메뉴 건너뛰기




Volumn , Issue , 2009, Pages 1-46

Muscle structure and function

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84893606285     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (11)

References (132)
  • 2
    • 33747811148 scopus 로고    scopus 로고
    • 3D structure of relaxed fish muscle myosin filaments by single particle analysis
    • Al-Khayat, H.A., E.P. Morris, R.W. Kensler, and J.M. Squire. 2006. 3D structure of relaxed fish muscle myosin filaments by single particle analysis. J. Struct. Biol. 155:202-217.
    • (2006) J. Struct. Biol , vol.155 , pp. 202-217
    • Al-Khayat, H.A.1    Morris, E.P.2    Kensler, R.W.3    Squire, J.M.4
  • 5
    • 1842431755 scopus 로고    scopus 로고
    • Calsequestrin and the calcium release channel of skeletal and cardiac muscle
    • Beard, N.A., D.R. Laver, and A.F. Dulhunty. 2004. Calsequestrin and the calcium release channel of skeletal and cardiac muscle. Prog. Biophys. Mol. Biol. 85:33-69.
    • (2004) Prog. Biophys. Mol. Biol , vol.85 , pp. 33-69
    • Beard, N.A.1    Laver, D.R.2    Dulhunty, A.F.3
  • 6
    • 0035943673 scopus 로고    scopus 로고
    • Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres
    • Bellin, R.M., T.W. Huiatt, D.R. Critchley, and R.M. Robson. 2001. Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres. J. Biol. Chem. 276:32330-32337.
    • (2001) J. Biol. Chem , vol.276 , pp. 32330-32337
    • Bellin, R.M.1    Huiatt, T.W.2    Critchley, D.R.3    Robson, R.M.4
  • 7
    • 0022899276 scopus 로고
    • The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscle
    • Bennett, P., R. Craig, R. Starr, and G. Offer. 1986. The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscle. J. Muscle Res. Cell Motil. 7:550-567.
    • (1986) J. Muscle Res. Cell Motil , vol.7 , pp. 550-567
    • Bennett, P.1    Craig, R.2    Starr, R.3    Offer, G.4
  • 8
    • 0033939421 scopus 로고    scopus 로고
    • Calcium ion in skeletal muscle: Its crucial role for muscle function, plasticity, and disease
    • Berchtold, M.W., H. Brinkmeier, and M. Muntener. 2000. Calcium ion in skeletal muscle: its crucial role for muscle function, plasticity, and disease. Physiol. Rev. 80:1215-1265.
    • (2000) Physiol. Rev. , vol.80 , pp. 1215-1265
    • Berchtold, M.W.1    Brinkmeier, H.2    Muntener, M.3
  • 9
    • 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. Nat. New Biol. 238:97-101.
    • (1972) Nat. Ne , vol.238 , pp. 97-101
    • Bremel, R.D.1    Weber, A.2
  • 10
    • 0023161167 scopus 로고
    • Mechanical and structural approaches to correlation of cross-bridge action in muscle with actomyosin ATPase in solution
    • Brenner, B. 1987. Mechanical and structural approaches to correlation of cross-bridge action in muscle with actomyosin ATPase in solution. Annu. Rev. Physiol. 49:655-672.
    • (1987) Annu. Rev. Physiol , vol.49 , pp. 655-672
    • Brenner, B.1
  • 11
    • 0141746289 scopus 로고    scopus 로고
    • Number and spatial distribution of nuclei in the muscle fibres of normal mice studied in vivo
    • Bruusgaard, J C., K. Liestol, M. Ekmark, K. Kollstad, and K. Gundersen. 2003. Number and spatial distribution of nuclei in the muscle fibres of normal mice studied in vivo. J. Physiol. 551:467-478.
    • (2003) J. Physiol , vol.551 , pp. 467-478
    • Bruusgaard, J.C.1    Liestol, K.2    Ekmark, M.3    Kollstad, K.4    Gundersen, K.5
  • 12
    • 0036446688 scopus 로고    scopus 로고
    • Structure and nucleotide-dependent changes of thick filaments in relaxed and rigor plaice fin muscle
    • Cantino, M.E., M.W. Chew, P.K. Luther, E. Morris, and J.M. Squire. 2002. Structure and nucleotide-dependent changes of thick filaments in relaxed and rigor plaice fin muscle. J. Struct. Biol. 137:164-175.
    • (2002) J. Struct. Biol , vol.137 , pp. 164-175
    • Cantino, M.E.1    Chew, M.W.2    Luther, P.K.3    Morris, E.4    Squire, J.M.5
  • 13
    • 0022613021 scopus 로고
    • Resting myosin crossbridge configuration in frog muscle thick filaments
    • Cantino, M.E. and J.M. Squire.1986. Resting myosin crossbridge configuration in frog muscle thick filaments. J. Cell Biol. 102:610-618.
    • (1986) J. Cell Biol , vol.102 , pp. 610-618
    • Cantino, M.E.1    Squire, J.M.2
  • 14
    • 0025970527 scopus 로고
    • Actin: Protein structure and filament dynamics
    • Carlier, M.F. 1991. Actin: protein structure and filament dynamics. J. Biol. Chem. 266:1-4.
    • (1991) J. Biol. Chem , vol.266 , pp. 1-4
    • Carlier, M.F.1
  • 15
    • 0029586906 scopus 로고
    • Packing of α-helical coiled-coil myosin rods in vertebrate muscle thick filaments
    • Chew, M.W.K. and J.M. Squire. 1995. Packing of α-helical coiled-coil myosin rods in vertebrate muscle thick filaments. J. Struct. Biol. 115:233-249.
