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Volumn 70, Issue 1, 1996, Pages 430-442

Nonuniform elasticity of titin in cardiac myocytes: A study using immunoelectron microscopy and cellular mechanics

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN;

EID: 0030048904     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79586-3     Document Type: Article
Times cited : (101)

References (57)
  • 1
    • 0025860260 scopus 로고
    • Cardiac myocyte mechanics
    • Brady, A. 1991. Cardiac myocyte mechanics. Physiol. Rev. 71:413-424.
    • (1991) Physiol. Rev. , vol.71 , pp. 413-424
    • Brady, A.1
  • 2
    • 0028028999 scopus 로고
    • Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin
    • Erickson, H. 1994. Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin. Proc. Natl. Acad. Sci. USA. 91:10114-10118.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10114-10118
    • Erickson, H.1
  • 4
    • 85012661423 scopus 로고
    • Details of the I-band structure as revealed by the localization of ferritin
    • Franzini-Armstrong, C. 1970. Details of the I-band structure as revealed by the localization of ferritin. Tissue Cell. 2.327-338.
    • (1970) Tissue Cell , vol.2 , pp. 327-338
    • Franzini-Armstrong, C.1
  • 5
    • 0027318073 scopus 로고
    • Characterization of a partial cDNA clone encoding porcine skeletal muscle titin: Comparison with rabbit and mouse skeletal muscle titin sequences
    • Fritz, J., J. Wolff, and M Greaser. 1993. Characterization of a partial cDNA clone encoding porcine skeletal muscle titin: comparison with rabbit and mouse skeletal muscle titin sequences. Comp. Biochem. Physiol. 105B:357-360.
    • (1993) Comp. Biochem. Physiol. , vol.105 B , pp. 357-360
    • Fritz, J.1    Wolff, J.2    Greaser, M.3
  • 6
    • 0026147304 scopus 로고
    • Titin, a huge, elastic sarcomeric protein with a probable role in morphogenesis
    • Fulton, A., and W. Isaacs. 1991. Titin, a huge, elastic sarcomeric protein with a probable role in morphogenesis. BioEssays. 13:157-161.
    • (1991) BioEssays , vol.13 , pp. 157-161
    • Fulton, A.1    Isaacs, W.2
  • 7
    • 0027448024 scopus 로고
    • Elastic filaments in situ in cardiac muscle: Deep-etch replica analysis in combination with selective removal of actin and myosin filaments
    • Funatsu, T., E. Kono, H. Higuchi, S. Kimura, S. Ishiwata, T. Yoshioka, K. Maruyama. and S. Tsukita. 1993. Elastic filaments in situ in cardiac muscle: deep-etch replica analysis in combination with selective removal of actin and myosin filaments. J. Cell Biol. 120:711-724.
    • (1993) J. Cell Biol. , vol.120 , pp. 711-724
    • Funatsu, T.1    Kono, E.2    Higuchi, H.3    Kimura, S.4    Ishiwata, S.5    Yoshioka, T.6    Maruyama, K.7    Tsukita, S.8
  • 8
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrcpetitive epitopes starting at the Z-line extends close to the M-line
    • Fürst, D., M. Osborn, M. Nave, and K. Weber. 1988. The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrcpetitive epitopes starting at the Z-line extends close to the M-line J. Cell Biol. 106: 1563-1572.
    • (1988) J. Cell Biol. , vol.106 , pp. 1563-1572
    • Fürst, D.1    Osborn, M.2    Nave, M.3    Weber, K.4
  • 9
    • 0028957373 scopus 로고
    • Passive tension in cardiac muscle: Contribution of collagen, titin, microtubules and intermediate filaments
    • Granzier, H. L. M., and T. Irving. 1995. Passive tension in cardiac muscle: contribution of collagen, titin, microtubules and intermediate filaments. Biophys. J. 68:1027-1044.
