메뉴 건너뛰기




Volumn 387, Issue 6630, 1997, Pages 308-312

Elasticity and unfolding of single molecules of the giant muscle protein titin

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN;

EID: 0031006659     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/387308a0     Document Type: Article
Times cited : (685)

References (26)
  • 1
    • 0030091595 scopus 로고    scopus 로고
    • Cytoskeleton: Titin as a scaffold and spring
    • Trinick, J. Cytoskeleton: titin as a scaffold and spring. Curr. Biol. 6, 258-260 (1996).
    • (1996) Curr. Biol. , vol.6 , pp. 258-260
    • Trinick, J.1
  • 2
    • 0028289058 scopus 로고
    • Connectin, an elastic protein of striated muscle
    • Maruyama, K. Connectin, an elastic protein of striated muscle. Biophys. Chem. 50, 73-85 (1994).
    • (1994) Biophys. Chem. , vol.50 , pp. 73-85
    • Maruyama, K.1
  • 3
    • 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, 293-296 (1995).
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 4
    • 0030576501 scopus 로고    scopus 로고
    • Towards a molecular understanding of the elasticity of titin
    • Linke, W. A. et al. Towards a molecular understanding of the elasticity of titin. J. Mol. Biol. 261, 62-71 (1996).
    • (1996) J. Mol. Biol. , vol.261 , pp. 62-71
    • Linke, W.A.1
  • 5
    • 0029882110 scopus 로고    scopus 로고
    • A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
    • Gautel, M. & Goulding, D. A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series. FEBS Lett. 385, 11-14 (1996).
    • (1996) FEBS Lett. , vol.385 , pp. 11-14
    • Gautel, M.1    Goulding, D.2
  • 6
    • 0027488781 scopus 로고
    • Characterization of α-connectin from striated muscle by dynamic light scattering
    • Higuchi, H., Nakauchi, Y., Maruyama, K. & Fujime, S. Characterization of α-connectin from striated muscle by dynamic light scattering. Biophys. J. 65, 1906-1915 (1993).
    • (1993) Biophys. J. , vol.65 , pp. 1906-1915
    • Higuchi, H.1    Nakauchi, Y.2    Maruyama, K.3    Fujime, S.4
  • 7
    • 0027189534 scopus 로고
    • Viscoelasticity of the sarcomere matrix of skeletal-muscles: The titin-myosin composite filament is a dual-stage molecular spring
    • Wang, K., McCarter, R., Wright, J., Beverly, J. & Ramirez-Mitchell, R. Viscoelasticity of the sarcomere matrix of skeletal-muscles: the titin-myosin composite filament is a dual-stage molecular spring. Biophys. J. 64, 1161-1177 (1993).
    • (1993) Biophys. J. , vol.64 , pp. 1161-1177
    • Wang, K.1    McCarter, R.2    Wright, J.3    Beverly, J.4    Ramirez-Mitchell, R.5
  • 9
    • 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, 10114-10118 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10114-10118
    • Erickson, H.P.1
  • 10
    • 0028834886 scopus 로고
    • The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity
    • Politou, A. S., Thomas, D. J. & Pastore, A. The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity. Biophys. J. 69, 2601-2610 (1995).
    • (1995) Biophys. J. , vol.69 , pp. 2601-2610
    • Politou, A.S.1    Thomas, D.J.2    Pastore, A.3
  • 12
    • 36849115224 scopus 로고
    • Polymer conformational statistics. III. Modified Gaussian models of stiff chains
    • Fixman, M. & Kovac, J. Polymer conformational statistics. III. Modified Gaussian models of stiff chains. J. Chem. Phys. 56, 1564-1568 (1973).
    • (1973) J. Chem. Phys. , vol.56 , pp. 1564-1568
    • Fixman, M.1    Kovac, J.2
  • 13
    • 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. Elastic properties of single titin molecules made visible through fluorescent F-actin binding. Biochem. Biophys. Res. Comm. 221, 491-497 (1996).
    • (1996) Biochem. Biophys. Res. Comm. , vol.221 , pp. 491-497
    • Kellermayer, M.S.Z.1    Granzier, H.L.2
  • 15
    • 0028347588 scopus 로고
    • Immunoglobulin-type domains of titin: Same fold, different stability?