    • (1995) J. Struct. Biol , vol.115 , pp. 233-249
    • Chew, M.W.K.1    Squire, J.M.2
  • 16
    • 0027532691 scopus 로고
    • Properties of skeletal muscle mitochondria isolated from subsarcolemmal and intermyofibrillar regions
    • Cogswell, A. M., R.J. Stevens, and D.A. Hood. 1993. Properties of skeletal muscle mitochondria isolated from subsarcolemmal and intermyofibrillar regions. Am. J. Physiol. 264:C383-389.
    • (1993) Am. J. Physiol , vol.264 , pp. C383-C389
    • Cogswell, A.M.1    Stevens, R.J.2    Hood, D.A.3
  • 17
    • 0033965314 scopus 로고    scopus 로고
    • Control of actin assembly and disassembly at filament ends
    • Cooper, J.A. and D.A. Schafer. 2000. Control of actin assembly and disassembly at filament ends. Curr. Opin. Cell. Biol. 12:97-103.
    • (2000) Curr. Opin. Cell. Biol , vol.12 , pp. 97-103
    • Cooper, J.A.1    Schafer, D.A.2
  • 18
    • 0017234893 scopus 로고
    • The location of C-protein in rabbit skeletal muscle
    • Craig, R. and G. Offer. 1976. The location of C-protein in rabbit skeletal muscle. Proc. Roy. Soc. London B 192:451-461.
    • (1976) Proc. Roy. Soc. London B , vol.192 , pp. 451-461
    • Craig, R.1    Offer, G.2
  • 19
    • 33646009721 scopus 로고    scopus 로고
    • Structure and function of myosin filaments
    • Craig, R. and J.L. Woodhead. 2006. Structure and function of myosin filaments. Curr. Opin. Struct. Biol. 16:204-212.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 204-212
    • Craig, R.1    Woodhead, J.L.2
  • 20
    • 8744300054 scopus 로고    scopus 로고
    • Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion
    • Critchley, D.R. 2004. Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion. Biochem. Soc. Trans. 32:831-836.
    • (2004) Biochem. Soc. Trans , vol.32 , pp. 831-836
    • Critchley, D.R.1
  • 21
    • 0026694489 scopus 로고
    • Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres
    • Dantzig, J.A., Y.E. Goldman, N.C. Millar, J. Lacktis, and E. Homsher. 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
  • 22
    • 0023754977 scopus 로고
    • Assembly processes in vertebrate skeletal thick filament formation
    • Davis, J.S. 1988. Assembly processes in vertebrate skeletal thick filament formation. Annu. Rev. Biophys. Biophys. Chem. 17:217-239.
    • (1988) Annu. Rev. Biophys. Biophys. Chem , vol.17 , pp. 217-239
    • Davis, J.S.1
  • 23
    • 33744978162 scopus 로고    scopus 로고
    • Myosin binding protein C in the heart
    • de Tombe, P.P. 2006. Myosin binding protein C in the heart. Circ. Res. 98:1234-1236.
    • (2006) Circ. Res , vol.98 , pp. 1234-1236
    • De Tombe, P.P.1
  • 25
    • 0038190993 scopus 로고    scopus 로고
    • Costameres: The Achilles’ heel of Herculean muscle
    • Ervasti, J.M. 2003. Costameres: the Achilles’ heel of Herculean muscle. J. Biol. Chem. 278:13591-13594.
    • (2003) J. Biol. Chem , vol.278 , pp. 13591-13594
    • Ervasti, J.M.1
  • 26
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah, C.S. and F.C. Reinach. 1995. The troponin complex and regulation of muscle contraction. FASEB J. 9:755-767.
    • (1995) FASEB J , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 27
    • 0034776199 scopus 로고    scopus 로고
    • Telethonin and other new proteins of the Z-disc of skeletal muscle
    • Faulkner, G., G. Lanfranchi, and G. Valle. 2001. Telethonin and other new proteins of the Z-disc of skeletal muscle. IUBMB Life 51:275-282.
    • (2001) IUBMB Life , vol.51 , pp. 275-282
    • Faulkner, G.1    Lanfranchi, G.2    Valle, G.3
  • 28
    • 0036788917 scopus 로고    scopus 로고
    • Ryanodine receptor calcium release channels
    • Fill, M. and J.A. Copello. 2002. Ryanodine receptor calcium release channels. Physiol. Rev. 82:893-922.
    • (2002) Physiol. Rev , vol.82 , pp. 893-922
    • Fill, M.1    Copello, J.A.2
  • 29
    • 0142157493 scopus 로고    scopus 로고
    • Tropomodulins: Life at the slow end
    • Fischer, R.S. and V.M. Fowler. 2003. Tropomodulins: life at the slow end. Trends Cell. Biol. 13:593-601.
    • (2003) Trends Cell. Biol , vol.13 , pp. 593-601
    • Fischer, R.S.1    Fowler, V.M.2
  • 30
    • 38649111025 scopus 로고    scopus 로고
    • Support for a trimeric collar of myosin binding protein C in cardiac and fast skeletal muscle, but not in slow skeletal muscle
    • Flashman, E., L. Korkie, H. Watkins, C. Redwood, and J.C. Moolman-Smook. 2008. Support for a trimeric collar of myosin binding protein C in cardiac and fast skeletal muscle, but not in slow skeletal muscle. FEBS Lett. 582:434-438.