    • (1995) Biophys. J. , vol.68 , pp. 1027-1044
    • Granzier, H.L.M.1    Irving, T.2
  • 10
    • 0027517018 scopus 로고
    • Interplay between passive tension and strong and weak cross-bridges in insect asynchronous flight muscle: A functional dissection by gelsolin mediated thin filament removal
    • Granzier, H. L. M., and K. Wang. 1993a. Interplay between passive tension and strong and weak cross-bridges in insect asynchronous flight muscle: a functional dissection by gelsolin mediated thin filament removal. J. Gen. Physiol. 101.235-270.
    • (1993) J. Gen. Physiol. , vol.101 , pp. 235-270
    • Granzier, H.L.M.1    Wang, K.2
  • 11
    • 0027511216 scopus 로고
    • Gel electrophoresis of giant proteins: Solubilization and silver staining of titin and nebulin from single muscle fiber segments
    • Granzier, H. L. M., and K. Wang. 1993b. Gel electrophoresis of giant proteins: solubilization and silver staining of titin and nebulin from single muscle fiber segments. Electrophoresis. 14:56-64.
    • (1993) Electrophoresis , vol.14 , pp. 56-64
    • Granzier, H.L.M.1    Wang, K.2
  • 12
    • 0027436282 scopus 로고
    • Passive tension and stiffness of vertebrate skeletal muscle and insect flight muscle: The contribution of weak crossbridges and elastic filaments
    • Granzier, H. L. M., and K. Wang. 1993c. Passive tension and stiffness of vertebrate skeletal muscle and insect flight muscle: the contribution of weak crossbridges and elastic filaments. Biophys. J. 65:2141-2159.
    • (1993) Biophys. J. , vol.65 , pp. 2141-2159
    • Granzier, H.L.M.1    Wang, K.2
  • 13
    • 0026603854 scopus 로고
    • Changes in contractile properties with selective digestion of connectin (titin) in skinned fibers of frog skeletal muscle
    • Higuchi, H. 1992. Changes in contractile properties with selective digestion of connectin (titin) in skinned fibers of frog skeletal muscle. J. Biochem. 111:291-295.
    • (1992) J. Biochem. , vol.111 , pp. 291-295
    • Higuchi, H.1
  • 14
    • 0027488781 scopus 로고
    • Characterization of β-connectin (titin 2) from striated muscle by dynamic light scattering
    • Higuchi, H., N. Nakauchi, K Maruyama. and S. Fujime. 1993. Characterization of β-connectin (titin 2) from striated muscle by dynamic light scattering. Biophys. J. 65:1906-1915.
    • (1993) Biophys. J. , vol.65 , pp. 1906-1915
    • Higuchi, H.1    Nakauchi, N.2    Maruyama, K.3    Fujime, S.4
  • 15
    • 0026634116 scopus 로고
    • Localization and elasticity of connectin filaments in skinned frog muscle fibers subjected to partial depolymerization of thick filaments
    • Higuchi, H., T. Suzuli, S. Kimura, S. Yoshioka, K. Maruyama, and Y. Umazuma. 1992. Localization and elasticity of connectin filaments in skinned frog muscle fibers subjected to partial depolymerization of thick filaments. J. Muscle Res. Cell Motil. 13:285-294.
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 285-294
    • Higuchi, H.1    Suzuli, T.2    Kimura, S.3    Yoshioka, S.4    Maruyama, K.5    Umazuma, Y.6
  • 16
    • 0022476931 scopus 로고
    • Monoclonal antibodies distinguish titins from heart and skeletal muscle
    • Hill, C., and K. Weber. 1986. Monoclonal antibodies distinguish titins from heart and skeletal muscle. J. Cell Biol. 102:1099-1108.
    • (1986) J. Cell Biol. , vol.102 , pp. 1099-1108
    • Hill, C.1    Weber, K.2
  • 17
    • 0026755352 scopus 로고
    • Passive force generation and titin isoforms in mammalian skeletal muscle
    • Horowits, R. 1992. Passive force generation and titin isoforms in mammalian skeletal muscle. Biophys. J. 61:392-398.
    • (1992) Biophys. J. , vol.61 , pp. 392-398
    • Horowits, R.1
  • 18
    • 0023047016 scopus 로고
    • A physiological role for titin and nebulin in skeletal muscle
    • Horowits, R., E. S. Kempner, M. E. Bisher, and R. Podolsky. 1986. A physiological role for titin and nebulin in skeletal muscle. Nature. 323:160-164.
