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Volumn 422, Issue 6930, 2003, Pages 446-449

Hidden complexity in the mechanical properties of titin

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; ELASTICITY; IMMUNOLOGY; MUSCLE; PHYSIOLOGY;

EID: 0037468835     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01517     Document Type: Article
Times cited : (241)

References (30)
  • 1
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal-antibodies in immunoelectron microscopy - A map of 10 nonrepetitive epitopes starting at the Z-line extends close to the M-line
    • Furst, 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 10 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
    • Furst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 2
    • 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, 1711-1716 (1992).
    • (1992) EMBO J. , vol.11 , pp. 1711-1716
    • Labeit, S.1    Gautel, M.2    Lakey, A.3    Trinick, J.4
  • 3
    • 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
  • 4
    • 0031809493 scopus 로고    scopus 로고
    • Characterizing titin's I-band Ig domain region as an entropic spring
    • Linke, W. A., Stockmeier, M. R., Ivemeyer, M., Hosser, H. & Mundel, P. Characterizing titin's I-band Ig domain region as an entropic spring. J. Cell Sci. 111, 1567-1574 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 1567-1574
    • Linke, W.A.1    Stockmeier, M.R.2    Ivemeyer, M.3    Hosser, H.4    Mundel, P.5
  • 5
    • 0033616713 scopus 로고    scopus 로고
    • Mechanical and chemical unfolding of a single protein: A comparison
    • Carrion-Vazquez, M. et al. Mechanical and chemical unfolding of a single protein: A comparison. Proc. Natl Acad. Sci. USA 96, 3694-3699 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3694-3699
    • Carrion-Vazquez, M.1
  • 6
    • 0033523904 scopus 로고    scopus 로고
    • Mechanical unfolding intermediates in titin modules
    • Marszalek, P. E. et al. Mechanical unfolding intermediates in titin modules. Nature 402, 100-103 (1999).
    • (1999) Nature , vol.402 , pp. 100-103
    • Marszalek, P.E.1
  • 8
    • 0036280490 scopus 로고    scopus 로고
    • The effect of core destabilization on the mechanical resistance of I 27
    • Brockwell, D. J. et al. The effect of core destabilization on the mechanical resistance of I27. Biophys. J. 83, 458-472 (2002).
    • (2002) Biophys. J. , vol.83 , pp. 458-472
    • Brockwell, D.J.1
  • 9
    • 0036389817 scopus 로고    scopus 로고
    • Mechanical unfolding of a titin Ig domain: Structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering
    • Fowler, S. B. et al. Mechanical unfolding of a titin Ig domain: Structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering. J. Mol. Biol. 322, 841-849 (2002).
    • (2002) J. Mol. Biol. , vol.322 , pp. 841-849
    • Fowler, S.B.1
  • 10
    • 0037194788 scopus 로고    scopus 로고
    • Reverse engineering of the giant muscle protein titin
    • Li, H. B. et al. Reverse engineering of the giant muscle protein titin. Nature 418, 998-1002 (2002).
    • (2002) Nature , vol.418 , pp. 998-1002
    • Li, H.B.1
  • 11
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu, H., Isralewitz, B., Krammer, A., Vogel, V. & Schulten, K. Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys. J. 75, 662-671 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 12
    • 0033917135 scopus 로고    scopus 로고
    • The key event in force-induced unfolding of titin's immunoglobulin domains
    • Lu, H. & Schulten, K. The key event in force-induced unfolding of titin's immunoglobulin domains. Biophys. J. 79, 51-65 (2000).
    • (2000) Biophys. J. , vol.79 , pp. 51-65
    • Lu, H.1    Schulten, K.2
  • 13
    • 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0035957219 scopus 로고    scopus 로고
    • Polyproline II helix is a key structural motif of the elastic PEVK segment of titin
    • Ma, K., Kan, L. S. & Wang, K. Polyproline II helix is a key structural motif of the elastic PEVK segment of titin. Biochemistry 40, 3427-3438 (2001).
    • (2001) Biochemistry , vol.40 , pp. 3427-3438
    • Ma, K.1    Kan, L.S.2    Wang, K.3
  • 17
    • 0031795571 scopus 로고    scopus 로고
    • A spring tale: New facts on titin elasticity
    • Linke, W. A. & Granzier, H. A spring tale: New facts on titin elasticity. Biophys. J. 75, 2613-2614 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 2613-2614
