001. X-ray diffraction evidence for the lack of stereospecific protein interactions in highly activated actomyosin complex. J. Mol. Biol. 305:863-874.
    • (2001) J. Mol. Biol. , vol.305 , pp. 863-874
    • Iwamoto, H.1    Oiwa, K.2    Suzuki, T.3    Fujisawa, T.4
  • 31
    • 0036293422 scopus 로고    scopus 로고
    • States of thin filament regulatory proteins as revealed by combined cross-linking/X-ray diffraction techniques
    • Iwamoto, H., K. Oiwa, T. Suzuki, and T. Fujisawa. 2002. States of thin filament regulatory proteins as revealed by combined cross-linking/X-ray diffraction techniques. J. Mol. Biol. 317:707-720.
    • (2002) J. Mol. Biol. , vol.317 , pp. 707-720
    • Iwamoto, H.1    Oiwa, K.2    Suzuki, T.3    Fujisawa, T.4
  • 32
    • 0034058866 scopus 로고    scopus 로고
    • Time-resolved two-dimensional X-ray diffraction study of the effect of shortening on activation of contracting skeletal muscle
    • Iwamoto, H., T. Suzuki, and T. Fujisawa. 2000. Time-resolved two-dimensional X-ray diffraction study of the effect of shortening on activation of contracting skeletal muscle. Pflügers Arch. Eur. J. Physiol. 439:646-649.
    • (2000) Pflügers Arch. Eur. J. Physiol. , vol.439 , pp. 646-649
    • Iwamoto, H.1    Suzuki, T.2    Fujisawa, T.3
  • 33
    • 0141662405 scopus 로고    scopus 로고
    • X-ray evidence for structural changes of thin filament induced by cycling myosin heads
    • Iwamoto, H., J. Wakayama, T. Tamura, T. Fujisawa, and N. Yagi. 2003. X-ray evidence for structural changes of thin filament induced by cycling myosin heads. Biophys. J. 84:248a.
    • (2003) Biophys. J. , vol.84
    • Iwamoto, H.1    Wakayama, J.2    Tamura, T.3    Fujisawa, T.4    Yagi, N.5
  • 35
    • 0024286070 scopus 로고
    • Orientation of actin monomer in the F-actin filament: Radial coordinate of glutamine-41 and effect of myosin subfragment 1 binding on the monomer orientation
    • Kasprzak, A. A., R. Takashi, and M. F. Morales. 1988. Orientation of actin monomer in the F-actin filament: radial coordinate of glutamine-41 and effect of myosin subfragment 1 binding on the monomer orientation. Biochemistry. 27:4512-4522.
    • (1988) Biochemistry , vol.27 , pp. 4512-4522
    • Kasprzak, A.A.1    Takashi, R.2    Morales, M.F.3
  • 36
    • 0027163347 scopus 로고
    • Cross-bridge scheme and force per crossbridge state in skinned rabbit psoas muscle fibers
    • Kawai, M., and Y. Zhao. 1993. Cross-bridge scheme and force per crossbridge state in skinned rabbit psoas muscle fibers. Biophys. J. 65:638-651.
    • (1993) Biophys. J. , vol.65 , pp. 638-651
    • Kawai, M.1    Zhao, Y.2
  • 37
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-Pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin promoter both on polymerization and on binding of heavy meromyosin
    • Kouyama, T., and K. Mihashi. 1981. Fluorimetry study of N-(1-Pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin promoter both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114:33-38.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 38
    • 0036224804 scopus 로고    scopus 로고
    • Structural features of cross-bridges in isometrically contracting skeletal muscle
    • Kraft, T., T. Mattei, A. Radocaj, B. Piep. C. Nocula, M. Furch and B. Brenner. 2002. Structural features of cross-bridges in isometrically contracting skeletal muscle. Biophys. J. 82:2536-2547.