    • (1986) Nature , vol.323 , pp. 160-164
    • Horowits, R.1    Kempner, E.S.2    Bisher, M.E.3    Podolsky, R.4
  • 19
    • 0024426462 scopus 로고
    • Elastic behavior of connectin filaments during thick filament movement in activated skeletal muscle
    • Horowits, R., K. Maruyama, and R. Podolsky. 1989. Elastic behavior of connectin filaments during thick filament movement in activated skeletal muscle J. Cell Biol. 109:2169-2176.
    • (1989) J. Cell Biol. , vol.109 , pp. 2169-2176
    • Horowits, R.1    Maruyama, K.2    Podolsky, R.3
  • 20
    • 0023576830 scopus 로고
    • The positional stability of thick filaments in activated skeletal muscle: Evidence for the role of titin filaments
    • Horowits, R., and R. Podolsky. 1987. The positional stability of thick filaments in activated skeletal muscle: evidence for the role of titin filaments J. Cell Biol. 105:2217-2223.
    • (1987) J. Cell Biol. , vol.105 , pp. 2217-2223
    • Horowits, R.1    Podolsky, R.2
  • 21
    • 0022548661 scopus 로고
    • Sodium dodecyl sulfate gel electrophoresis studies of connectin-like high molecular weight proteins of various types of vertebrate and invertebrate muscles
    • Hu. D., S. Kimura, and K. Maruyama. 1986. Sodium dodecyl sulfate gel electrophoresis studies of connectin-like high molecular weight proteins of various types of vertebrate and invertebrate muscles. J. Biochem. 99.1485-1492
    • (1986) J. Biochem. , vol.99 , pp. 1485-1492
    • Hu, D.1    Kimura, S.2    Maruyama, K.3
  • 22
    • 0023756132 scopus 로고
    • Extensible and less-extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies
    • Itoh. Y., T. Suzuki, S. Kimura, K. Ohashi, H. Higuchi, H Sawada, T. Shinizu, M. Shibata, and K. Maruyama. 1988. Extensible and less-extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies. J. Biochem. 104: 504-508.
    • (1988) J. Biochem. , vol.104 , pp. 504-508
    • Itoh, Y.1    Suzuki, T.2    Kimura, S.3    Ohashi, K.4    Higuchi, H.5    Sawada, H.6    Shinizu, T.7    Shibata, M.8    Maruyama, K.9
  • 23
    • 0028918871 scopus 로고
    • Cloned rat cardiac titin class I and class II motifs: Expression, purification, characterization, and interaction with F-actin
    • Jin, J.-P. 1995. Cloned rat cardiac titin class I and class II motifs: expression, purification, characterization, and interaction with F-actin. J Biol. Chem. 270(12):6908-6916.
    • (1995) J Biol. Chem. , vol.270 , Issue.12 , pp. 6908-6916
    • Jin, J.-P.1
  • 24
    • 0026008748 scopus 로고
    • Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: Correlation of thin filament length, nebulin size, and epitope profile
    • Kruger, M., J. Wright, and K. Wang. 1991. Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: correlation of thin filament length, nebulin size, and epitope profile. J Cell Biol. 115: 97-107.
    • (1991) J Cell Biol. , vol.115 , pp. 97-107
    • Kruger, M.1    Wright, J.2    Wang, K.3
  • 25
    • 0023872824 scopus 로고
    • Giant polypeptides of skeletal muscle titin: Sedimentation equilibrium in guanidine hydrochloride
    • Kurzban, G., and K. Wang. 1988. Giant polypeptides of skeletal muscle titin: sedimentation equilibrium in guanidine hydrochloride. Biochem. Biophys. Res. Commun. 150:1155-1161.
    • (1988) Biochem. Biophys. Res. Commun. , vol.150 , pp. 1155-1161
    • Kurzban, G.1    Wang, K.2
  • 26
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Anderson, J. 1984 Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods. 10:203-209.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 203-209
    • Kyhse-Anderson, J.1
  • 28
    • 0026582867 scopus 로고
    • Towards a molecular understanding of titin
    • Labeit, S., M. Gautel, A. Lackey, and J. Trinick. 1992. Towards a molecular understanding of titin. EMBO J. 11:1711-1716.
