메뉴 건너뛰기




Volumn 24, Issue 2-3, 2003, Pages 175-189

Gigantic variety: Expression patterns of titin isoforms in striated muscles and consequences for myofibrillar passive stiffness

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; CONNECTIN;

EID: 0142249479     PISSN: 01424319     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1026053530766     Document Type: Conference Paper
Times cited : (157)

References (123)
  • 1
    • 0036751719 scopus 로고    scopus 로고
    • Passive stiffness changes in soleus muscles from desmin knockout mice are not due to titin modifications
    • Anderson J, Joumaa V, Stevens L, Neagoe C, Li Z, Mounier Y, Linke WA and Goubel F (2002) Passive stiffness changes in soleus muscles from desmin knockout mice are not due to titin modifications. Pflügers Arch 444: 771-776.
    • (2002) Pflügers Arch , vol.444 , pp. 771-776
    • Anderson, J.1    Joumaa, V.2    Stevens, L.3    Neagoe, C.4    Li, Z.5    Mounier, Y.6    Linke, W.A.7    Goubel, F.8
  • 2
    • 0035941407 scopus 로고    scopus 로고
    • The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system
    • Bang ML, Centner T, Fornoff F, Geach AJ, Gotthardt M, McNabb M, Witt CC, Labeit D, Gregorio CC, Granzier H and Labeit S (2001) The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system. Circ Res 89: 1065-1072.
    • (2001) Circ Res , vol.89 , pp. 1065-1072
    • Bang, M.L.1    Centner, T.2    Fornoff, F.3    Geach, A.J.4    Gotthardt, M.5    McNabb, M.6    Witt, C.C.7    Labeit, D.8    Gregorio, C.C.9    Granzier, H.10    Labeit, S.11
  • 3
    • 0030750332 scopus 로고    scopus 로고
    • Basis of passive tension and stiffness in isolated rabbit myofibrils
    • Bartoo ML, Linke WA and Pollack GH (1997) Basis of passive tension and stiffness in isolated rabbit myofibrils. Am J Physiol 273: C266-C276.
    • (1997) Am J Physiol , vol.273
    • Bartoo, M.L.1    Linke, W.A.2    Pollack, G.H.3
  • 5
    • 0006141594 scopus 로고
    • The extensibility of muscle
    • Brodie TG (1895) The extensibility of muscle. J Anat Physiol 29: 367-388.
    • (1895) J Anat Physiol , vol.29 , pp. 367-388
    • Brodie, T.G.1
  • 6
    • 73049120263 scopus 로고
    • Ultrastructure of the resting and contracted striated muscle fiber at different degrees of stretch
    • Carlsen F, Knappeis GG and Buchthal F (1961) Ultrastructure of the resting and contracted striated muscle fiber at different degrees of stretch. J Biophys Biochem Cytol 11: 95-117.
    • (1961) J Biophys Biochem Cytol , vol.11 , pp. 95-117
    • Carlsen, F.1    Knappeis, G.G.2    Buchthal, F.3
  • 9
    • 0035947754 scopus 로고    scopus 로고
    • Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes
    • Cazorla O, Wu Y, Irving TC and Granzier H (2001) Titin-based modulation of calcium sensitivity of active tension 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
  • 13
    • 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 SB, Best RB, Toca Herrera JL, Rutherford TJ, Steward A, Paci E, Karplus M and Clarke J (2002) 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) J Mol Biol , vol.322 , pp. 841-849
    • Fowler, S.B.1    Best, R.B.2    Toca Herrera, J.L.3    Rutherford, T.J.4    Steward, A.5    Paci, E.6    Karplus, M.7    Clarke, J.8
  • 16
    • 0035797846 scopus 로고    scopus 로고
    • Length dependence of tension generation in rat skinned cardiac muscle: Role of titin in the Frank-Starling mechanism of the heart
    • Fukuda N, Sasaki D, Ishiwata S and Kurihara S (2001) Length dependence of tension generation in rat skinned cardiac muscle: role of titin in the Frank-Starling mechanism of the heart. Circulation 104: 1639-1645.
    • (2001) Circulation , vol.104 , pp. 1639-1645
    • Fukuda, N.1    Sasaki, D.2    Ishiwata, S.3    Kurihara, S.4
  • 17
    • 0025062549 scopus 로고
    • Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin
    • Funatsu T, Higuchi H and Ishiwata S (1990) Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin. J Cell Biol 110: 53-62.