    • (2008) FEBS Lett , vol.582 , pp. 434-438
    • Flashman, E.1    Korkie, L.2    Watkins, H.3    Redwood, C.4    Moolman-Smook, J.C.5
  • 31
    • 0020475827 scopus 로고
    • Troponin and its interactions with tropomyosin. An electron microscope study
    • Flicker, P.F., G.N. Phillips Jr., and C. Cohen. 1982. Troponin and its interactions with tropomyosin. An electron microscope study. J. Mol. Biol. 162:495-501.
    • (1982) J. Mol. Biol , vol.162 , pp. 495-501
    • Flicker, P.F.1    Phillips, G.N.2    Cohen, C.3
  • 32
    • 33644856260 scopus 로고    scopus 로고
    • New insights into myosin evolution and classification
    • Foth, B.J., M.C. Goedecke, and D. Soldati. 2006. New insights into myosin evolution and classification. Proc. Natl. Acad. Sci. 103:368-3686.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 368-3686
    • Foth, B.J.1    Goedecke, M.C.2    Soldati, D.3
  • 33
    • 0141809370 scopus 로고    scopus 로고
    • Tropomodulin contains two actin filament pointed endcapping domains
    • Fowler, V.M., N.J. Greenfield, and J. Moyer. 2003. Tropomodulin contains two actin filament pointed endcapping domains. J. Biol. Chem. 278:40000-40009.
    • (2003) J. Biol. Chem , vol.278 , pp. 40000-40009
    • Fowler, V.M.1    Greenfield, N.J.2    Moyer, J.3
  • 34
    • 33744494538 scopus 로고    scopus 로고
    • The sarcomeric Z-disc: A nodal point in signalling and disease
    • Frank, D., C. Kuhn, H.A. Katus, and N. Frey. 2006. The sarcomeric Z-disc: a nodal point in signalling and disease. J. Mol. Med. 84:446-468.
    • (2006) J. Mol. Med , vol.84 , pp. 446-468
    • Frank, D.1    Kuhn, C.2    Katus, H.A.3    Frey, N.4
  • 35
    • 0034622584 scopus 로고    scopus 로고
    • Inhibition of actin-myosin subfragment 1 ATPase activity by troponin I and IC: Relationship to the thin filament states of muscle
    • Geeves, M.A., M. Chai, and S.S. Lehrer. 2000. Inhibition of actin-myosin subfragment 1 ATPase activity by troponin I and IC: relationship to the thin filament states of muscle. Biochemistry. 39:9345-9350.
    • (2000) Biochemistry , vol.39 , pp. 9345-9350
    • Geeves, M.A.1    Chai, M.2    Lehrer, S.S.3
  • 36
    • 26844566272 scopus 로고    scopus 로고
    • The molecular mechanism of muscle contraction
    • Geeves, M.A. and K.C. Holmes. 2005. The molecular mechanism of muscle contraction. Adv. Protein Chem. 71:161-193.
    • (2005) Adv. Protein Chem , vol.71 , pp. 161-193
    • Geeves, M.A.1    Holmes, K.C.2
  • 37
    • 0019432392 scopus 로고
    • The synthesis and deployment of filamin in chicken skeletal muscle
    • Gomer, R.H. and E. Lazarides. 1981. The synthesis and deployment of filamin in chicken skeletal muscle. Cell 23:524-532.
    • (1981) Cell , vol.23 , pp. 524-532
    • Gomer, R.H.1    Lazarides, E.2
  • 38
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A.M., E. Homsher, and M. Regnier. 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
  • 39
    • 0013905011 scopus 로고
    • The variation in isometric tension with sarcomere length in vertebrate muscle fibres
    • Gordon, A.M., A.F. Huxley, and F.J. Julian. 1966. The variation in isometric tension with sarcomere length in vertebrate muscle fibres. J. Physiol. 184:170-192.
    • (1966) J. Physiol , vol.184 , pp. 170-192
    • Gordon, A.M.1    Huxley, A.F.2    Julian, F.J.3
  • 41
    • 37049012075 scopus 로고    scopus 로고
    • Structure-function relations of the giant elastic protein titin in striated and smooth muscle cells
    • Granzier, H. and S. Labeit. 2007. Structure-function relations of the giant elastic protein titin in striated and smooth muscle cells. Muscle Nerve 36:740-755.
    • (2007) Muscle Nerve , vol.36 , pp. 740-755
    • Granzier, H.1    Labeit, S.2
  • 42
    • 33749681688 scopus 로고    scopus 로고
    • New insights in the role of cardiac myosin binding protein C as a regulator of cardiac contractility
    • Granzier, H.L. and K.B. Campbell. 2006. New insights in the role of cardiac myosin binding protein C as a regulator of cardiac contractility. Circ. Res. 99:795-797.
    • (2006) Circ. Res , vol.99 , pp. 795-797
    • Granzier, H.L.1    Campbell, K.B.2
  • 44
    • 0032899830 scopus 로고    scopus 로고
    • Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers
    • Hijikata, T., T. Murakami, M. Imamura, N. Fujimaki, and H. Ishikawa. 1999. Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers. J. Cell Sci. 112(Pt. 6):867-876.
    • (1999) J. Cell Sci , vol.112 , pp. 867-876
    • Hijikata, T.1    Murakami, T.2    Imamura, M.3    Fujimaki, N.4    Ishikawa, H.5
  • 45
    • 47649083199 scopus 로고    scopus 로고
    • Plectin 1 links intermediate filaments to costameric sarcolemma through (beta)-synemin, (alpha)-dystrobrevin and actin
    • Hijikata, T., A. Nakamura, K. Isokawa, M. Imamura, K. Yuasa, R. Ishikawa, K. Kohama, S. Takeda, and H. Yorifuji. 2008. Plectin 1 links intermediate filaments to costameric sarcolemma through (beta)-synemin, (alpha)-dystrobrevin and actin. J. Cell Sci. 121:2062-2074.
