메뉴 건너뛰기




Volumn 155, Issue 2, 2006, Pages 273-284

A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle X-ray fibre diagrams from non-overlap muscle

Author keywords

Actin; Calcium activation; Crossbridge binding; Myosin crossbridge; Steric blocking; Striated muscle activation; Thin filament structure; Tropomyosin

Indexed keywords

ACTIN; CALCIUM; MYOSIN; TROPOMYOSIN; TROPONIN;

EID: 33747767574     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.02.020     Document Type: Article
Times cited : (148)

References (68)
  • 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., Yagi N., and Squire J.M. Structural changes in actin-tropomyosin during muscle regulation: computer modelling of low-angle X-ray diffraction data. J. Mol. Biol. 252 (1995) 611-632
    • (1995) J. Mol. Biol. , vol.252 , pp. 611-632
    • Al-Khayat, H.A.1    Yagi, N.2    Squire, J.M.3
  • 2
    • 0023187156 scopus 로고
    • Co-operative interactions between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle
    • Brandt P.W., Diamond M.S., Rutchik J., and Schachat F.H. Co-operative interactions between troponin-tropomyosin units extend the length of the thin filament in skeletal muscle. J. Mol. Biol. 195 (1987) 885-896
    • (1987) J. Mol. Biol. , vol.195 , pp. 885-896
    • Brandt, P.W.1    Diamond, M.S.2    Rutchik, J.3    Schachat, F.H.4
  • 6
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman E.H., Francis N., and DeRosier D.J. F-actin is a helix with a random variable twist. Nature 298 (1982) 131-135
    • (1982) Nature , vol.298 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.J.3
  • 7
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15 (1997) 132-134
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 8
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D55 (1999) 938-940
    • (1999) Acta Crystallogr. , vol.D55 , pp. 938-940
    • Esnouf, R.M.1
  • 9
    • 26844566272 scopus 로고    scopus 로고
    • The molecular mechanism of muscle contraction
    • Geeves M.A., and Holmes K.C. The molecular mechanism of muscle contraction. Adv. Protein Chem. 71 (2005) 161-193
    • (2005) Adv. Protein Chem. , vol.71 , pp. 161-193
    • Geeves, M.A.1    Holmes, K.C.2
  • 10
    • 0036193163 scopus 로고    scopus 로고
    • Modeling thin filament cooperativity
    • Geeves M.A., and Lehrer S.S. Modeling thin filament cooperativity. Biophys. J. 82 (2002) 1677-1681
    • (2002) Biophys. J. , vol.82 , pp. 1677-1681
    • Geeves, M.A.1    Lehrer, S.S.2
  • 11
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction of striated muscle
    • Gordon A.M., Homsher E., and Regnier M. Regulation of contraction of striated muscle. Physiol. Rev. 80 (2000) 853-924
    • (2000) Physiol. Rev. , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 12
    • 0015218120 scopus 로고
    • Reconstitution of troponin activity from three protein components
    • Greaser M.L., and Gergely J. Reconstitution of troponin activity from three protein components. J. Biol. Chem. 246 (1971) 4226-4233
    • (1971) J. Biol. Chem. , vol.246 , pp. 4226-4233
    • Greaser, M.L.1    Gergely, J.2
  • 13
    • 0015935352 scopus 로고
    • Purification and properties of the components of troponin
    • Greaser M.L., and Gergely J. Purification and properties of the components of troponin. J. Biol. Chem. 248 (1973) 2125-2133
    • (1973) J. Biol. Chem. , vol.248 , pp. 2125-2133
    • Greaser, M.L.1    Gergely, J.2
  • 14
    • 0019013686 scopus 로고
    • Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex
    • Greene L.E., and Eisenberg E. Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex. Proc. Natl. Acad. Sci. USA 77 (1980) 2616-2620
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2616-2620
    • Greene, L.E.1    Eisenberg, E.2
  • 15
    • 85010916780 scopus 로고
    • The structure of f-actin and the actin filaments isolated from muscle
    • Hanson J., and Lowy J. The structure of f-actin and the actin filaments isolated from muscle. J. Mol. Biol. 6 (1963) 46-60
    • (1963) J. Mol. Biol. , vol.6 , pp. 46-60