    • Linke, W.A.1    Granzier, H.2
  • 18
    • 0035115798 scopus 로고    scopus 로고
    • Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils
    • Minajeva, A., Kulke, M., Fernandez, J. M. & Linke, W. A. Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils. Biophys. J. 80, 1442-1451 (2001).
    • (2001) Biophys. J. , vol.80 , pp. 1442-1451
    • Minajeva, A.1    Kulke, M.2    Fernandez, J.M.3    Linke, W.A.4
  • 19
    • 0035919831 scopus 로고    scopus 로고
    • Flexibility and extensibility in the titin molecule: Analysis of electron microscope data
    • Tskhovrebova, L. & Trinick, J. Flexibility and extensibility in the titin molecule: Analysis of electron microscope data. J. Mol. Biol. 310, 755-771 (2001).
    • (2001) J. Mol. Biol. , vol.310 , pp. 755-771
    • Tskhovrebova, L.1    Trinick, J.2
  • 20
    • 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, 308-312 (1997).
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 21
    • 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, 1109-1112 (1997).
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 22
    • 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, 1112-1116 (1997).
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.Z.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 23
    • 0029801781 scopus 로고    scopus 로고
    • Assembly of the cardiac I-band region of titin/connectin: Expression of the cardiac-specific regions and their structural relation to the elastic segments
    • Gautel, M., Lehtonen, E. & Pietruschka, F. Assembly of the cardiac I-band region of titin/connectin: Expression of the cardiac-specific regions and their structural relation to the elastic segments. J. Muscle Res. Cell Motil. 17, 449-461 (1996).
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 449-461
    • Gautel, M.1    Lehtonen, E.2    Pietruschka, F.3
  • 24
    • 0034984382 scopus 로고    scopus 로고
    • Mapping the folding pathway of an immunoglobulin domain: Structural detail from phi value analysis and movement of the transition state
    • Fowler, S. B. & Clarke, J. Mapping the folding pathway of an immunoglobulin domain: Structural detail from phi value analysis and movement of the transition state. Structure 9, 355-366 (2001).
    • (2001) Structure , vol.9 , pp. 355-366
    • Fowler, S.B.1    Clarke, J.2
  • 25
    • 0037126019 scopus 로고    scopus 로고
    • A simple method for probing the mechanical unfolding pathway of proteins in detail
    • Best, R. B., Fowler, S. B., Toca-Herrera, J. L. & Clarke, J. A simple method for probing the mechanical unfolding pathway of proteins in detail. Proc. Natl Acad. Sci. USA 99, 12143-12148 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12143-12148
    • Best, R.B.1    Fowler, S.B.2    Toca-Herrera, J.L.3    Clarke, J.4
  • 26
    • 0036707999 scopus 로고    scopus 로고
    • Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy
    • Steward, A., Toca-Herrera, J. L. & Clarke, J. Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy. Protein Sci. 11, 2179-2183 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 2179-2183
    • Steward, A.1    Toca-Herrera, J.L.2    Clarke, J.3
  • 27
    • 0034804341 scopus 로고    scopus 로고
    • Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation
    • Best, R. B., Li, B., Steward, A., Daggett, V. & Clarke, J. Can non-mechanical proteins withstand force? Stretching barnase by atomic force microscopy and molecular dynamics simulation. Biophys J. 81, 2344-2356 (2001).
    • (2001) Biophys J. , vol.81 , pp. 2344-2356
    • Best, R.B.1    Li, B.2    Steward, A.3    Daggett, V.4    Clarke, J.5
  • 28
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force-lifetime-and chemistry in single molecular bonds
    • Evans, E. Probing the relation between force-lifetime-and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. Struct. 30, 105-128 (2001).
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 105-128
    • Evans, E.1
  • 30
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin 1-band: Extensible components of muscle elasticity
    • Improta, S., Politou, A. S. & Pastore, A. Immunoglobulin-like modules from titin 1-band: Extensible components of muscle elasticity. Structure 4, 323-337 (1996).
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.S.2    Pastore, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.