    • (2008) J. Cell Sci , vol.121 , pp. 2062-2074
    • Hijikata, T.1    Nakamura, A.2    Isokawa, K.3    Imamura, M.4    Yuasa, K.5    Ishikawa, R.6    Kohama, K.7    Takeda, S.8    Yorifuji, H.9
  • 46
  • 47
    • 0041825389 scopus 로고    scopus 로고
    • Muscle-type creatine kinase interacts with central domains of the M-band proteins myomesin and M-protein
    • Hornemann, T., S. Kempa, M. Himmel, K. Hayess, D. O. Furst, and T. Wallimann. 2003. Muscle-type creatine kinase interacts with central domains of the M-band proteins myomesin and M-protein. J. Mol. Biol. 332: 877-887.
    • (2003) J. Mol. Biol , vol.332 , pp. 877-887
    • Hornemann, T.1    Kempa, S.2    Himmel, M.3    Hayess, K.4    Furst, D.O.5    Wallimann, T.6
  • 48
    • 85010249552 scopus 로고
    • The low-angle x-ray diagram of vertebrate striated muscle and its behavior during contraction and rigor
    • Huxley, H.E. and W. Brown. 1967. The low-angle x-ray diagram of vertebrate striated muscle and its behavior 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
  • 49
    • 0030031120 scopus 로고    scopus 로고
    • Multiple-and single-molecule analysis of the actomyosin motor by nanometer-piconewton manipulation with a microneedle: Unitary steps and forces
    • Ishijima, A., H. Kojima, H. Higuchi, Y. Harada, T. Funatsu, and T. Yanagida. 1996. Multiple-and single-molecule analysis of the actomyosin motor by nanometer-piconewton manipulation with a microneedle: unitary steps and forces. Biophys. J. 70:383-400.
    • (1996) Biophys. J , vol.70 , pp. 383-400
    • Ishijima, A.1    Kojima, H.2    Higuchi, H.3    Harada, Y.4    Funatsu, T.5    Yanagida, T.6
  • 51
    • 13844292743 scopus 로고    scopus 로고
    • The mammalian cardiac muscle thick filament: Backbone contributions to meridional reflections
    • Kensler, R.W. 2005. The mammalian cardiac muscle thick filament: backbone contributions to meridional reflections. J. Struct. Biol. 149:313-324.
    • (2005) J. Struct. Biol , vol.149 , pp. 313-324
    • Kensler, R.W.1
  • 52
    • 13844264469 scopus 로고    scopus 로고
    • The mammalian cardiac muscle thick filament: Crossbridge arrangement
    • Kensler, R.W. 2005b. The mammalian cardiac muscle thick filament: Crossbridge arrangement. J. Struct. Biol. 149:303-312.
    • (2005) J. Struct. Biol , vol.149 , pp. 303-312
    • Kensler, R.W.1
  • 53
    • 0022493066 scopus 로고
    • Mitochondrial reticulum in limb skeletal muscle
    • Kirkwood, S.P., E.A. Munn, and G.A. Brooks. 1986. Mitochondrial reticulum in limb skeletal muscle. Am. J. Physiol. 251:C395-C402.
    • (1986) Am. J. Physiol , vol.251 , pp. C395-C402
    • Kirkwood, S.P.1    Munn, E.A.2    Brooks, G.A.3
  • 56
    • 0037115642 scopus 로고    scopus 로고
    • Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2
    • Lange, S., D. Auerbach, P. McLoughlin, E. Perriard, B.W. Schafer, J.C. Perriard, and E. Ehler. 2002. Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2. J. Cell Sci. 115:4925-4936.
    • (2002) J. Cell Sci , vol.115 , pp. 4925-4936
    • Lange, S.1    Auerbach, D.2    McLoughlin, P.3    Perriard, E.4    Schafer, B.W.5    Perriard, J.C.6    Ehler, E.7
  • 58
    • 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
  • 60
    • 0034900675 scopus 로고    scopus 로고
    • Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions
    • Levine, R., A. Weisberg, I. Kulikovskaya, G. McClellan, and S. Winegrad. 2001. Multiple structures of thick filaments in resting cardiac muscle and their influence on cross-bridge interactions. Biophys. J. 81:1070-1082.
    • (2001) Biophys. J , vol.81 , pp. 1070-1082
    • Levine, R.1    Weisberg, A.2    Kulikovskaya, I.3    McClellan, G.4    Winegrad, S.5
  • 61
    • 0032407540 scopus 로고    scopus 로고
    • Defining actin filament length in striated muscle: Rulers and caps or dynamic stability?
    • Littlefield, R. and V.M. Fowler. 1998. Defining actin filament length in striated muscle: rulers and caps or dynamic stability?. Annu. Rev. Cell. Dev. Biol. 14:487-525.
    • (1998) Annu. Rev. Cell. Dev. Biol , vol.14 , pp. 487-525
    • Littlefield, R.1    Fowler, V.M.2
  • 62
    • 0037022537 scopus 로고    scopus 로고
    • Each actin subunit has three nebulin binding sites: Implications for steric blocking
    • Lukoyanova, N., M.S. VanLoock, A. Orlova, V.E. Galkin, K. Wang, and E.H. Egelman. 2002. Each actin subunit has three nebulin binding sites: implications for steric blocking. Curr. Biol. 12:383-388.
