메뉴 건너뛰기




Volumn 122, Issue 1-2, 1998, Pages 197-205

Complete unfolding of the titin molecule under external force

Author keywords

Force measuring laser tweezer; Single molecule manipulation; Titin; Unfolding refolding; Wormlike chain

Indexed keywords

CONNECTIN;

EID: 0031711834     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.3988     Document Type: Article
Times cited : (61)

References (39)
  • 1
    • 0030604697 scopus 로고    scopus 로고
    • Titin domain patterns correlate with the axial disposition of myosin at the end of the thick filament
    • Bennett P. M., Gautel M. Titin domain patterns correlate with the axial disposition of myosin at the end of the thick filament. J. Mol. Biol. 259:1996;896-903.
    • (1996) J. Mol. Biol. , vol.259 , pp. 896-903
    • Bennett, P.M.1    Gautel, M.2
  • 3
    • 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. P. 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. 91:1994;10114-10118.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10114-10118
    • Erickson, H.P.1
  • 4
    • 0030052266 scopus 로고    scopus 로고
    • A molecular map of the interactions between titin and myosin-binding protein C: Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • Freiburg A., Gautel M. A molecular map of the interactions between titin and myosin-binding protein C: Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur. J. Biochem. 235:1996;317-323.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 6
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z line extends close to the M line
    • Fürst D. O., Osborn M., Nave R., Weber K. The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z line extends close to the M line. J. Cell. Biol. 106:1988;1563-1572.
    • (1988) J. Cell. Biol. , vol.106 , pp. 1563-1572
    • Fürst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 7
    • 0030855930 scopus 로고    scopus 로고
    • Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction
    • Granzier H. L., Kellermayer M., Helmes M., Trombitás K. Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction. Biophys. J. 73:1997;2043-2053.
    • (1997) Biophys. J. , vol.73 , pp. 2043-2053
    • Granzier, H.L.1    Kellermayer, M.2    Helmes, M.3    Trombitás, K.4
  • 8
    • 0025774399 scopus 로고
    • Effect of thin filament length on the force-sarcomere length relation of skeletal muscle
    • Granzier H. L. M., Akster H. A., ter Keurs H. E. D. J. Effect of thin filament length on the force-sarcomere length relation of skeletal muscle. Am. J. Physiol. 260:1991;C1060-C1070.
    • (1991) Am. J. Physiol. , vol.260
    • Granzier, H.L.M.1    Akster, H.A.2    Ter Keurs, H.E.D.J.3
  • 9
    • 0028957373 scopus 로고
    • Passive tension in cardiac muscle: The contribution of collagen, titin, microtubules and intermediate filaments
    • Granzier H. L. M., Irving T. Passive tension in cardiac muscle: The contribution of collagen, titin, microtubules and intermediate filaments. Biophys. J. 68:1995;1027-1044.
    • (1995) Biophys. J. , vol.68 , pp. 1027-1044
    • Granzier, H.L.M.1    Irving, T.2
  • 10
    • 0027488781 scopus 로고
    • Characterization of beta-connectin (titin 2) from striated muscle by dynamic light scattering
    • Higuchi H., Nakauchi Y., Maruyama K., Fujime S. Characterization of beta-connectin (titin 2) from striated muscle by dynamic light scattering. Biophys. J. 65:1993;1906-1915.
    • (1993) Biophys. J. , vol.65 , pp. 1906-1915
    • Higuchi, H.1    Nakauchi, Y.2    Maruyama, K.3    Fujime, S.4
  • 11
    • 0026634116 scopus 로고
    • Localization and elasticity of connectin (titin) filaments in skinned frog muscle fibres subjected to partial depolymerization of thick filaments
    • Higuchi H., Suzuki T., Kimura S., Yoshioka T., Maruyama K., Umazume Y. Localization and elasticity of connectin (titin) filaments in skinned frog muscle fibres subjected to partial depolymerization of thick filaments. J. Muscle Res. Cell Motil. 13:1992;285-294.
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 285-294
    • Higuchi, H.1    Suzuki, T.2    Kimura, S.3    Yoshioka, T.4    Maruyama, K.5    Umazume, Y.6
  • 12
    • 0023047016 scopus 로고
