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Volumn 26, Issue 6-8, 2005, Pages 285-289

Can the passive elasticity of muscle be explained directly from the mechanics of individual titin molecules?

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EID: 33745726393     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-005-9034-5     Document Type: Conference Paper
Times cited : (9)

References (44)
  • 1
    • 0031258656 scopus 로고    scopus 로고
    • Evidence that the tandem Ig domains near the end of the muscle thick filament form an inelastic part of the I-band titin
    • Bennett PM, Hodkin TE and Hawkins C (1997) Evidence that the tandem Ig domains near the end of the muscle thick filament form an inelastic part of the I-band titin. J Struct Biol 120: 93-104.
    • (1997) J Struct Biol , vol.120 , pp. 93-104
    • Bennett, P.M.1    Hodkin, T.E.2    Hawkins, C.3
  • 3
    • 0035947754 scopus 로고    scopus 로고
    • Titin-based modulation of calcium sensitivity of active force in mouse skinned cardiac myocytes
    • Cazorla O, Wu Y, Irving TC and Granzier H (2001) Titin-based modulation of calcium sensitivity of active force in mouse skinned cardiac myocytes. Circ Res 88: 1028-1035.
    • (2001) Circ Res , vol.88 , pp. 1028-1035
    • Cazorla, O.1    Wu, Y.2    Irving, T.C.3    Granzier, H.4
  • 4
    • 1242265483 scopus 로고    scopus 로고
    • Polymer-induced depletion interaction between weakly attractive plates
    • Cifra P and Bleha T (2004) Polymer-induced depletion interaction between weakly attractive plates. Langmuir 20: 764-770.
    • (2004) Langmuir , vol.20 , pp. 764-770
    • Cifra, P.1    Bleha, T.2
  • 5
    • 3342991494 scopus 로고    scopus 로고
    • Experimental investigation of protein folding and misfolding
    • Dobson CM (2004) Experimental investigation of protein folding and misfolding. Methods 34: 4-14.
    • (2004) Methods , vol.34 , pp. 4-14
    • Dobson, C.M.1
  • 6
    • 0041822089 scopus 로고    scopus 로고
    • Join the crowd
    • Ellis RJ and Minton AP (2003) Join the crowd. Nature 425: 27-28.
    • (2003) Nature , vol.425 , pp. 27-28
    • Ellis, R.J.1    Minton, A.P.2
  • 7
    • 0033538417 scopus 로고    scopus 로고
    • Modularity and homology: Modelling of the type II module family from titin
    • Fraternali F and Pastore A (1999) Modularity and homology: modelling of the type II module family from titin. J Mol Biol 290: 581-593.
    • (1999) J Mol Biol , vol.290 , pp. 581-593
    • Fraternali, F.1    Pastore, A.2
  • 8
    • 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, Kono E, Higuchi H, Kimura S, Ishiwata S, Yoshioka T, Maruyama K and Tsukita S (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
  • 9
    • 0036517816 scopus 로고    scopus 로고
    • Ischemia-induced association of the stress protein alpha B-crystallin with I-band portion of cardiac titin
    • Golenhofen N, Arbeiter A, Koob R and Drenckhahn D (2002) Ischemia-induced association of the stress protein alpha B-crystallin with I-band portion of cardiac titin. J Mol Cell Cardiol 34: 309-319.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 309-319
    • Golenhofen, N.1    Arbeiter, A.2    Koob, R.3    Drenckhahn, D.4
  • 10
    • 0030048904 scopus 로고    scopus 로고
    • Nonuniform elasticity of titin in cardiac myocytes: A study using immunoelectron microscopy and cellular mechanics
    • Granzier H, Helmes M and Trombitás K (1996) Nonuniform elasticity of titin in cardiac myocytes: a study using immunoelectron microscopy and cellular mechanics. Biophys J 70: 430-442.
    • (1996) Biophys J , vol.70 , pp. 430-442
    • Granzier, H.1    Helmes, M.2    Trombitás, K.3
  • 11
    • 0030855930 scopus 로고    scopus 로고
    • Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction
    • Granzier H, Kellermayer M, Helmes M and Trombitás K (1997) Titin elasticity and mechanism of passive force development in rat cardiac myocytes probed by thin-filament extraction. Biophys J 73: 2043-2053.
    • (1997) Biophys J , vol.73 , pp. 2043-2053
    • Granzier, H.1    Kellermayer, M.2    Helmes, M.3    Trombitás, K.4
  • 12
    • 0027488781 scopus 로고
    • Characterization of β-connectin (titin 2) from striated mucle by dynamic light scattering
    • Higuchi H, Nakauchi Y, Maruyama K and Fujime S (1993) Characterization of β-connectin (titin 2) from striated mucle by dynamic light scattering. Biophys J 65: 1906-1915.