    • (2002) Curr. Biol , vol.12 , pp. 383-388
    • Lukoyanova, N.1    Vanloock, M.S.2    Orlova, A.3    Galkin, V.E.4    Wang, K.5    Egelman, E.H.6
  • 63
    • 0036300408 scopus 로고    scopus 로고
    • Troponin-I interacts with the Met47 region of skeletal muscle actin. Implications for the mechanism of thin filament regulation by calcium
    • Luo, Y., J. Leszyk, B. Li, Z. Li, J. Gergely, and T. Tao. 2002. Troponin-I interacts with the Met47 region of skeletal muscle actin. Implications for the mechanism of thin filament regulation by calcium. J. Mol. Biol. 316:429-434.
    • (2002) J. Mol. Biol , vol.316 , pp. 429-434
    • Luo, Y.1    Leszyk, J.2    Li, B.3    Li, Z.4    Gergely, J.5    Tao, T.6
  • 64
    • 0036297519 scopus 로고    scopus 로고
    • The three-dimensional structure of a vertebrate wide (Slow muscle) Z-band: Lessons on Z-band assembly
    • Luther, P.K., J.S. Barry, and J.M. Squire. 2002. The three-dimensional structure of a vertebrate wide (slow muscle) Z-band: lessons on Z-band assembly. J. Mol. Biol. 315:9-20.
    • (2002) J. Mol. Biol , vol.315 , pp. 9-20
    • Luther, P.K.1    Barry, J.S.2    Squire, J.M.3
  • 65
    • 0030250140 scopus 로고    scopus 로고
    • Evolution of myosin filament arrangements in vertebrate skeletal muscle
    • Luther, P.K., J.M. Squire, and P.L. Forey. 1996. Evolution of myosin filament arrangements in 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
  • 66
    • 0038158092 scopus 로고    scopus 로고
    • Integrins: Redundant or important players in skeletal muscle
    • Mayer, U. 2003. Integrins: redundant or important players in skeletal muscle? J. Biol. Chem. 278: 14587-14590.
    • (2003) J. Biol. Chem , vol.278 , pp. 14587-14590
    • Mayer, U.1
  • 68
    • 0032054640 scopus 로고    scopus 로고
    • F-actin-binding proteins
    • McGough, A. 1998. F-actin-binding proteins. Curr. Opin. Struct. Biol. 8:166-176.
    • (1998) Curr. Opin. Struct. Biol , vol.8 , pp. 166-176
    • McGough, A.1
  • 69
    • 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 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.1    Geeves, M.A.2
  • 70
    • 0021103673 scopus 로고
    • Periodic features in the amino acid sequence of nematode myosin rod
    • McLachlan, A.D. and J. Karn. 1983. Periodic features in the amino acid sequence of nematode myosin rod. J. Mol. Biol. 164:605-626.
    • (1983) J. Mol. Biol , vol.164 , pp. 605-626
    • McLachlan, A.D.1    Karn, J.2
  • 71
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function
    • Michele, D.E. and K.P. Campbell. 2003. Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function. J. Biol. Chem. 278:15457-15460.
    • (2003) J. Biol. Chem , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 73
    • 33746791896 scopus 로고    scopus 로고
    • Myosin light chain 2 into the mainstream of cardiac development and contractility
    • Moss, R.L. and D.P. Fitzsimons. 2006. Myosin light chain 2 into the mainstream of cardiac development and contractility. Circ. Res. 99:225-227.
    • (2006) Circ. Res , vol.99 , pp. 225-227
    • Moss, R.L.1    Fitzsimons, D.P.2
  • 74
    • 0020064675 scopus 로고
    • Potentiated state of the tropomyosin actin filament and nucleotide-containing myosin subfragment 1
    • Murray, J.M., M.K. Knox, C.E. Trueblood, and A. Weber. 1982. Potentiated state of the tropomyosin actin filament and nucleotide-containing myosin subfragment 1. Biochemistry. 21:906-915.
    • (1982) Biochemistry , vol.21 , pp. 906-915
    • Murray, J.M.1    Knox, M.K.2    Trueblood, C.E.3    Weber, A.4
  • 75
    • 0036139685 scopus 로고    scopus 로고
    • Advances in neurobiology of the neuromuscular junction: Implications for the anesthesiologist
    • Naguib, M., P. Flood, J.J. McArdle, and H.R. Brenner. 2002. Advances in neurobiology of the neuromuscular junction: implications for the anesthesiologist. Anesthesiology 96:202-231.
    • (2002) Anesthesiology , vol.96 , pp. 202-231
    • Naguib, M.1    Flood, P.2    McArdle, J.J.3    Brenner, H.R.4
  • 76
    • 33751567905 scopus 로고    scopus 로고
    • Structural basis of actin filament capping at the barbed-end: A cryo-electron microscopy study
    • Narita, A., S. Takeda, A. Yamashita, and Y. Maeda. 2006. Structural basis of actin filament capping at the barbed-end: a cryo-electron microscopy study. EMBO J. 25:5626-5633.
    • (2006) EMBO J , vol.25 , pp. 5626-5633
    • Narita, A.1    Takeda, S.2    Yamashita, A.3    Maeda, Y.4
  • 77
    • 0035957530 scopus 로고    scopus 로고
    • Ca(2+)-induced switching of troponin and tropomyosin on actin filaments as revealed by electron cryo-microscopy
    • Narita, A., T. Yasunaga, T. Ishikawa, K. Mayanagi, and T. Wakabayashi. 2001. Ca(2+)-induced switching of troponin and tropomyosin on actin filaments as revealed by electron cryo-microscopy. J. Mol. Biol. 308:241-261.