    • (2002) Biophys. J. , vol.82 , pp. 2536-2547
    • Kraft, T.1    Mattei, T.2    Radocaj, A.3    Piep, B.4    Nocula, C.5    Furch, M.6    Brenner, B.7
  • 39
    • 0032984795 scopus 로고    scopus 로고
    • The effect of thin filament activation on the attachment of weak binding cross-bridges: A two-dimensional X-ray diffraction study on single muscle fibers
    • Kraft, T., S. Xu, B. Brenner, and L. C. Yu. 1999. The effect of thin filament activation on the attachment of weak binding cross-bridges: a two-dimensional X-ray diffraction study on single muscle fibers. Biophys. J. 76:1494-1513.
    • (1999) Biophys. J. , vol.76 , pp. 1494-1513
    • Kraft, T.1    Xu, S.2    Brenner, B.3    Yu, L.C.4
  • 40
    • 0023042009 scopus 로고
    • Structural changes during activation of frog muscle by time-resolved X-ray diffraction
    • Kress, M., H. E. Huxley, A. R. Faruqi, and J. Hendrix. 1986. Structural changes during activation of frog muscle 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    Faruqi, A.R.3    Hendrix, J.4
  • 41
    • 0026732710 scopus 로고
    • Mammalian skeletal muscle fibers distinguished by contents of phosphocreatine, ATP, and Pi
    • Kushmerick, M. J., T. S. Moerland, and R. W. Wiseman. 1992. Mammalian skeletal muscle fibers distinguished by contents of phosphocreatine, ATP, and Pi. Proc. Natl. Acad. Sci. USA. 89:7521-7525.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7521-7525
    • Kushmerick, M.J.1    Moerland, T.S.2    Wiseman, R.W.3
  • 42
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., D. Popp, and K. C. Holmes. 1993. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 43
    • 0023782821 scopus 로고
    • Cause of changes in the thin filament-associated reflexions on activation of frog muscle-myosin binding or conformational change of actin
    • Maeda, Y., D. Popp, and S. M. McLaughlin. 1988. Cause of changes in the thin filament-associated reflexions on activation of frog muscle - myosin binding or conformational change of actin. Adv. Exp. Med. Biol. 226:381-390.
    • (1988) Adv. Exp. Med. Biol. , vol.226 , pp. 381-390
    • Maeda, Y.1    Popp, D.2    McLaughlin, S.M.3
  • 44
    • 0016862443 scopus 로고
    • Use of an X-ray television for diffraction of the frog striated muscle
    • Matsubara, I., N. Yagi, and H. Hashizume. 1975. Use of an X-ray television for diffraction of the frog striated muscle. Nature. 255:728-729.
    • (1975) Nature , vol.255 , pp. 728-729
    • Matsubara, I.1    Yagi, N.2    Hashizume, H.3
  • 45
    • 0021773118 scopus 로고
    • Intensification of the 5.9-nm actin layer line in contracting muscle
    • Matsubara, I., N. Yagi, H. Miura, M. Ozeki, and T. Izumi. 1984. Intensification of the 5.9-nm actin layer line in contracting muscle. Nature. 312:471-473.
    • (1984) Nature , vol.312 , pp. 471-473
    • Matsubara, I.1    Yagi, N.2    Miura, H.3    Ozeki, M.4    Izumi, T.5
  • 46
    • 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
  • 47
    • 0028024932 scopus 로고
    • Domain motion in actin observed by fluorescence resonance energy transfer
    • Miki M., and T. Kouyama. 1994. Domain motion in actin observed by fluorescence resonance energy transfer. Biochemistry. 33:10171-10177.
    • (1994) Biochemistry , vol.33 , pp. 10171-10177
    • Miki, M.1    Kouyama, T.2
  • 48
    • 0020364082 scopus 로고
    • Fluorescence anisotropy of labeled F-actin: Influence of divalent cations on the interaction between F-actin and myosin heads
    • Miki, M., P. Wahl, and J.-C. Auchet. 1982. Fluorescence anisotropy of labeled F-actin: influence of divalent cations on the interaction between F-actin and myosin heads. Biochemistry. 21:3661-3665.