    • Hanson, J.1    Lowy, J.2
  • 16
    • 78651151948 scopus 로고
    • The structure of actin filaments and the origin of the axial periodicity in the I-substance of vertebrate striated muscle
    • Hanson J., and Lowy J. The structure of actin filaments and the origin of the axial periodicity in the I-substance of vertebrate striated muscle. Proc. Royal Soc. Lond. B 160 (1964) 449-460
    • (1964) Proc. Royal Soc. Lond. B , vol.160 , pp. 449-460
    • Hanson, J.1    Lowy, J.2
  • 17
    • 0000733783 scopus 로고
    • X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle
    • Haselgrove J.C. X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle. Cold Spring Habor Symp. Quant. Biol. 37 (1972) 341-352
    • (1972) Cold Spring Habor Symp. Quant. Biol. , vol.37 , pp. 341-352
    • Haselgrove, J.C.1
  • 18
    • 0026672241 scopus 로고
    • Analysis of troponin-tropomyosin binding to actin. Troponin does not promote interactions between tropomyosin molecules
    • Hill L.E., Mehegan J.P., Butters C.A., and Tobacman L.S. Analysis of troponin-tropomyosin binding to actin. Troponin does not promote interactions between tropomyosin molecules. J. Biol. Chem. 267 (1992) 16106-16113
    • (1992) J. Biol. Chem. , vol.267 , pp. 16106-16113
    • Hill, L.E.1    Mehegan, J.P.2    Butters, C.A.3    Tobacman, L.S.4
  • 19
    • 0015899936 scopus 로고
    • Calcium sensitive binding of troponin to actin-tropomyosin: a two-site model for troponin action
    • Hitchcock S.E., Huxley H.E., and Szent-Gyorgyi A.G. Calcium sensitive binding of troponin to actin-tropomyosin: a two-site model for troponin action. J. Mol. Biol. 80 (1973) 825-836
    • (1973) J. Mol. Biol. , vol.80 , pp. 825-836
    • Hitchcock, S.E.1    Huxley, H.E.2    Szent-Gyorgyi, A.G.3
  • 20
    • 0141843643 scopus 로고    scopus 로고
    • Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide
    • Holmes K.C., Angert I., Kull F.J., Jahn W., and Schroder R.R. Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide. Nature 425 (2003) 423-427
    • (2003) Nature , vol.425 , pp. 423-427
    • Holmes, K.C.1    Angert, I.2    Kull, F.J.3    Jahn, W.4    Schroder, R.R.5
  • 21
    • 0010693355 scopus 로고
    • The effect of disorientation on the intensity distribution of non-crystalline fibres. 1. Theory
    • Holmes K.C., and Barrington Leigh J. The effect of disorientation on the intensity distribution of non-crystalline fibres. 1. Theory. Acta Crystallogr. A30 (1974) 635-638
    • (1974) Acta Crystallogr. , vol.A30 , pp. 635-638
    • Holmes, K.C.1    Barrington Leigh, J.2
  • 23
    • 0000244537 scopus 로고
    • Structural changes in actin and myosin-containing filaments during contraction
    • Huxley H.E. Structural changes in actin and myosin-containing filaments during contraction. Cold Spring Habor Symp. Quant. Biol. 37 (1972) 361-376
    • (1972) Cold Spring Habor Symp. Quant. Biol. , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of proteins structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of proteins structures. J. Appl. Crystallogr. 24 (1991) 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 26
    • 0028179144 scopus 로고
    • Ca(2+)-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
    • Lehman W., Craig R., and Vibert P. Ca(2+)-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature 368 (1994) 65-67
    • (1994) Nature , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 27
    • 0035970288 scopus 로고    scopus 로고
    • Troponin organization on relaxed and activated thin filaments revealed by electron microscopy and three-dimensional reconstruction
    • Lehman W., Rosol M., Tobacman L.S., and Craig R. Troponin organization on relaxed and activated thin filaments revealed by electron microscopy and three-dimensional reconstruction. J. Mol. Biol. 307 (2001) 739-744
    • (2001) J. Mol. Biol. , vol.307 , pp. 739-744
    • Lehman, W.1    Rosol, M.2    Tobacman, L.S.3    Craig, R.4
  • 28
    • 0029131118 scopus 로고
    • Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments
    • Lehman W., Vibert P., Uman P., and Craig R. Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments. J. Mol. Biol. 251 (1995) 191-196
    • (1995) J. Mol. Biol. , vol.251 , pp. 191-196
    • Lehman, W.1    Vibert, P.2    Uman, P.3    Craig, R.4
  • 29
    • 0020490904 scopus 로고
    • Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase
    • Lehrer S.S., and Morris E.P. Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase. J. Biol. Chem. 257 (1982) 8073-8080
    • (1982) J. Biol. Chem. , vol.257 , pp. 8073-8080
    • Lehrer, S.S.1    Morris, E.P.2
  • 30
    • 0028940312 scopus 로고
    • An atomic model of the unregulated thin filament obtained by X-ray fibre diffraction on oriented actin-tropomyosin gels
    • Lorenz M., Poole K.J., Popp D., Rosenbaum G., and Holmes K.C. An atomic model of the unregulated thin filament obtained by X-ray fibre diffraction on oriented actin-tropomyosin gels. J. Mol. Biol. 246 (1995) 108-119
    • (1995) J. Mol. Biol. , vol.246 , pp. 108-119
    • Lorenz, M.1    Poole, K.J.2    Popp, D.3    Rosenbaum, G.4    Holmes, K.C.5
  • 31
    • 0027131941 scopus 로고
    • Refinement of the f-actin model against X-ray fibre diffraction data by the use of a directed mutation algorithm
    • Lorenz M., Popp D., and Holmes K.C. Refinement of the f-actin model against X-ray fibre diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234 (1993) 826-836
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 32
    • 0026043263 scopus 로고
    • X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles
    • Lowy J., Popp D., and Stewart A.A. X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles. Biophys. J. 60 (1991) 812-824
    • (1991) Biophys. J. , vol.60 , pp. 812-824
    • Lowy, J.1    Popp, D.2    Stewart, A.A.3
  • 33
    • 0025308626 scopus 로고
    • Studies of the diffuse X-ray scattering from contracting frog skeletal muscles
    • Lowy J., and Poulsen F.R. Studies of the diffuse X-ray scattering from contracting frog skeletal muscles. Biophys. J. 57 (1990) 977-985
    • (1990) Biophys. J. , vol.57 , pp. 977-985
    • Lowy, J.1    Poulsen, F.R.2
  • 34
    • 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., Popp D., and McLaughlin S.M. 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 (1988) 381-390
    • (1988) Adv. Exp. Med. Biol. , vol.226 , pp. 381-390
    • Maeda, Y.1    Popp, D.2    McLaughlin, S.M.3
  • 35
    • 0019882706 scopus 로고
    • Non-polymerizable tropomyosin: preparation, some properties and f-actin binding
    • Mak A.S., and Smillie L.B. Non-polymerizable tropomyosin: preparation, some properties and f-actin binding. Biochem. Biophys. Res. Commun. 16 (1981) 208-214
    • (1981) Biochem. Biophys. Res. Commun. , vol.16 , pp. 208-214
    • Mak, A.S.1    Smillie, L.B.2
  • 36
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
    • McKillop D.F., and Geeves M.A. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys. J. 65 (1993) 693-701
    • (1993) Biophys. J. , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 37
    • 0017136639 scopus 로고
    • The 14-fold periodicity in α-tropomyosin and the interaction with actin
    • McLachlan A.D., and Stewart M. The 14-fold periodicity in α-tropomyosin and the interaction with actin. J. Mol. Biol. 103 (1976) 271-298
    • (1976) J. Mol. Biol. , vol.103 , pp. 271-298
    • McLachlan, A.D.1    Stewart, M.2
  • 38
    • 0027251071 scopus 로고
    • Atomic structure of gelsolin segment 1 in complex with actin and the mechanism of filament severing
    • McLaughlan P.J., Gooch J.T., Mannherz H.G., and Weeds A.G. Atomic structure of gelsolin segment 1 in complex with actin and the mechanism of filament severing. Nature 364 (1993) 685-692
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlan, P.J.1    Gooch, J.T.2    Mannherz, H.G.3    Weeds, A.G.4
  • 39
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D Version 2: photorealistic molecular graphics
    • Merritt E.A., and Bacon D.J. Raster3D Version 2: photorealistic molecular graphics. Meth. Enzymol. 277 (1997) 505-524