    • (2001) J. Mol. Biol , vol.308 , pp. 241-261
    • Narita, A.1    Yasunaga, T.2    Ishikawa, T.3    Mayanagi, K.4    Wakabayashi, T.5
  • 79
    • 33847067962 scopus 로고    scopus 로고
    • Axial dispositions and conformations of myosin crossbridges along thick filaments in relaxed and contracting states of vertebrate striated muscles by x-ray fiber diffraction
    • Oshima, K., Y. Takezawa, Y. Sugimoto, T. Kobayashi, T.C. Irving, and K. Wakabayashi. 2007. Axial dispositions and conformations of myosin crossbridges along thick filaments in relaxed and contracting states of vertebrate striated muscles by x-ray fiber diffraction. J. Mol. Biol. 367:275-301.
    • (2007) J. Mol. Biol , vol.367 , pp. 275-301
    • Oshima, K.1    Takezawa, Y.2    Sugimoto, Y.3    Kobayashi, T.4    Irving, T.C.5    Wakabayashi, K.6
  • 80
    • 2442481067 scopus 로고    scopus 로고
    • Alpha-actinin revisited: A fresh look at an old player
    • Otey, C.A. and O. Carpen. 2004. Alpha-actinin revisited: a fresh look at an old player. Cell Motil. Cytoskeleton 58:104-111.
    • (2004) Cell Motil. Cytoskeleton , vol.58 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 82
    • 48249127189 scopus 로고    scopus 로고
    • Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc
    • Pappas, C.T., N. Bhattacharya, J.A. Cooper, and C.C. Gregorio. 2008. Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc. Mol. Biol. Cell 19:1837-1847.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1837-1847
    • Pappas, C.T.1    Bhattacharya, N.2    Cooper, J.A.3    Gregorio, C.C.4
  • 83
    • 6344260556 scopus 로고    scopus 로고
    • Desmin: A major intermediate filament protein essential for the structural integrity and function of muscle
    • Paulin, D. and Z. Li. 2004. Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle. Exp. Cell Res. 301:1-7.
    • (2004) Exp. Cell Res , vol.301 , pp. 1-7
    • Paulin, D.1    Li, Z.2
  • 84
    • 0019573953 scopus 로고
    • Identification of a second binding region on rabbit skeletal troponin-T for alpha-tropomyosin
    • Pearlstone, J.R. and L.B. Smillie. 1981. Identification of a second binding region on rabbit skeletal troponin-T for alpha-tropomyosin. FEBS Lett. 128:119-122.
    • (1981) FEBS Lett , vol.128 , pp. 119-122
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 85
    • 34047219171 scopus 로고    scopus 로고
    • SERCA pump isoforms: Their role in calcium transport and disease
    • Periasamy, M. and A. Kalyanasundaram. 2007. SERCA pump isoforms: their role in calcium transport and disease. Muscle Nerve 35:430-442.
    • (2007) Muscle Nerve , vol.35 , pp. 430-442
    • Periasamy, M.1    Kalyanasundaram, A.2
  • 86
    • 0031855272 scopus 로고    scopus 로고
    • Troponin T: Genetics, properties and function
    • Perry, S.V. 1998. Troponin T: genetics, properties and function. J. Muscle Res. Cell Motil. 19:575-602.
    • (1998) J. Muscle Res. Cell Motil , vol.19 , pp. 575-602
    • Perry, S.V.1
  • 87
    • 0033044797 scopus 로고    scopus 로고
    • Troponin I: Inhibitor or facilitator
    • Perry, S.V. 1999. Troponin I: inhibitor or facilitator. Mol. Cell. Biochem. 190:9-32.
    • (1999) Mol. Cell. Biochem , vol.190 , pp. 9-32
    • Perry, S.V.1
  • 88
    • 0034841005 scopus 로고    scopus 로고
    • Vertebrate tropomyosin: Distribution, properties and function
    • Perry, S.V. 2001 Vertebrate tropomyosin: distribution, properties and function. J. Muscle Res. Cell Motil. 22:5-49.
    • (2001) J. Muscle Res. Cell Motil , vol.22 , pp. 5-49
    • Perry, S.V.1
  • 89
    • 0028347405 scopus 로고
    • Nebulin, a helical actin binding protein
    • Pfuhl, M., S.J. Winder, and A. Pastore. 1994. Nebulin, a helical actin binding protein. EMBO J. 13:1782-1789.
    • (1994) EMBO J , vol.13 , pp. 1782-1789
    • Pfuhl, M.1    Winder, S.J.2    Pastore, A.3
  • 92
    • 2442544551 scopus 로고    scopus 로고
    • Light microscopy and image analysis of thin filament lengths utilizing dual probes on beef, chicken, and rabbit myofibrils
    • Ringkob, T.P., D.R. Swartz, and M.L. Greaser. 2004. Light microscopy and image analysis of thin filament lengths utilizing dual probes on beef, chicken, and rabbit myofibrils. J. Anim. Sci. 82:1445-1453.
    • (2004) J. Anim. Sci , vol.82 , pp. 1445-1453
    • Ringkob, T.P.1    Swartz, D.R.2    Greaser, M.L.3
  • 93
    • 0037832412 scopus 로고    scopus 로고
    • The basement membrane/basal lamina of skeletal muscle
    • Sanes, J.R. 2003. The basement membrane/basal lamina of skeletal muscle. J. Biol. Chem. 278:12601-12604.