    • (1992) EMBO J. , vol.11 , pp. 1711-1716
    • Labeit, S.1    Gautel, M.2    Lackey, A.3    Trinick, J.4
  • 29
    • 0027934071 scopus 로고
    • Passive and active tension in single cardiac myofibrils
    • Linke. W., V. Popov, and G, Pollack. 1994. Passive and active tension in single cardiac myofibrils. Biophys. J. 67:782-792.
    • (1994) Biophys. J. , vol.67 , pp. 782-792
    • Linke, W.1    Popov, V.2    Pollack, G.3
  • 30
    • 0022487438 scopus 로고
    • Connectin an elastic filamentous protein of striated muscle
    • Maruyama, K. 1986. Connectin an elastic filamentous protein of striated muscle. Int. Rev. Cytol. 104:81-114.
    • (1986) Int. Rev. Cytol. , vol.104 , pp. 81-114
    • Maruyama, K.1
  • 31
    • 0028289058 scopus 로고
    • Connectin, an elastic protein of striated muscle
    • Maruyama, K. 1994. Connectin, an elastic protein of striated muscle. Biophys. Chem. 50:73-85.
    • (1994) Biophys. Chem. , vol.50 , pp. 73-85
    • Maruyama, K.1
  • 33
    • 0021279759 scopus 로고
    • Molecular size and shape of β-connectin, an elastic protein of striated muscle
    • Maruyama, K., S. Kimura, H. Yoshidomi, H. Sawada, and M. Kikuchi. 1984. Molecular size and shape of β-connectin, an elastic protein of striated muscle. J. Biochem. 95:1423-1433.
    • (1984) J. Biochem. , vol.95 , pp. 1423-1433
    • Maruyama, K.1    Kimura, S.2    Yoshidomi, H.3    Sawada, H.4    Kikuchi, M.5
  • 34
    • 0015090563 scopus 로고
    • Stereological measurements of cardiac ultrastructures implicated in excitation-contraction coupling
    • Page, S., L. McCallister, and B. Power. 1971. Stereological measurements of cardiac ultrastructures implicated in excitation-contraction coupling. Proc. Natl. Acad. Sci. USA. 68:1464-1466
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1464-1466
    • Page, S.1    McCallister, L.2    Power, B.3
  • 35
    • 0028069866 scopus 로고
    • Isolation and characterization of titin T1 from bovine cardiac muscle
    • Pan, K , S. Damodaran, and M. Greaser. 1994. Isolation and characterization of titin T1 from bovine cardiac muscle. Biochemistry. 33: 8255-8261.
    • (1994) Biochemistry , vol.33 , pp. 8255-8261
    • Pan, K.1    Damodaran, S.2    Greaser, M.3
  • 36
    • 0024796965 scopus 로고
    • The organization of titin (connectin) and nebulin in the sarcomeres: An immunocytolocalization study
    • Pierobon-Bormioli, S., R. Betto, and G. Salviati. 1989. The organization of titin (connectin) and nebulin in the sarcomeres: an immunocytolocalization study. J. Muscle Res. Cell Motil. 10:446-456.
    • (1989) J. Muscle Res. Cell Motil. , vol.10 , pp. 446-456
    • Pierobon-Bormioli, S.1    Betto, R.2    Salviati, G.3
  • 37
    • 0026665940 scopus 로고
    • A method to reconstruct myocardial sarcomere lengths and orientations at transmural sites in beating canine hearts
    • Rodriguez, E., W. Hunter, M. Royce, M. Leppo, A. Douglas, and H. Weisman. 1992. A method to reconstruct myocardial sarcomere lengths and orientations at transmural sites in beating canine hearts. Am. J. Physiol. 263:H293-H306.
    • (1992) Am. J. Physiol. , vol.263
    • Rodriguez, E.1    Hunter, W.2    Royce, M.3    Leppo, M.4    Douglas, A.5    Weisman, H.6
  • 38
    • 0024503656 scopus 로고
    • Stiffness and shortening changes in myofilament-extracted rat cardiac myocytes
    • Roos, K., and A. Brady, 1989. Stiffness and shortening changes in myofilament-extracted rat cardiac myocytes. Am. J. Physiol. 256:H539-H551.