    • (1993) Biophys J , vol.65 , pp. 1906-1915
    • Higuchi, H.1    Nakauchi, Y.2    Maruyama, K.3    Fujime, S.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 and Podolsky RJ (1987) 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: 2217-2223.
    • (1987) J Cell Biol , vol.105 , pp. 2217-2223
    • Horowits, R.1    Podolsky, R.J.2
  • 14
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer MSZ, Smith SB, Granzier HL and Bustamante C (1997) Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science 276: 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
  • 15
    • 0038740870 scopus 로고    scopus 로고
    • Mechanics and structure of titin oligomers explored with atomic force microscopy
    • Kellermayer MSZ, Granzier HL and Bustamante C (2003) Mechanics and structure of titin oligomers explored with atomic force microscopy. Biochim Biophys Acia 1604: 105-114.
    • (2003) Biochim Biophys Acia , vol.1604 , pp. 105-114
    • Kellermayer, M.S.Z.1    Granzier, H.L.2    Bustamante, C.3
  • 16
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S and Kolmerer B (1995) Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270: 293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 18
    • 4143147307 scopus 로고    scopus 로고
    • The elasticity of single titin molecules using a two-bead optical tweezers assays
    • Leake MC, Wilson D, Gautel M and Simmons RM (2004) The elasticity of single titin molecules using a two-bead optical tweezers assays. Biophys J 87: 1112-1135.
    • (2004) Biophys J , vol.87 , pp. 1112-1135
    • Leake, M.C.1    Wilson, D.2    Gautel, M.3    Simmons, R.M.4
  • 19
    • 0037569697 scopus 로고    scopus 로고
    • Cardiac titin: Molecular basis of elasticity and cellular contribution to elastic and viscous stiffness components in myocardium
    • Linke WA and Fernandez JM (2002) Cardiac titin: molecular basis of elasticity and cellular contribution to elastic and viscous stiffness components in myocardium. J Muscle Res Cell Motil 23: 483-497.
    • (2002) J Muscle Res Cell Motil , vol.23 , pp. 483-497
    • Linke, W.A.1    Fernandez, J.M.2
  • 21
    • 4444302854 scopus 로고    scopus 로고
    • Multiple sources of passive stress relaxation in muscle fibres
    • Linke WA and Leake MC (2004) Multiple sources of passive stress relaxation in muscle fibres. Phys Med Biol 49: 3613-3627.
    • (2004) Phys Med Biol , vol.49 , pp. 3613-3627
    • Linke, W.A.1    Leake, M.C.2
  • 22
    • 0031809493 scopus 로고    scopus 로고
    • Characterizing titin's I-band Ig domain region as an entropic spring
    • Linke WA, Stockmeier MR, Ivemeyer M, Hosser H and Mundel P (1998) Characterizing titin's I-band Ig domain region as an entropic spring. J Cell Sci 111: 1567-1574.
    • (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
  • 24
    • 0035957219 scopus 로고    scopus 로고
    • Polyproline II helix is a key structural motif of the elastic PEVK segment of titin
    • Ma K, Kan LS and Wang K (2001) Polyproline II helix is a key structural motif of the elastic PEVK segment of titin. Biochem 40: 3427-3438.
    • (2001) Biochem , vol.40 , pp. 3427-3438
    • Ma, K.1    Kan, L.S.2    Wang, K.3
  • 25
    • 0037132502 scopus 로고    scopus 로고
    • Interaction of nebulin SH3 domain with titin PEVK and myopalladin: Implications for the signaling and assembly role of titin and nebulin
    • Ma K and Wang K (2002) Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin. FEBS Lett 532: 273-278.
    • (2002) FEBS Lett , vol.532 , pp. 273-278
    • Ma, K.1    Wang, K.2
  • 27
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton AP (2000) Implications of macromolecular crowding for protein assembly. Curr Opin Struct Biol 10: 34-39.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 29
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M, Gautel M, Oesterhelt F, Fernandez JM and Gaub HE (1997) Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276: 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
  • 31
    • 0019834569 scopus 로고
    • End-filaments: A new structural element of vertebrate skeletal muscle thick filaments
    • Trinick JA (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
  • 32
    • 0030091595 scopus 로고    scopus 로고
    • Cytoskeleton - Titin as a scaffold and spring
    • Trinick J (1996) Cytoskeleton - titin as a scaffold and spring. Curr Biol 6: 258-260.