    • (2003) J. Biol. Chem , vol.278 , pp. 12601-12604
    • Sanes, J.R.1
  • 95
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • Siemankowski, R.F., M.O. Wiseman, and H.D. White. 1985. ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc. Natl. Acad. Sci. U.S.A. 82:658-662.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 658-662
    • Siemankowski, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 100
    • 0042093724 scopus 로고    scopus 로고
    • Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain
    • Squire, J.M., P.K. Luther, and C. Knupp. 2003. Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain. J. Mol. Biol. 331:713-724.
    • (2003) J. Mol. Biol , vol.331 , pp. 713-724
    • Squire, J.M.1    Luther, P.K.2    Knupp, C.3
  • 101
    • 0031777885 scopus 로고    scopus 로고
    • A new look at thin filament regulation in vertebrate skeletal muscle
    • Squire, J.M. and E.P. Morris. 1998. A new look at thin filament regulation in vertebrate skeletal muscle. FASEB J. 12:761-771.
    • (1998) FASEB J , vol.12 , pp. 761-771
    • Squire, J.M.1    Morris, E.P.2
  • 102
    • 0024592372 scopus 로고
    • Dissociation of force from myofibrillar MgATPase and stiffness at short sarcomere lengths in rat and toad skeletal muscle
    • Stephenson, D.G., A.W. Stewart, and G.J. Wilson. 1989. Dissociation of force from myofibrillar MgATPase and stiffness at short sarcomere lengths in rat and toad skeletal muscle. J. Physiol. 410:351-366.
    • (1989) J. Physiol , vol.410 , pp. 351-366
    • Stephenson, D.G.1    Stewart, A.W.2    Wilson, G.J.3
  • 103
    • 26244466046 scopus 로고    scopus 로고
    • Skip Residues and Charge Interactions in Myosin II Coiled-coils: Implications for Molecular Packing
    • Straussman, R., J.M. Squire, A. Ben-Ya’acov, and S. Ravid. 2005. Skip Residues and Charge Interactions in Myosin II Coiled-coils: Implications for Molecular Packing. Journal of Molecular Biology. 353:613-628.
    • (2005) Journal of Molecular Biology , vol.353 , pp. 613-628
    • Straussman, R.1    Squire, J.M.2    Ben-Ya’acov, A.3    Ravid, S.4
  • 104
    • 0032869609 scopus 로고    scopus 로고
    • Exchange of alpha-actinin in isolated rigor myofibrils
    • Swartz, D.R. 1999. Exchange of alpha-actinin in isolated rigor myofibrils. J. Muscle Res. Cell Motil. 20:457-467.
    • (1999) J. Muscle Res. Cell Motil , vol.20 , pp. 457-467
    • Swartz, D.R.1
  • 105
    • 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
  • 106
    • 43949172570 scopus 로고
    • Structural studies of rigor bovine myofibrils using fluorescence microscopy. II. Influence of sarcomere length on the binding of myosin subfragment 1, alphaactinin 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, alphaactinin 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
  • 108
    • 33746374729 scopus 로고    scopus 로고
    • Myofibrillar troponin exists in three states and there is signal transduction along skeletal myofibrillar thin filaments
    • Swartz, D.R., Z. Yang, A. Sen, S.B. Tikunova, and J.P. Davis. 2006. Myofibrillar troponin exists in three states and there is signal transduction along skeletal myofibrillar thin filaments. J. Mol. Biol. 361:420-435.
    • (2006) J. Mol. Biol , vol.361 , pp. 420-435
    • Swartz, D.R.1    Yang, Z.2    Sen, A.3    Tikunova, S.B.4    Davis, J.P.5
  • 109
    • 0035919832 scopus 로고    scopus 로고
    • The three-dimensional structure of alpha-actinin obtained by cryoelectron microscopy suggests a model for Ca(2+)-dependent actin binding
    • Tang, J., D.W. Taylor, and K.A. Taylor. 2001. The three-dimensional structure of alpha-actinin obtained by cryoelectron microscopy suggests a model for Ca(2+)-dependent actin binding. J. Mol. Biol. 310:845-858.
    • (2001) J. Mol. Biol , vol.310 , pp. 845-858
    • Tang, J.1    Taylor, D.W.2    Taylor, K.A.3
  • 110
    • 0023032139 scopus 로고
    • Energy stored and dissipated in skeletal muscle basement membranes during sinusoidal oscillations
    • Tidball, J.G. 1986. Energy stored and dissipated in skeletal muscle basement membranes during sinusoidal oscillations. Biophys. J. 50:1127-1138.
    • (1986) Biophys. J , vol.50 , pp. 1127-1138
    • Tidball, J.G.1
  • 111
    • 0026318162 scopus 로고
    • Force transmission across muscle cell membranes
    • Tidball, J.G. 1991. Force transmission across muscle cell membranes. J. Biomech. 24(Suppl. 1):43-52.
    • (1991) J. Biomech , vol.24 , pp. 43-52
    • Tidball, J.G.1
  • 113
    • 0019834569 scopus 로고
    • End-filaments: A new structural element of vertebrate skeletal muscle thick filaments
    • Trinick, J.A. 1981. End-filaments: a new structural element of vertebrate skeletal muscle thick filaments. J. Mol. Biol. 151 309-314.
    • (1981) J. Mol. Biol , vol.151 , pp. 309-314
    • Trinick, J.A.1
  • 115
    • 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
  • 116
    • 0028283285 scopus 로고
    • The muscle Z band: Lessons in stress management
    • Vigoreaux, J.O. 1994. The muscle Z band: lessons in stress management. J. Muscle Res. Cell Motil. 15:237-255.