    • (1982) Biochemistry , vol.21 , pp. 3661-3665
    • Miki, M.1    Wahl, P.2    Auchet, J.-C.3
  • 49
    • 0030988670 scopus 로고    scopus 로고
    • A conformational change in F-actin when myosin binds: Fluorescence resonance energy transfer detects an increase in the radial coordinate of Cys-374
    • Moens, P. D. J., and C. G. dos Remedios. 1997. A conformational change in F-actin when myosin binds: fluorescence resonance energy transfer detects an increase in the radial coordinate of Cys-374. Biochemistry. 36:7353-7360.
    • (1997) Biochemistry , vol.36 , pp. 7353-7360
    • Moens, P.D.J.1    Dos Remedios, C.G.2
  • 51
    • 0028907435 scopus 로고
    • Structural dynamics of F-actin: I. Changes in the C terminus
    • Orlova, A., and E. H. Egelman. 1995. Structural dynamics of F-actin: I. Changes in the C terminus. J. Mol. Biol. 245:582-597.
    • (1995) J. Mol. Biol. , vol.245 , pp. 582-597
    • Orlova, A.1    Egelman, E.H.2
  • 52
    • 0031556946 scopus 로고    scopus 로고
    • Cooperative rigor binding of myosin to actin is a function of F-actin structure
    • Orlova, A., and E. H. Egelman. 1997. Cooperative rigor binding of myosin to actin is a function of F-actin structure. J. Mol. Biol. 265:469-474.
    • (1997) J. Mol. Biol. , vol.265 , pp. 469-474
    • Orlova, A.1    Egelman, E.H.2
  • 53
    • 0015935349 scopus 로고
    • Structural 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. Structural 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
  • 54
    • 0014412965 scopus 로고
    • Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 Å resolution: The atomic model
    • Perutz, M. F., H. Muirhead, J. M. Cox, and L. C. G. Goaman. 1968. Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 Å resolution: the atomic model. Nature. 219:131-139.
    • (1968) Nature , vol.219 , pp. 131-139
    • Perutz, M.F.1    Muirhead, H.2    Cox, J.M.3    Goaman, L.C.G.4
  • 58
    • 0029840598 scopus 로고    scopus 로고
    • Calcium alone does not fully activate the thin fiament for S1 binding to rigor myofibrils
    • Swartz, D. R., R. L. Moss, and M. L. Greaser. 1996. Calcium alone does not fully activate the thin fiament for S1 binding to rigor myofibrils. Biophys. J. 71:1891-1904.
    • (1996) Biophys. J. , vol.71 , pp. 1891-1904
    • Swartz, D.R.1    Moss, R.L.2    Greaser, M.L.3
  • 59
    • 0017413273 scopus 로고
    • Electron microscopic investigation of the flexibility of F-actin
    • Takebayashi, T., Y. Morita, and F. Oosawa. 1977. Electron microscopic investigation of the flexibility of F-actin. Biochim. Biophys. Acta. 492:357-363.
    • (1977) Biochim. Biophys. Acta , vol.492 , pp. 357-363
    • Takebayashi, T.1    Morita, Y.2    Oosawa, F.3
  • 60
    • 0032999729 scopus 로고    scopus 로고
    • Backward movements of cross-bridges by application of stretch and by binding of MgADP to skeletal muscle fibers in the rigor state as studies by X-ray diffraction
    • Takezawa, Y., D.-S. Kim, M. Ogino, Y. Sugimoto, T. Kobayashi, T. Arata, and K. Wakabayashi. 1999. Backward movements of cross-bridges by application of stretch and by binding of MgADP to skeletal muscle fibers in the rigor state as studies by X-ray diffraction. Biophys. J. 76:1770-1783.