    • (1990) J Cell Biol , vol.110 , pp. 53-62
    • Funatsu, T.1    Higuchi, H.2    Ishiwata, S.3
  • 19
    • 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 DO, Osborn M, Nave R and Weber K (1988) 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: 1563-1572.
    • (1988) J Cell Biol , vol.106 , pp. 1563-1572
    • Fürst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 20
    • 0035134297 scopus 로고    scopus 로고
    • Passive extensibility of skeletal muscle: Review of the literature with clinical implications
    • Gajdosik RL (2001) Passive extensibility of skeletal muscle: review of the literature with clinical implications. Clin Biomech (Bristol, Avon) 16: 87-101.
    • (2001) Clin Biomech (Bristol, Avon) , vol.16 , pp. 87-101
    • Gajdosik, R.L.1
  • 21
    • 0036924186 scopus 로고    scopus 로고
    • Steered molecular dynamics studies of titin I1 domain unfolding
    • Gao M, Wilmanns M and Schulten K (2002) Steered molecular dynamics studies of titin I1 domain unfolding. Biophys J 83: 3435-3445.
    • (2002) Biophys J , vol.83 , pp. 3435-3445
    • Gao, M.1    Wilmanns, M.2    Schulten, K.3
  • 22
    • 0002542624 scopus 로고
    • Elongation of the primary myofilaments in highly stretched insect flight muscle fibrils
    • Garamvölgyi N (1966) Elongation of the primary myofilaments in highly stretched insect flight muscle fibrils. Biochem Biophys Acta 1: 89-100.
    • (1966) Biochem Biophys Acta , vol.1 , pp. 89-100
    • Garamvölgyi, N.1
  • 23
    • 0029882110 scopus 로고    scopus 로고
    • A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
    • Gautel M and Goulding D (1996) A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series. FEBS Lett 385: 11-14.
    • (1996) FEBS Lett , vol.385 , pp. 11-14
    • Gautel, M.1    Goulding, D.2
  • 24
  • 25
    • 0028957373 scopus 로고
    • Passive tension in cardiac muscle: Contribution of collagen, titin, microtubules, and intermediate filaments
    • Granzier HL and Irving TC (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.1    Irving, T.C.2
  • 26
    • 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 Trombitas 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    Trombitas, K.4
  • 27
    • 0036623918 scopus 로고    scopus 로고
    • Cardiac titin: An adjustable multifunctional spring
    • Granzier H and Labeit S (2002) Cardiac titin: an adjustable multifunctional spring. J Physiol 541: 335-342.
    • (2002) J Physiol , vol.541 , pp. 335-342
    • Granzier, H.1    Labeit, S.2
  • 28
    • 0027436282 scopus 로고
    • Passive tension and stiffness of vertebrate skeletal and insect flight muscles: The contribution of weak cross-bridges and elastic filaments
    • Granzier HL and Wang K (1993) Passive tension and stiffness of vertebrate skeletal and insect flight muscles: the contribution of weak cross-bridges and elastic filaments. Biophys J 65: 2141-2159.
    • (1993) Biophys J , vol.65 , pp. 2141-2159
    • Granzier, H.L.1    Wang, K.2
  • 29
    • 0006140289 scopus 로고
    • The elasticity of animal tissue
    • Haycraft JB (1904) The elasticity of animal tissue. J Physiol 31: 392-409.
    • (1904) J Physiol , vol.31 , pp. 392-409
    • Haycraft, J.B.1
  • 30
    • 0033546073 scopus 로고    scopus 로고
    • Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: Titin is an adjustable spring
    • Helmes M, Trombitas K, Centner T, Kellermayer M, Labeit S, Linke WA and Granzier H (1999) Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: titin is an adjustable spring. Circ Res 84: 1339-1352.
    • (1999) Circ Res , vol.84 , pp. 1339-1352
    • Helmes, M.1    Trombitas, K.2    Centner, T.3    Kellermayer, M.4    Labeit, S.5    Linke, W.A.6    Granzier, H.7
  • 31
    • 0000682154 scopus 로고
    • The heat of shortening and the dynamic constants of muscle
    • Hill AV (1938) The heat of shortening and the dynamic constants of muscle. Proc Roy Soc Lond B 126: 136-195.
    • (1938) Proc Roy Soc Lond B , vol.126 , pp. 136-195
    • Hill, A.V.1
  • 32
    • 76949136455 scopus 로고
    • The thermodynamics of elasticity in resting striated muscle
    • Hill AV (1952) The thermodynamics of elasticity in resting striated muscle. Proc Roy Soc Lond B 139: 464-497.