    • (1997) Meth. Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 40
    • 0023374114 scopus 로고
    • Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy
    • Milligan R.A., and Flicker P.F. Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy. J. Cell Biol. 105 (1987) 29-39
    • (1987) J. Cell Biol. , vol.105 , pp. 29-39
    • Milligan, R.A.1    Flicker, P.F.2
  • 41
    • 0035957530 scopus 로고    scopus 로고
    • Ca(2+)-induced switching of troponin and tropomyosin on actin filaments as revealed by electron cryo-microscopy
    • Narita A., Yasunaga T., Ishikawa T., Mayanagi K., and Wakabayashi T. Ca(2+)-induced switching of troponin and tropomyosin on actin filaments as revealed by electron cryo-microscopy. J. Mol. Biol. 308 (2001) 241-261
    • (2001) J. Mol. Biol. , vol.308 , pp. 241-261
    • Narita, A.1    Yasunaga, T.2    Ishikawa, T.3    Mayanagi, K.4    Wakabayashi, T.5
  • 42
    • 0016652387 scopus 로고
    • Symmetry and molecular arrangement in paracrystals of reconstituted muscle thin filaments
    • O'Brien E.J., Gillis J.M., and Couch J. Symmetry and molecular arrangement in paracrystals of reconstituted muscle thin filaments. J. Mol. Biol. 99 (1975) 461-475
    • (1975) J. Mol. Biol. , vol.99 , pp. 461-475
    • O'Brien, E.J.1    Gillis, J.M.2    Couch, J.3
  • 44
    • 0035197514 scopus 로고    scopus 로고
    • The helical parameters of f-actin precisely determined from X-ray fibre diffraction of well-oriented sols
    • Oda T., Makino K., Yamashita I., Namba K., and Maeda Y. The helical parameters of f-actin precisely determined from X-ray fibre diffraction of well-oriented sols. Results Probl. Cell Differ. 32 (2001) 43-58
    • (2001) Results Probl. Cell Differ. , vol.32 , pp. 43-58
    • Oda, T.1    Makino, K.2    Yamashita, I.3    Namba, K.4    Maeda, Y.5
  • 45
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein L.R., Graceffa P., and Dominguez R. The crystal structure of uncomplexed actin in the ADP state. Science 293 (2001) 708-711
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 46
    • 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., and Squire J.M. Structural role of tropomyosin in muscle regulation: analysis of the X-ray diffraction patterns from relaxed and contracting muscles. J. Mol. Biol. 75 (1973) 33-55
    • (1973) J. Mol. Biol. , vol.75 , pp. 33-55
    • Parry, D.A.1    Squire, J.M.2
  • 47
    • 0015944672 scopus 로고
    • Structural studies on the tropomyosin-troponin complex of vertebrate skeletal muscle
    • Parry D.A.D. Structural studies on the tropomyosin-troponin complex of vertebrate skeletal muscle. Biochem. Biophys. Res. Commun. 57 (1974) 216-224
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 216-224
    • Parry, D.A.D.1
  • 48
    • 0016777712 scopus 로고
    • Analysis of the primary sequence of alpha-tropomyosin from rabbit skeletal muscle
    • Parry D.A.D. Analysis of the primary sequence of alpha-tropomyosin from rabbit skeletal muscle. J. Mol. Biol. 98 (1975) 519-535
    • (1975) J. Mol. Biol. , vol.98 , pp. 519-535
    • Parry, D.A.D.1
  • 49
    • 0016860910 scopus 로고
    • Double helix of tropomyosin
    • Parry D.A.D. Double helix of tropomyosin. Nature 256 (1975) 346-347
    • (1975) Nature , vol.256 , pp. 346-347
    • Parry, D.A.D.1
  • 50
    • 0034841005 scopus 로고    scopus 로고
    • Vertebrate tropomyosin: distribution, properties and function
    • Perry S.V. Vertebrate tropomyosin: distribution, properties and function. J. Muscle Res. Cell Motil. 22 (2001) 5-49
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 5-49
    • Perry, S.V.1
  • 52
    • 13844297588 scopus 로고    scopus 로고
    • Single particle analysis of relaxed and activated muscle thin filaments
    • Pirani A., Xu C., Hatch V., Craig R., Tobacman L.S., and Lehman W. Single particle analysis of relaxed and activated muscle thin filaments. J. Mol. Biol. 346 (2005) 761-772
    • (2005) J. Mol. Biol. , vol.346 , pp. 761-772
    • Pirani, A.1    Xu, C.2    Hatch, V.3    Craig, R.4    Tobacman, L.S.5    Lehman, W.6