    • (1999) Biophys. J. , vol.76 , pp. 1770-1783
    • Takezawa, Y.1    Kim, D.-S.2    Ogino, M.3    Sugimoto, Y.4    Kobayashi, T.5    Arata, T.6    Wakabayashi, K.7
  • 61
    • 0034623058 scopus 로고    scopus 로고
    • A new model of cooperative myosin-thin filament binding
    • Tobacman, L. S., and C. A. Butters. 2000. A new model of cooperative myosin-thin filament binding. J. Biol. Chem. 275:27587-27593.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27587-27593
    • Tobacman, L.S.1    Butters, C.A.2
  • 62
    • 0036001362 scopus 로고    scopus 로고
    • Diffraction by partially occupied helices
    • Tsaturyan, A. K. 2002. Diffraction by partially occupied helices. Acta Crystallogr. A58:292-294.
    • (2002) Acta Crystallogr. A , vol.58 , pp. 292-294
    • Tsaturyan, A.K.1
  • 63
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • Vibert, P., R. Craig, and W. Lehman. 1997. Steric-model for activation of muscle thin filaments. J. Mol. Biol. 266:8-14.
    • (1997) J. Mol. Biol. , vol.266 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 65
    • 0023762517 scopus 로고
    • Intensity changes of actin-based layer lines from frog skeletal muscles during an isometric contraction
    • Wakabayashi, K., Y. Ueno, Y. Amemiya, and H. Tanaka. 1988b. Intensity changes of actin-based layer lines from frog skeletal muscles during an isometric contraction. Adv. Exp. Med. Biol. 226:353-367.
    • (1988) Adv. Exp. Med. Biol. , vol.226 , pp. 353-367
    • Wakabayashi, K.1    Ueno, Y.2    Amemiya, Y.3    Tanaka, H.4
  • 66
    • 0021867708 scopus 로고
    • Time-resolved X-ray diffraction studies on the intensity changes of the 5.9 and 5.1 nm actin layer lines from frog skeletal muscle during an isometric tetanus using synchrotron radiation
    • Wakabayashi, K., H. Tanaka, Y. Amemiya, A. Fujishima, T. Kobayashi, T. Hamanaka, H. Sugi, and T. Mitsui. 1985. Time-resolved X-ray diffraction studies on the intensity changes of the 5.9 and 5.1 nm actin layer lines from frog skeletal muscle during an isometric tetanus using synchrotron radiation. Biophys. J. 47:847-850.
    • (1985) Biophys. J. , vol.47 , pp. 847-850
    • Wakabayashi, K.1    Tanaka, H.2    Amemiya, Y.3    Fujishima, A.4    Kobayashi, T.5    Hamanaka, T.6    Sugi, H.7    Mitsui, T.8
  • 67
    • 0001891718 scopus 로고
    • Structure of relaxed myosin filaments in relation to nucleotide state in vertebrate skeletal muscle
    • Wray, J. S. 1987. Structure of relaxed myosin filaments in relation to nucleotide state in vertebrate skeletal muscle. J. Muscle Res. Cell Motil. 8:62a.
    • (1987) J. Muscle Res. Cell Motil. , vol.8
    • Wray, J.S.1
  • 68
    • 0026780695 scopus 로고
    • Effects of N-ethylmaleimide on the structure of skinned frog skeletal muscles
    • Yagi, N. 1992. Effects of N-ethylmaleimide on the structure of skinned frog skeletal muscles. J. Muscle Res. Cell Motil. 13:457-463.
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 457-463
    • Yagi, N.1
  • 69
    • 0030485290 scopus 로고    scopus 로고
    • Labelling of thin filaments by myosin heads in contracting and rigor vertebrate skeletal muscles
    • Yagi, N. 1996. Labelling of thin filaments by myosin heads in contracting and rigor vertebrate skeletal muscles. Acta Crystallogr. D52:1169-1173.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 1169-1173
    • Yagi, N.1
  • 70
    • 0017773079 scopus 로고
    • Return of myosin heads to thick filaments after muscle contraction
    • Yagi, N., M. H. Ito, H. Nakajima, T. Izumi, and I. Matsubara. 1977. Return of myosin heads to thick filaments after muscle contraction. Science. 197:685-687.