    • A physiological role for titin and nebulin in skeletal muscle
    • Horowits R., Kempner E. S., Bisher M. E., Podolsky R. J. A physiological role for titin and nebulin in skeletal muscle. Nature. 323:1986;160-164.
    • (1986) Nature , vol.323 , pp. 160-164
    • Horowits, R.1    Kempner, E.S.2    Bisher, M.E.3    Podolsky, R.J.4
  • 13
    • 0023576830 scopus 로고
    • The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: Evidence for the role of titin filaments
    • Horowits R., Podolsky R. J. The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: Evidence for the role of titin filaments. J. Cell Biol. 105:1987;2217-2223.
    • (1987) J. Cell Biol. , vol.105 , pp. 2217-2223
    • Horowits, R.1    Podolsky, R.J.2
  • 15
    • 0023756132 scopus 로고
    • Extensible and less-extensible domains of connection filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies
    • Itoh Y., Suzuki T., Kimura S., Ohashi K., Higuchi H., Sawada H., Shimizu T., Shibata M., Maruyama K. Extensible and less-extensible domains of connection filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies. J. Biochem. 104:1988;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    Shimizu, T.7    Shibata, M.8    Maruyama, K.9
  • 16
    • 0344657025 scopus 로고    scopus 로고
    • Correlating titin isoform expression with mechanical properties of cardiac and skeletal myofibrils
    • Ivemeyer M., Olivieri N., Freiburg A., Kolmerer B., Labeit S., Linke W. A. Correlating titin isoform expression with mechanical properties of cardiac and skeletal myofibrils. Biophys. J. 72:1997;A281.
    • (1997) Biophys. J. , vol.72 , pp. 281
    • Ivemeyer, M.1    Olivieri, N.2    Freiburg, A.3    Kolmerer, B.4    Labeit, S.5    Linke, W.A.6
  • 17
    • 0030022007 scopus 로고    scopus 로고
    • Calcium dependent inhibition of in vitro thin-filament motility by native titin
    • Kellermayer M. S. Z., Granzier H. L. M. Calcium dependent inhibition of in vitro thin-filament motility by native titin. FEBS Lett. 380:1996a;281-286.
    • (1996) FEBS Lett. , vol.380 , pp. 281-286
    • Kellermayer, M.S.Z.1    Granzier, H.L.M.2
  • 18
    • 0029886571 scopus 로고    scopus 로고
    • Elastic properties of single titin molecules made visible through fluorescent F-actin binding
    • Kellermayer M. S. Z., Granzier H. L. M. Elastic properties of single titin molecules made visible through fluorescent F-actin binding. Biochem. Biophys. Res. Commun. 221:1996b;491-497.
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 491-497
    • Kellermayer, M.S.Z.1    Granzier, H.L.M.2
  • 19
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer M. S. Z., Smith S. B., Granzier H. L., Bustamante C. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science. 276:1997;1112-1116.
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 20
    • 0026582867 scopus 로고
    • Towards a molecular understanding of titin
    • Labeit S., Gautel M., Lakey A., Trinick J. Towards a molecular understanding of titin. EMBO J. 11:1992;1711-1716.
    • (1992) EMBO J. , vol.11 , pp. 1711-1716
    • Labeit, S.1    Gautel, M.2    Lakey, A.3    Trinick, J.4
  • 21
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S., Kolmerer B. Titins: Giant proteins in charge of muscle ultrastructure and elasticity. Science. 270:1995;293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 23
    • 0030982846 scopus 로고    scopus 로고
    • Connectin/titin, giant elastic protein of muscle
    • Maruyama K. Connectin/titin, giant elastic protein of muscle. FASEB J. 11:1997;341-345.
    • (1997) FASEB J. , vol.11 , pp. 341-345
    • Maruyama, K.1
  • 24
    • 0028838439 scopus 로고
    • Purification and biochemical characterization of myomesin, a myosin-binding and titin-binding protein, from bovine skeletal muscle
    • Obermann W. J., Plessmann U., Weber K., Fürst D. O. Purification and biochemical characterization of myomesin, a myosin-binding and titin-binding protein, from bovine skeletal muscle. Eur. J. Biochem. 233:1995;110-115.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 110-115
    • Obermann, W.J.1    Plessmann, U.2    Weber, K.3    Fürst, D.O.4
  • 25
    • 0029836627 scopus 로고    scopus 로고