    • (1996) Curr Biol , vol.6 , pp. 258-260
    • Trinick, J.1
  • 33
    • 0030976481 scopus 로고    scopus 로고
    • Interaction between titin and thin filaments in intact cardiac muscle
    • Trombitás K, Greaser ML and Pollack GH (1997) Interaction between titin and thin filaments in intact cardiac muscle. J Muscle Res Cell Motil 18: 345-351.
    • (1997) J Muscle Res Cell Motil , vol.18 , pp. 345-351
    • Trombitás, K.1    Greaser, M.L.2    Pollack, G.H.3
  • 34
    • 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 and Granzier H (1998) Titin extensibility in situ: entropic elasticity of permanently folded and permanently unfolded molecular segments. J Cell Biol 140: 853-859.
    • (1998) J Cell Biol , vol.140 , pp. 853-859
    • Trombitás, K.1    Greaser, M.2    Labeit, S.3    Jin, J.-P.4    Kellermayer, M.5    Helmes, M.6    Granzier, H.7
  • 36
    • 0033637514 scopus 로고    scopus 로고
    • Extensibility of isoforms of cardiac titin: Variation in contour length of molecular subsegments provides a basis for cellular passive stiffness diversity
    • Trombitás K, Redkar A, Centner T, Wu Y, Labeit S and Granzier H (2000) Extensibility of isoforms of cardiac titin: variation in contour length of molecular subsegments provides a basis for cellular passive stiffness diversity. Biophys J 79: 3226-3234.
    • (2000) Biophys J , vol.79 , pp. 3226-3234
    • Trombitás, K.1    Redkar, A.2    Centner, T.3    Wu, Y.4    Labeit, S.5    Granzier, H.6
  • 37
    • 0242322488 scopus 로고    scopus 로고
    • Molecular basis of passive stress relaxation in human soleus fibers: Assessment of the role of immunoglobulin-like domain unfolding
    • Trombitás K, Wu Y, McNabb M, Greaser M, Kellermayer MSZ, Labeit S and Granzier H (2003) Molecular basis of passive stress relaxation in human soleus fibers: assessment of the role of immunoglobulin-like domain unfolding. Biophys J 85: 3142-3153.
    • (2003) Biophys J , vol.85 , pp. 3142-3153
    • Trombitás, K.1    Wu, Y.2    McNabb, M.3    Greaser, M.4    Kellermayer, M.S.Z.5    Labeit, S.6    Granzier, H.7
  • 38
    • 0035919831 scopus 로고    scopus 로고
    • Flexibility and extensibility in the titin molecule: Analysis of electron microscope data
    • Tskhovrebova L and Trinick J (2001) Flexibility and extensibility in the titin molecule: analysis of electron microscope data. J Mol Biol 310: 755-771.
    • (2001) J Mol Biol , vol.310 , pp. 755-771
    • Tskhovrebova, L.1    Trinick, J.2
  • 40
    • 0031006659 scopus 로고    scopus 로고
    • Elasticity and unfolding of single molecules of the giant muscle protein titin
    • Tskhovrebova L, Trinick J, Sleep JA and Simmons RM (1997) Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature 387: 308-312.
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.M.4
  • 41
    • 0034254189 scopus 로고    scopus 로고
    • Molecular crowding perturbs protein refolding kinetics: Implications for folding inside the cell
    • Van den Berg B, Wain R, Dobson CM and Ellis RJ (2000) Molecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. EMBO J 19: 3870-3875.
    • (2000) EMBO J , vol.19 , pp. 3870-3875
    • Van Den Berg, B.1    Wain, R.2    Dobson, C.M.3    Ellis, R.J.4
  • 43
    • 1642303150 scopus 로고    scopus 로고
    • Effect of confinement on dynamics and rheology of dilute DNA solutions. I. Entropic spring force under confinement and a numerical algorithm
    • Woo NJ, Shaqfeh ESG and Khonami B (2004) Effect of confinement on dynamics and rheology of dilute DNA solutions. I. Entropic spring force under confinement and a numerical algorithm. J Rheol 48: 281-298.
    • (2004) J Rheol , vol.48 , pp. 281-298
    • Woo, N.J.1    Shaqfeh, E.S.G.2    Khonami, B.3
  • 44
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • Zimmerman SB (1993) Macromolecular crowding: biochemical, biophysical, and physiological consequences. Annu Rev Biophys Biomol Struct 22: 27-65.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 27-65
    • Zimmerman, S.B.1


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