    • (1977) Science , vol.197 , pp. 685-687
    • Yagi, N.1    Ito, M.H.2    Nakajima, H.3    Izumi, T.4    Matsubara, I.5
  • 71
    • 0023683604 scopus 로고
    • Changes in the 5.9 nm actin layer-line on activation of frog skeletal muscles
    • Yagi, N., and I. Matsubara. 1988. Changes in the 5.9 nm actin layer-line on activation of frog skeletal muscles. Adv. Exp. Med. Biol. 226:369-380.
    • (1988) Adv. Exp. Med. Biol. , vol.226 , pp. 369-380
    • Yagi, N.1    Matsubara, I.2
  • 72
    • 0024974910 scopus 로고
    • Structural changes in the thin filament during activation studied by X-ray diffraction of highly stretched skeletal muscle
    • Yagi, N., and I. Matsubara. 1989. Structural changes in the thin filament during activation studied by X-ray diffraction of highly stretched skeletal muscle. J. Mol. Biol. 208:359-363.
    • (1989) J. Mol. Biol. , vol.208 , pp. 359-363
    • Yagi, N.1    Matsubara, I.2
  • 73
    • 0027220889 scopus 로고
    • An X-ray diffraction study of frog skeletal muscle during shortening near the maximum velocity
    • Yagi, N., S. Takemori, and M. Watanabe. 1993. An X-ray diffraction study of frog skeletal muscle during shortening near the maximum velocity. J. Mol. Biol. 231:668-677.
    • (1993) J. Mol. Biol. , vol.231 , pp. 668-677
    • Yagi, N.1    Takemori, S.2    Watanabe, M.3
  • 74
    • 0032472434 scopus 로고    scopus 로고
    • 1H-nuclear magnetic resonance evidence for actomyosin-dependent structural changes of the intracellular water of frog skeletal muscle fiber
    • 1H-nuclear magnetic resonance evidence for actomyosin-dependent structural changes of the intracellular water of frog skeletal muscle fiber. Biochim. Biophys. Acta. 1379:224-232.
    • (1998) Biochim. Biophys. Acta , vol.1379 , pp. 224-232
    • Yamada, T.1
  • 75
    • 0018196447 scopus 로고
    • Polarized fluorescence from ε-ADP incorporated into F-actin in a myosin-free single fiber: Conformation of F-actin and changes induced in it by heavy meromyosin
    • Yanagida, T., and F. Oosawa. 1978. Polarized fluorescence from ε-ADP incorporated into F-actin in a myosin-free single fiber: conformation of F-actin and changes induced in it by heavy meromyosin. J. Mol. Biol. 126:507-524.
    • (1978) J. Mol. Biol. , vol.126 , pp. 507-524
    • Yanagida, T.1    Oosawa, F.2
  • 76
    • 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
  • 77
    • 0022419480 scopus 로고
    • X-ray diffraction study of fast and slow mammalian skeletal muscle in the live relaxed state
    • Zappe, H. A., and Y. Maeda. 1985. X-ray diffraction study of fast and slow mammalian skeletal muscle in the live relaxed state. J. Mol. Biol. 185:211-214.
    • (1985) J. Mol. Biol. , vol.185 , pp. 211-214
    • Zappe, H.A.1    Maeda, Y.2
  • 78
    • 0027933737 scopus 로고
    • Kinetic and thermodynamic studies of the cross-bridge cycle in rabbit psoas muscle fibers
    • Zhao, Y., and M. Kawai. 1994. Kinetic and thermodynamic studies of the cross-bridge cycle in rabbit psoas muscle fibers. Biophys. J. 67:1655-1668.
    • (1994) Biophys. J. , vol.67 , pp. 1655-1668
    • Zhao, Y.1    Kawai, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.