    • (1952) Proc Roy Soc Lond B , vol.139 , pp. 464-497
    • Hill, A.V.1
  • 33
    • 0014387009 scopus 로고
    • Tension due to interaction between the sliding filaments in resting striated muscle. The effect of stimulation
    • Hill DK (1968) Tension due to interaction between the sliding filaments in resting striated muscle. The effect of stimulation. J Physiol 199: 637-684.
    • (1968) J Physiol , vol.199 , pp. 637-684
    • Hill, D.K.1
  • 34
    • 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
  • 35
    • 0023047016 scopus 로고
    • A physiological role for titin and nebulin in skeletal muscle
    • Horowits R, Kempner ES, Bisher ME and Podolsky RJ (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.J.4
  • 36
    • 0024426462 scopus 로고
    • Elastic behavior of connectin filaments during thick filament movement in activated skeletal muscle
    • Horowits R, Maruyama K and Podolsky RJ (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.J.3
  • 37
    • 0023896719 scopus 로고
    • Thick filament movement and isometric tension in activated skeletal muscle
    • Horowits R and Podolsky RJ (1988) Thick filament movement and isometric tension in activated skeletal muscle. Biophys J 54: 165-171.
    • (1988) Biophys J , vol.54 , pp. 165-171
    • Horowits, R.1    Podolsky, R.J.2
  • 38
    • 36949093311 scopus 로고
    • Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation
    • Huxley HE and Hanson J (1954) Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature 173: 149-152.
    • (1954) Nature , vol.173 , pp. 149-152
    • Huxley, H.E.1    Hanson, J.2
  • 39
    • 72949127255 scopus 로고
    • The maximum length for contraction in vertebrate striated muscle
    • Huxley AF and Peachey LD (1961) The maximum length for contraction in vertebrate striated muscle. J Physiol 156: 150-165.
    • (1961) J Physiol , vol.156 , pp. 150-165
    • Huxley, A.F.1    Peachey, L.D.2
  • 40
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from I-band titin: Extensible components of muscle elasticity
    • Improta S, Politou A and Pastore A (1996) Immunoglobulin-like modules from I-band titin: extensible components of muscle elasticity. Structure 4: 323-337.
    • (1996) Structure , vol.4 , pp. 323-337
    • Improta, S.1    Politou, A.2    Pastore, A.3
  • 41
    • 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, Suzuki T, Kimura S, Ohashi K, Higuchi H, Sawada H, Shimizu T, Shibata M and Maruyama K (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    Shimizu, T.7    Shibata, M.8    Maruyama, K.9
  • 42
    • 0034303611 scopus 로고    scopus 로고
    • Expression of titin in skeletal muscle varies with hind-limb unloading
    • Kasper CE and Xun L (2000) Expression of titin in skeletal muscle varies with hind-limb unloading. Biol Res Nurs 2: 107-115.
    • (2000) Biol Res Nurs , vol.2 , pp. 107-115
    • Kasper, C.E.1    Xun, L.2
  • 43
  • 44
    • 0035144607 scopus 로고    scopus 로고
    • Mechanical fatigue in repetitively stretched single molecules of titin
    • Kellermayer MS, Smith SB, Bustamante C and Granzier HL (2001) Mechanical fatigue in repetitively stretched single molecules of titin. Biophys J 80: 852-863.
    • (2001) Biophys J , vol.80 , pp. 852-863
    • Kellermayer, M.S.1    Smith, S.B.2    Bustamante, C.3    Granzier, H.L.4
  • 45
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer MS, 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.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 46
    • 0036389773 scopus 로고    scopus 로고
    • Titin organisation and the 3D architecture of the vertebrate-striated muscle I-band
    • Knupp C, Luther PK and Squire JM (2002) Titin organisation and the 3D architecture of the vertebrate-striated muscle I-band. J Mol Biol 322: 731-739.
    • (2002) J Mol Biol , vol.322 , pp. 731-739
    • Knupp, C.1    Luther, P.K.2    Squire, J.M.3
  • 47
    • 0037423366 scopus 로고    scopus 로고
    • The hydrophilic domain of small ankyrin 1 interacts with the two NH2-terminal immunoglobulin domains of titin
    • Kontrogianni-Konstantopoulos A and Bloch RJ (2003) The hydrophilic domain of small ankyrin 1 interacts with the two NH2-terminal immunoglobulin domains of titin. J Biol Chem 278: 3985-3991.