    • (1989) Am. J. Physiol. , vol.256
    • Roos, K.1    Brady, A.2
  • 40
    • 4243405097 scopus 로고
    • Characterization of a novel 5.4-kb cDNA fragment coding for the amino-terminal region of rabbit cardiac titin
    • Sebestyén, M., J. Wolff, and M. Greaser. 1995. Characterization of a novel 5.4-kb cDNA fragment coding for the amino-terminal region of rabbit cardiac titin. Biophys. J. 68:A65.
    • (1995) Biophys. J. , vol.68
    • Sebestyén, M.1    Wolff, J.2    Greaser, M.3
  • 41
    • 0022519194 scopus 로고
    • Enhancement of immunoblot sensitivity by heating of hydrated filters
    • Swerdlow, P., D. Finley, and A. Varshavsky. 1986. Enhancement of immunoblot sensitivity by heating of hydrated filters. Ann. Biochem. 156:147-153.
    • (1986) Ann. Biochem. , vol.156 , pp. 147-153
    • Swerdlow, P.1    Finley, D.2    Varshavsky, A.3
  • 42
    • 0027787483 scopus 로고
    • Connectin content in rabbit cardiac and skeletal muscle
    • Suzuki, J., S. Kimura, and K. Maruyama. 1993. Connectin content in rabbit cardiac and skeletal muscle. Int. J. Biochem. 25:1853-1858.
    • (1993) Int. J. Biochem. , vol.25 , pp. 1853-1858
    • Suzuki, J.1    Kimura, S.2    Maruyama, K.3
  • 43
    • 0028017499 scopus 로고
    • Electron microscopic filament lengths of connectin and its fragments
    • Suzuki, J., S. Kimura, and K. Maruyama. 1994. Electron microscopic filament lengths of connectin and its fragments. J. Biochem. 116: 406-410.
    • (1994) J. Biochem. , vol.116 , pp. 406-410
    • Suzuki, J.1    Kimura, S.2    Maruyama, K.3
  • 44
    • 0025877737 scopus 로고
    • Elastic filaments and giant proteins in muscle
    • Trinick, J. 1991. Elastic filaments and giant proteins in muscle. Curr. Opin. Cell Biol. 3:112-118.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 112-118
    • Trinick, J.1
  • 45
    • 0021591504 scopus 로고
    • Purification and properties of native titin
    • Trinick, J., P. Knight and A. Whiting. 1984. Purification and properties of native titin. J. Mol. Biol 180:331-356.
    • (1984) J. Mol. Biol , vol.180 , pp. 331-356
    • Trinick, J.1    Knight, P.2    Whiting, A.3
  • 47
    • 0027313537 scopus 로고
    • Elastic properties of the titin filament in the Z-line region of vertebrate striated muscle
    • Trombitás, K., and G. Pollack. 1993. Elastic properties of the titin filament in the Z-line region of vertebrate striated muscle. J. Muscle Res. Cell Motil 14:416-422.
    • (1993) J. Muscle Res. Cell Motil , vol.14 , pp. 416-422
    • Trombitás, K.1    Pollack, G.2
  • 48
    • 0027447329 scopus 로고
    • Elastic properties of the titin filaments demonstrated using a "freeze-break" technique
    • Trombitás, K., G. Pollack, J. Wright, and K. Wang. 1993. Elastic properties of the titin filaments demonstrated using a "freeze-break" technique. Cell Motil. Cytoskeleton. 24:274-283.
    • (1993) Cell Motil. Cytoskeleton. , vol.24 , pp. 274-283
    • Trombitás, K.1    Pollack, G.2    Wright, J.3    Wang, K.4
  • 49
    • 0002236823 scopus 로고
    • Fine structure and mechanical properties of insect muscle
    • R. Tregear, editor. North-Holland Publishing., Amsterdam
    • Trombitás, K., and A. Tigyi-Sebes. 1977. Fine structure and mechanical properties of insect muscle. In Insect Flight Muscle. R. Tregear, editor. North-Holland Publishing., Amsterdam. 79-90.