    • Politou, A. S., Gautel, M., Pfuhl, M., Labeit, S. & Pastore, A. Immunoglobulin-type domains of titin: same fold, different stability? Biochemistry 33, 4730-4737 (1994).
    • (1994) Biochemistry , vol.33 , pp. 4730-4737
    • Politou, A.S.1    Gautel, M.2    Pfuhl, M.3    Labeit, S.4    Pastore, A.5
  • 16
    • 0030573054 scopus 로고    scopus 로고
    • Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans
    • Fong, S. et al. Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J. Mol. Biol. 264, 624-639 (1996).
    • (1996) J. Mol. Biol. , vol.264 , pp. 624-639
    • Fong, S.1
  • 17
    • 0026575457 scopus 로고
    • Reversible unfolding of an isolated heparin and DNA binding fragment, the first type III module from fibronectin
    • Litvinovich, S. V., Novokhatny, V. V., Brew, S. A. & Ingram, K. C. Reversible unfolding of an isolated heparin and DNA binding fragment, the first type III module from fibronectin. Biochim. Biophys. Acta 1119, 57-62 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1119 , pp. 57-62
    • Litvinovich, S.V.1    Novokhatny, V.V.2    Brew, S.A.3    Ingram, K.C.4
  • 18
    • 0029763434 scopus 로고    scopus 로고
    • Rapid refolding of a proline-rich all-beta-sheet fibronectin type-III module
    • Plaxco, K. W., Spitzfaden, C., Campbell, I. D. & Dobson, C. M. Rapid refolding of a proline-rich all-beta-sheet fibronectin type-III module. Proc. Natl Acad. Sci. USA 93, 10703-10706 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10703-10706
    • Plaxco, K.W.1    Spitzfaden, C.2    Campbell, I.D.3    Dobson, C.M.4
  • 19
    • 0027536473 scopus 로고
    • A survey of the interactions made by the giant protein titin
    • Soteriou, A., Gamage, M. & Trinick, J. A survey of the interactions made by the giant protein titin. J. Cell Sci. 104, 119-123 (1993).
    • (1993) J. Cell Sci. , vol.104 , pp. 119-123
    • Soteriou, A.1    Gamage, M.2    Trinick, J.3
  • 20
    • 0024961666 scopus 로고
    • Does titin regulate the length of muscle thick filaments
    • Whiting, J., Wardale, J. & Trinick, J. Does titin regulate the length of muscle thick filaments. J. Mol. Biol. 205, 263-268 (1989).
    • (1989) J. Mol. Biol. , vol.205 , pp. 263-268
    • Whiting, J.1    Wardale, J.2    Trinick, J.3
  • 21
    • 0023924769 scopus 로고
    • The organisation 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 organisation 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, 1563-1572 (1988).
    • (1988) J. Cell Biol. , vol.106 , pp. 1563-1572
    • Fürst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 22
    • 0029976424 scopus 로고    scopus 로고
    • Quantitative measurements of force and displacement using an optical trap
    • Simmons, R. M., Finer, J. T., Chu, S. & Spudich, J. A. Quantitative measurements of force and displacement using an optical trap. Biophys. J. 70, 1813-1822 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 1813-1822
    • Simmons, R.M.1    Finer, J.T.2    Chu, S.3    Spudich, J.A.4
  • 23
    • 0028071373 scopus 로고
    • Entropic elasticity of λ-phage DNA
    • Bustamante, C. Entropic elasticity of λ-phage DNA. Science 265, 1599-1600 (1994).
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1
  • 24
    • 0031575403 scopus 로고    scopus 로고
    • Direct visualization of extensibility in isolated titin molecules
    • Tskhovrebova, L. & Trinick, J. Direct visualization of extensibility in isolated titin molecules. J. Mol. Biol. 265, 100-106 (1997).
    • (1997) J. Mol. Biol. , vol.265 , pp. 100-106
    • Tskhovrebova, L.1    Trinick, J.2
  • 26
    • 1842350276 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with force-measuring laser tweezers
    • in the press
    • Kellermayer, M. S. Z., Smith, S. B., Granzier, H. L. & Bustamante, C. Folding-unfolding transitions in single titin molecules characterized with force-measuring laser tweezers. Science (in the press).
    • Science
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.