    • (2003) J Biol Chem , vol.278 , pp. 3985-3991
    • Kontrogianni-Konstantopoulos, A.1    Bloch, R.J.2
  • 50
    • 0023872824 scopus 로고
    • Giant polypeptides of skeletal muscle titin: Sedimentation equilibrium in guanidine hydrochloride
    • Kurzban GP and Wang K (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.P.1    Wang, K.2
  • 52
    • 0026582867 scopus 로고
    • Towards a molecular understanding of titin
    • Labeit S, Gautel M, Lakey A and Trinick J (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    Lakey, A.3    Trinick, J.4
  • 53
    • 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
  • 54
    • 0031016596 scopus 로고    scopus 로고
    • The giant protein titin, emerging roles in physiology and pathophysiology
    • Labeit S, Kolmerer B and Linke WA (1997) The giant protein titin, emerging roles in physiology and pathophysiology. Circ Res 80: 290-294.
    • (1997) Circ Res , vol.80 , pp. 290-294
    • Labeit, S.1    Kolmerer, B.2    Linke, W.A.3
  • 57
    • 0035994676 scopus 로고    scopus 로고
    • Do muscles function as adaptable locomotor springs?
    • Lindstedt SL, Reich TE, Keim P and LaStayo PC (2002) Do muscles function as adaptable locomotor springs? J Exp Biol 205: 2211-2216.
    • (2002) J Exp Biol , vol.205 , pp. 2211-2216
    • Lindstedt, S.L.1    Reich, T.E.2    Keim, P.3    LaStayo, P.C.4
  • 58
    • 0033928461 scopus 로고    scopus 로고
    • Stretching molecular springs: Elasticity of titin filaments in vertebrate striated muscle
    • Linke WA (2000) Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle. Histol Histopathol 15: 799-811.
    • (2000) Histol Histopathol , vol.15 , pp. 799-811
    • Linke, W.A.1
  • 59
    • 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(5-6): 483-497.
    • (2002) J Muscle Res Cell Motil , vol.23 , Issue.5-6 , pp. 483-497
    • Linke, W.A.1    Fernandez, J.M.2
  • 60
    • 0031795571 scopus 로고    scopus 로고
    • A spring tale: New facts on titin elasticity
    • Linke WA and Granzier H (1998) A spring tale: new facts on titin elasticity. Biophys J 75: 2613-2614.
    • (1998) Biophys J , vol.75 , pp. 2613-2614
    • Linke, W.A.1    Granzier, H.2
  • 65
    • 0027934071 scopus 로고
    • Passive and active tension in single cardiac myofibrils
    • Linke WA, Popov VI and Pollack GH (1994) Passive and active tension in single cardiac myofibrils. Biophys J 67: 782-792.
    • (1994) Biophys J , vol.67 , pp. 782-792
    • Linke, W.A.1    Popov, V.I.2    Pollack, G.H.3
  • 66
    • 0033538859 scopus 로고    scopus 로고
    • I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure
    • Linke WA, Rudy DE, Centner T, Gautel M, Witt C, Labeit S and Gregorio CC (1999) I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure. J Cell Biol 146: 631-644.
    • (1999) J Cell Biol , vol.146 , pp. 631-644
    • Linke, W.A.1    Rudy, D.E.2    Centner, T.3    Gautel, M.4    Witt, C.5    Labeit, S.6    Gregorio, C.C.7
  • 67
    • 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 (1998b) 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
  • 69
    • 0031848099 scopus 로고    scopus 로고
    • Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation
    • Lu H, Isralewitz B, Krammer A, Vogel V and Schulten K (1998) Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation. Biophys J 75: 662-671.
    • (1998) Biophys J , vol.75 , pp. 662-671
    • Lu, H.1    Isralewitz, B.2    Krammer, A.3    Vogel, V.4    Schulten, K.5
  • 70
    • 0033917135 scopus 로고    scopus 로고
    • The key event in force-induced unfolding of titin's immunoglobulin domains
    • Lu H and Schulten K (2000) The key event in force-induced unfolding of titin's immunoglobulin domains. Biophys J 79: 51-65.
    • (2000) Biophys J , vol.79 , pp. 51-65
    • Lu, H.1    Schulten, K.2
  • 71
    • 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
  • 72
    • 0022402720 scopus 로고
    • Myofibrils bear most of the resting tension in frog skeletal muscle
    • Magid A and Law DJ (1985) Myofibrils bear most of the resting tension in frog skeletal muscle. Science 230: 1280-1282.