    • (1977) Insect Flight Muscle , pp. 79-90
    • Trombitás, K.1    Tigyi-Sebes, A.2
  • 50
    • 0021982444 scopus 로고
    • Sarcomere-associated cytoskeletal lattices in striated muscle
    • Wang, K. 1985. Sarcomere-associated cytoskeletal lattices in striated muscle. Cell Muscle Motil. 6:315-369.
    • (1985) Cell Muscle Motil. , vol.6 , pp. 315-369
    • Wang, K.1
  • 52
    • 0027189534 scopus 로고
    • Viscoelasticity of the sarcomere matrix of skeletal muscles: The titin-myosin composite filament is a dual-range molecular spring
    • Wang, K., R. McCarter, J. Wright, B. Jennate, and R. Ramirez-Mitchell. 1993. Viscoelasticity of the sarcomere matrix of skeletal muscles: the titin-myosin composite filament is a dual-range molecular spring Biophys. J. 64:1161-1177.
    • (1993) Biophys. J. , vol.64 , pp. 1161-1177
    • Wang, K.1    McCarter, R.2    Wright, J.3    Jennate, B.4    Ramirez-Mitchell, R.5
  • 53
    • 9044245846 scopus 로고
    • Architecture of the titin/nebulin containing cytoskeletal lattice of the striated muscle sarcomere: Evidence of elastic and inelastic domains of the bipolar filaments
    • Wang, K., J. Wright, and R. Ramirez-Mitchell. 1984a. Architecture of the titin/nebulin containing cytoskeletal lattice of the striated muscle sarcomere: evidence of elastic and inelastic domains of the bipolar filaments. J. Cell Biol. 99(4, Pt. 2):435a.
    • (1984) J. Cell Biol. , vol.99 , Issue.4 PART 2
    • Wang, K.1    Wright, J.2    Ramirez-Mitchell, R.3
  • 54
    • 0021452202 scopus 로고
    • Titin is an extraordinarily long, flexible, and slender myofibrillar protein
    • Wang. K., R. Ramirez-Mitchell, and D. Palter. 1984b. Titin is an extraordinarily long, flexible, and slender myofibrillar protein. Proc. Natl. Acad. Sci. USA. 81:3685-3689.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3685-3689
    • Wang, K.1    Ramirez-Mitchell, R.2    Palter, D.3
  • 55
    • 0022079716 scopus 로고
    • Immunocytochemical studies using a monoclonal antibody to bovine cardiac titin on intact and extracted myofibrils
    • Wang, S.-M., and M. Greaser. 1985. Immunocytochemical studies using a monoclonal antibody to bovine cardiac titin on intact and extracted myofibrils. J. Muscle Res. Cell Motil 6:293-312.
    • (1985) J. Muscle Res. Cell Motil , vol.6 , pp. 293-312
    • Wang, S.-M.1    Greaser, M.2
  • 56
    • 0024961666 scopus 로고
    • Does titin regulate the length of muscle thick filaments?
    • Whiting, A., J. Wardale, and J. Trinick. 1989. Does titin regulate the length of muscle thick filaments? J. Mol. Biol. 205:163-169.
    • (1989) J. Mol. Biol. , vol.205 , pp. 163-169
    • Whiting, A.1    Wardale, J.2    Trinick, J.3
  • 57
    • 0022646981 scopus 로고
    • Effects of mild trypsin treatment on the passive tension generation and connectin splitting in stretched, skinned fibers from frog skeletal muscle
    • Yoshioka, T., H. Higuchi, S. Kimura, K. Ohashi, Y. Umazume, and K. Maruyama. 1986. Effects of mild trypsin treatment on the passive tension generation and connectin splitting in stretched, skinned fibers from frog skeletal muscle. Biomed. Res. 7:181-186.
    • (1986) Biomed. Res. , vol.7 , pp. 181-186
    • Yoshioka, T.1    Higuchi, H.2    Kimura, S.3    Ohashi, K.4    Umazume, Y.5    Maruyama, K.6


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