    • (1994) J. Muscle Res. Cell Motil , vol.15 , pp. 237-255
    • Vigoreaux, J.O.1
  • 118
    • 0035836733 scopus 로고    scopus 로고
    • Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2
    • Wendt, T., D. Taylor, K.M. Trybus, and K. Taylor. 2001. Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2. Proc. Natl. Acad. Sci. U.S.A. 98:4361-4366.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4361-4366
    • Wendt, T.1    Taylor, D.2    Trybus, K.M.3    Taylor, K.4
  • 119
    • 0031663054 scopus 로고    scopus 로고
    • Role of plectin in cytoskeleton organization and dynamics
    • Wiche, G. 1998. Role of plectin in cytoskeleton organization and dynamics. J. Cell. Sci. 111(Pt. 17):2477-2486.
    • (1998) J. Cell. Sci , vol.111 , pp. 2477-2486
    • Wiche, G.1
  • 120
    • 0033612182 scopus 로고    scopus 로고
    • Cardiac myosin binding protein C
    • Winegrad, S. 1999. Cardiac myosin binding protein C. Circ. Res. 84:1117-1126.
    • (1999) Circ. Res , vol.84 , pp. 1117-1126
    • Winegrad, S.1
  • 122
    • 0018328198 scopus 로고
    • Structure of the backbone in myosin filaments of muscle
    • Wray, J.S. 1979. Structure of the backbone in myosin filaments of muscle. Nature 277:37-40.
    • (1979) Nature , vol.277 , pp. 37-40
    • Wray, J.S.1
  • 123
    • 0029987687 scopus 로고    scopus 로고
    • Myosin filament structure in vertebrate smooth muscle
    • Xu, J.-Q., B.A. Harder, P. Uman, and R. Craig. 1996. Myosin filament structure in vertebrate smooth muscle. J. Cell. Biol. 134:53-66.
    • (1996) J. Cell. Biol , vol.134 , pp. 53-66
    • Xu, J.-Q.1    Harder, B.A.2    Uman, P.3    Craig, R.4
  • 124
    • 0017773079 scopus 로고
    • Return of myosin heads to thick filaments after muscle contraction
    • Yagi, N., M.H. Ito, H. Nakajima, T. Izumi, and I. Matsubard. 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    Matsubard, I.5
  • 125
    • 0022259764 scopus 로고
    • Fine structure of wide and narrow vertebrate muscle Z-lines. A proposed model and computer simulation of Z-line architecture
    • Yamaguchi, M., M. Izumimoto, R.M. Robson, and M.H. Stromer. 1985. Fine structure of wide and narrow vertebrate muscle Z-lines. A proposed model and computer simulation of Z-line architecture. J. Mol. Biol. 184:621-643.
    • (1985) J. Mol. Biol , vol.184 , pp. 621-643
    • Yamaguchi, M.1    Izumimoto, M.2    Robson, R.M.3    Stromer, M.H.4
  • 126
    • 0020586760 scopus 로고
    • Evidence for actin involvement in cardiac Z-lines and Z-line analogues
    • Yamaguchi, M., R.M. Robson, and M.H. Stromer. 1983. Evidence for actin involvement in cardiac Z-lines and Z-line analogues. J. Cell. Biol. 96:435-442.
    • (1983) J. Cell. Biol , vol.96 , pp. 435-442
    • Yamaguchi, M.1    Robson, R.M.2    Stromer, M.H.3
  • 127
    • 0037387121 scopus 로고    scopus 로고
    • Crystal structure of CapZ: Structural basis for actin filament barbed end capping
    • Yamashita, A., K. Maeda, and Y. Maeda. 2003. Crystal structure of CapZ: structural basis for actin filament barbed end capping. EMBO J. 22:1529-1538.
    • (2003) EMBO J , vol.22 , pp. 1529-1538
    • Yamashita, A.1    Maeda, K.2    Maeda, Y.3
  • 128
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of alpha-actinin
    • Young, P., C. Ferguson, S. Banuelos, and M. Gautel. 1998. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin. EMBO J. 17:1614-1624.
    • (1998) EMBO J , vol.17 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Banuelos, S.3    Gautel, M.4
  • 129
    • 0018673482 scopus 로고
    • Interaction of alpha-actinin, filamin and tropomyosin with F-actin. Biochim. Biophys
    • Zeece, M.G., R.M. Robson, and P.J. Bechtel. 1979. Interaction of alpha-actinin, filamin and tropomyosin with F-actin. Biochim. Biophys. Acta 581:365-370.
    • (1979) Acta , vol.581 , pp. 365-370
    • Zeece, M.G.1    Robson, R.M.2    Bechtel, P.J.3
  • 131
    • 0034620545 scopus 로고    scopus 로고
    • Binding of troponin I and the troponin I-troponin C complex to actin-tropomysin. Dissociation by myosin subfragment 1
    • Zhou, X., E.P. Morris, and S.S. Lehrer. 2000. Binding of troponin I and the troponin I-troponin C complex to actin-tropomysin. Dissociation by myosin subfragment 1. Biochemistry. 39:1128-1132.
    • (2000) Biochemistry , vol.39 , pp. 1128-1132
    • Zhou, X.1    Morris, E.P.2    Lehrer, S.S.3
  • 132
    • 40649098633 scopus 로고    scopus 로고
    • Three-dimensional structure of vertebrate cardiac muscle myosin filaments
    • Zoghbi, M.E., J.L. Woodhead, R.L. Moss, and R. Craig. 2008. Three-dimensional structure of vertebrate cardiac muscle myosin filaments. Proc. Natl. Acad. Sci. U.S.A. 105:2386-2390.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 2386-2390
    • Zoghbi, M.E.1    Woodhead, J.L.2    Moss, R.L.3    Craig, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.