    • (1985) Science , vol.230 , pp. 1280-1282
    • Magid, A.1    Law, D.J.2
  • 75
    • 0021279759 scopus 로고
    • Molecular size and shape of β-connectin, an elastic protein of striated muscle
    • Maruyama K, Kimura S, Yoshidomi H, Sawada H and Kikuchi M (1984) Molecular size and shape of β-connectin, an elastic protein of striated muscle. J Biochem (Tokyo) 95: 1423-1493.
    • (1984) J Biochem (Tokyo) , vol.95 , pp. 1423-1493
    • Maruyama, K.1    Kimura, S.2    Yoshidomi, H.3    Sawada, H.4    Kikuchi, M.5
  • 77
    • 0017753011 scopus 로고
    • Connectin, an elastic protein of muscle. Comparative Biochemistry
    • Maruyama K, Murakami F and Ohashi K (1977b) Connectin, an elastic protein of muscle. Comparative Biochemistry. J Biochem (Tokyo) 82: 339-345.
    • (1977) J Biochem (Tokyo) , vol.82 , pp. 339-345
    • Maruyama, K.1    Murakami, F.2    Ohashi, K.3
  • 79
    • 0034886351 scopus 로고    scopus 로고
    • Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin
    • Mayans O, Wuerges J, Canela S, Gautel M and Wilmanns M (2001) Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin. Structure 9: 331-340.
    • (2001) Structure , vol.9 , pp. 331-340
    • Mayans, O.1    Wuerges, J.2    Canela, S.3    Gautel, M.4    Wilmanns, M.5
  • 80
    • 0036544533 scopus 로고    scopus 로고
    • Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1
    • McElhinny AS, Kakinuma K, Sorimachi H, Labeit S and Gregorio CC (2002) Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J Cell Biol 157: 125-136.
    • (2002) J Cell Biol , vol.157 , pp. 125-136
    • McElhinny, A.S.1    Kakinuma, K.2    Sorimachi, H.3    Labeit, S.4    Gregorio, C.C.5
  • 81
    • 0035115798 scopus 로고    scopus 로고
    • Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils
    • Minajeva A, Kulke M, Fernandez JM and Linke WA (2001) Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils. Biophys J 80: 1442-1451.
    • (2001) Biophys J , vol.80 , pp. 1442-1451
    • Minajeva, A.1    Kulke, M.2    Fernandez, J.M.3    Linke, W.A.4
  • 82
    • 0036554815 scopus 로고    scopus 로고
    • Titin-based contribution to shortening velocity of rabbit skeletal myofibrils
    • Minajeva A, Neagoe C, Kulke M and Linke WA (2002) Titin-based contribution to shortening velocity of rabbit skeletal myofibrils. J Physiol 540: 177-188.
    • (2002) J Physiol , vol.540 , pp. 177-188
    • Minajeva, A.1    Neagoe, C.2    Kulke, M.3    Linke, W.A.4
  • 83
    • 0035914471 scopus 로고    scopus 로고
    • Structural and functional studies of titin's fn3 modules reveal conserved surface patterns and binding to myosin S1 - A possible role in the Frank-Starling mechanism of the heart
    • Muhle-Goll C, Habeck M, Cazorla O, Nilges M, Labeit S and Granzier H (2001) Structural and functional studies of titin's fn3 modules reveal conserved surface patterns and binding to myosin S1 - a possible role in the Frank-Starling mechanism of the heart. J Mol Biol 313: 431-447.
    • (2001) J Mol Biol , vol.313 , pp. 431-447
    • Muhle-Goll, C.1    Habeck, M.2    Cazorla, O.3    Nilges, M.4    Labeit, S.5    Granzier, H.6
  • 84
    • 0029992593 scopus 로고    scopus 로고
    • The viscous, viscoelastic and elastic characteristics of resting fast and slow mammalian (rat) muscle fibres
    • Mutungi G and Ranatunga KW (1996) The viscous, viscoelastic and elastic characteristics of resting fast and slow mammalian (rat) muscle fibres. J Physiol 496: 827-836.
    • (1996) J Physiol , vol.496 , pp. 827-836
    • Mutungi, G.1    Ranatunga, K.W.2
  • 85
    • 0024440423 scopus 로고
    • Visualization of the polarity of isolated titin molecules: A single globular head on a long thin rod as the M Band anchoring domain?