    • The structure of the sarcomeric M band: Localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy
    • Obermann W. M. J., Gautel M., Steiner F., van der Ven P. F. M., Weber K., Fürst D. O. The structure of the sarcomeric M band: Localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy. J. Cell Biol. 134:1996;1441-1453.
    • (1996) J. Cell Biol. , vol.134 , pp. 1441-1453
    • Obermann, W.M.J.1    Gautel, M.2    Steiner, F.3    Van Der Ven, P.F.M.4    Weber, K.5    Fürst, D.O.6
  • 26
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M., Gautel M., Oesterhelt F., Fernandez J. M., Gaub H. E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1997;1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 27
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules
    • Smith S. B., Cui Y., Bustamante C. Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules. Science. 271:1996;795-799.
    • (1996) Science , vol.271 , pp. 795-799
    • Smith, S.B.1    Cui, Y.2    Bustamante, C.3
  • 31
    • 0025877737 scopus 로고
    • Elastic filaments and giant proteins in muscle
    • Trinick J. Elastic filaments and giant proteins in muscle. Curr. Opin. Cell Biol. 3:1991;112-118.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 112-118
    • Trinick, J.1
  • 32
    • 0030091595 scopus 로고    scopus 로고
    • Cytoskeleton: Titin as a scaffold and spring
    • Trinick J. Cytoskeleton: Titin as a scaffold and spring. Curr. Biol. 6:1996;258-260.
    • (1996) Curr. Biol. , vol.6 , pp. 258-260
    • Trinick, J.1
  • 33
    • 0032559640 scopus 로고    scopus 로고
    • Titin extensibility in situ: Entropic elasticity of permanently folded and permanently unfolded molecular segments
    • Trombitás K., Greaser M., Labeit S., Jin J.-P., Kellermayer M., Helmes M., Granzier H. Titin extensibility in situ: Entropic elasticity of permanently folded and permanently unfolded molecular segments. J. Cell Biol. 140:1998;1-7.
    • (1998) J. Cell Biol. , vol.140 , pp. 1-7
    • Trombitás, K.1    Greaser, M.2    Labeit, S.3    Jin, J.-P.4    Kellermayer, M.5    Helmes, M.6    Granzier, H.7
  • 34
    • 0029143981 scopus 로고
    • The mechanically active domain of titin in cardiac muscle
    • Trombitás K., Jin J.-P., Granzier H. L. The mechanically active domain of titin in cardiac muscle. Circ. Res. 77:1995;856-861.
    • (1995) Circ. Res. , vol.77 , pp. 856-861
    • Trombitás, K.1    Jin, J.-P.2    Granzier, H.L.3
  • 35
    • 0027313537 scopus 로고
    • Elastic properties of the titin filament in the Z-line region of vertebrate striated muscle
    • Trombitás K., Pollack G. H. Elastic properties of the titin filament in the Z-line region of vertebrate striated muscle. J. Muscle Res. Cell Motil. 14:1993;416-422.
    • (1993) J. Muscle Res. Cell Motil. , vol.14 , pp. 416-422
    • Trombitás, K.1    Pollack, G.H.2
  • 36
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • Tskhovrebova L., Trinick J., Sleep J. A., Simmons R. M. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature. 387:1997;308-312.
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 37
    • 0029805084 scopus 로고    scopus 로고
    • Titin/connectin and nebulin: Giant protein rulers of muscle structure and function
    • Wang K. Titin/connectin and nebulin: giant protein rulers of muscle structure and function. Adv. Biophys. 33:1996;123-134.
    • (1996) Adv. Biophys. , vol.33 , pp. 123-134
    • Wang, K.1
  • 38
    • 0021452202 scopus 로고
    • Titin is an extraordinarily long, flexible, and slender myofibrillar protein
    • Wang K., Ramirez M. R., Palter D. Titin is an extraordinarily long, flexible, and slender myofibrillar protein. Proc. Natl. Acad. Sci. USA. 81:1984;3685-3689.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3685-3689
    • Wang, K.1    Ramirez, M.R.2    Palter, D.3
  • 39
    • 0024961666 scopus 로고
    • Does titin regulate the length of muscle thick filaments
    • Whiting A., Wardale J., Trinick J. Does titin regulate the length of muscle thick filaments. J. Mol. Biol. 205:1989;263-268.
    • (1989) J. Mol. Biol. , vol.205 , pp. 263-268
    • Whiting, A.1    Wardale, J.2    Trinick, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.