  • 55
    • 0027447838 scopus 로고
    • Calcium ions and the structure of muscle actin filament. An X-ray diffraction study
    • Popp D., and Maeda Y. Calcium ions and the structure of muscle actin filament. An X-ray diffraction study. J. Mol. Biol. 229 (1993) 279-285
    • (1993) J. Mol. Biol. , vol.229 , pp. 279-285
    • Popp, D.1    Maeda, Y.2
  • 56
    • 0016213363 scopus 로고
    • Troponin, tropomyosin, and actin interactions in the Ca2+ regulation of muscle contraction
    • Potter J.D., and Gergely J. Troponin, tropomyosin, and actin interactions in the Ca2+ regulation of muscle contraction. Biochemistry 13 (1974) 2697-2703
    • (1974) Biochemistry , vol.13 , pp. 2697-2703
    • Potter, J.D.1    Gergely, J.2
  • 59
    • 0015530296 scopus 로고
    • Regulation of skeletal muscle contraction. II. Structural studies of the interaction of the tropomyosin-troponin complex with actin
    • Spudich J.A., Huxley H.E., and Finch J. Regulation of skeletal muscle contraction. II. Structural studies of the interaction of the tropomyosin-troponin complex with actin. J. Mol. Biol. 72 (1972) 619-632
    • (1972) J. Mol. Biol. , vol.72 , pp. 619-632
    • Spudich, J.A.1    Huxley, H.E.2    Finch, J.3
  • 60
    • 0031777885 scopus 로고    scopus 로고
    • A new look at thin filament regulation in vertebrate skeletal muscle
    • Squire J.M., and Morris E. A new look at thin filament regulation in vertebrate skeletal muscle. FASEB J. 12 (1998) 761-771
    • (1998) FASEB J. , vol.12 , pp. 761-771
    • Squire, J.M.1    Morris, E.2
  • 61
    • 0028861589 scopus 로고
    • Normal modes as refinement parameters for the f-actin model
    • Tirion M.M., ben-Avraham D., Lorenz M., and Holmes K.C. Normal modes as refinement parameters for the f-actin model. Biophys. J. 68 (1995) 5-12
    • (1995) Biophys. J. , vol.68 , pp. 5-12
    • Tirion, M.M.1    ben-Avraham, D.2    Lorenz, M.3    Holmes, K.C.4
  • 62
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • Tobacman L.S. Thin filament-mediated regulation of cardiac contraction. Annu. Rev. Physiol. 58 (1996) 447-481
    • (1996) Annu. Rev. Physiol. , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 63
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • Vibert P., Craig R., and Lehman W. Steric-model for activation of muscle thin filaments. J. Mol. Biol. 266 (1997) 8-14
    • (1997) J. Mol. Biol. , vol.266 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 65
    • 0027082784 scopus 로고
    • Effects of the amino-terminal regions of tropomyosin and troponin T on thin filament assembly
    • Willadsen K.A., Butters C.A., Hill L.E., and Tobacman L.S. Effects of the amino-terminal regions of tropomyosin and troponin T on thin filament assembly. J. Biol. Chem. 267 (1992) 23746-23752
    • (1992) J. Biol. Chem. , vol.267 , pp. 23746-23752
    • Willadsen, K.A.1    Butters, C.A.2    Hill, L.E.3    Tobacman, L.S.4
  • 66
    • 0023091230 scopus 로고
    • Structure of co-crystals of tropomyosin and troponin
    • White S.P., Cohen C., and Phillips Jr. G.N. Structure of co-crystals of tropomyosin and troponin. Nature 325 (1987) 826-828
    • (1987) Nature , vol.325 , pp. 826-828
    • White, S.P.1    Cohen, C.2    Phillips Jr., G.N.3
  • 67
    • 0033985268 scopus 로고    scopus 로고
    • Crystal structure of tropomyosin at seven Angstroms resolution
    • Whitby F.G., and Phillips G.N. Crystal structure of tropomyosin at seven Angstroms resolution. Proteins 38 (2000) 49-59
    • (2000) Proteins , vol.38 , pp. 49-59
    • Whitby, F.G.1    Phillips, G.N.2
  • 68
    • 0024974910 scopus 로고
    • Structural changes in the thin filament during activation studied by X-ray diffraction of highly stretched skeletal muscle
    • Yagi N., and Matsubara I. Structural changes in the thin filament during activation studied by X-ray diffraction of highly stretched skeletal muscle. J. Mol. Biol. 208 (1989) 359-363
    • (1989) J. Mol. Biol. , vol.208 , pp. 359-363
    • Yagi, N.1    Matsubara, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.