    • Nave R, Fürst DO and Weber K (1989) Visualization of the polarity of isolated titin molecules: a single globular head on a long thin rod as the M Band anchoring domain? J Cell Biol 109: 2177-2187.
    • (1989) J Cell Biol , vol.109 , pp. 2177-2187
    • Nave, R.1    Fürst, D.O.2    Weber, K.3
  • 87
    • 0025320429 scopus 로고
    • Essential problems in quantification of proteins following colloidal staining with coomassie brilliant blue dyes in polyacrylamide gels, and their solution
    • Neuhoff V, Stamm R, Pardowitz I, Arold N, Ehrhardt W and Taube D (1990) Essential problems in quantification of proteins following colloidal staining with coomassie brilliant blue dyes in polyacrylamide gels, and their solution. Electrophoresis 11: 101-117.
    • (1990) Electrophoresis , vol.11 , pp. 101-117
    • Neuhoff, V.1    Stamm, R.2    Pardowitz, I.3    Arold, N.4    Ehrhardt, W.5    Taube, D.6
  • 89
    • 0029644479 scopus 로고
    • Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: A new member of the 1 set
    • Pfuhl M and Pastore A (1995) Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin: a new member of the 1 set. Structure 3: 391-401.
    • (1995) Structure , vol.3 , pp. 391-401
    • Pfuhl, M.1    Pastore, A.2
  • 90
    • 12244291970 scopus 로고    scopus 로고
    • Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein
    • Pizon V, Iakovenko A, van der Ven PF, Kelly R, Fatu C, Fürst DO, Karsenti E and Gautel M (2002) Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein. J Cell Sci 115: 4469-4482.
    • (2002) J Cell Sci , vol.115 , pp. 4469-4482
    • Pizon, V.1    Iakovenko, A.2    Van Der Ven, P.F.3    Kelly, R.4    Fatu, C.5    Fürst, D.O.6    Karsenti, E.7    Gautel, M.8
  • 91
    • 0028834886 scopus 로고
    • The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity
    • Politou AS, Thomas DJ and Pastore A (1995) The folding and stability of titin immunoglobulin-like modules, with implications for the mechanism of elasticity. Biophys J 69: 2601-2610.
    • (1995) Biophys J , vol.69 , pp. 2601-2610
    • Politou, A.S.1    Thomas, D.J.2    Pastore, A.3
  • 93
    • 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
  • 94
    • 0031767965 scopus 로고    scopus 로고
    • The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy
    • Rief M, Gautel M, Schemmel A and Gaub HE (1998) The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy. Biophys J 75: 3008-3014.
    • (1998) Biophys J , vol.75 , pp. 3008-3014
    • Rief, M.1    Gautel, M.2    Schemmel, A.3    Gaub, H.E.4
  • 95
    • 84944818304 scopus 로고
    • The elastic properties of the arterial wall
    • Roy CS (1881) The elastic properties of the arterial wall. J Physiol 3: 125-159.
    • (1881) J Physiol , vol.3 , pp. 125-159
    • Roy, C.S.1
  • 96
    • 0001639575 scopus 로고
    • The connections between A- and I-band filaments in striated frog muscle
    • Sjöstrand F (1962) The connections between A-and I-band filaments in striated frog muscle. J Ultrastruct Res 7: 225-246.
    • (1962) J Ultrastruct Res , vol.7 , pp. 225-246
    • Sjöstrand, F.1
  • 97
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules
    • Smith SB, Cui Y and Bustamante C (1996) Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules. Science 271: 795-799.
    • (1996) Science , vol.271 , pp. 795-799
    • Smith, S.B.1    Cui, Y.2    Bustamante, C.3
  • 98
    • 13344285357 scopus 로고
    • Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence
    • Sorimachi H, Kinbara K, Kimura S, Takahashi M, Ishiura S, Sasagawa N, Sorimachi N, Shimada H, Tagawa K, Maruyama K, et al. (1995) Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence. J Biol Chem 270: 31158-31162.
    • (1995) J Biol Chem , vol.270 , pp. 31158-31162
    • Sorimachi, H.1    Kinbara, K.2    Kimura, S.3    Takahashi, M.4    Ishiura, S.5    Sasagawa, N.6    Sorimachi, N.7    Shimada, H.8    Tagawa, K.9    Maruyama, K.10
  • 99
    • 0028855384 scopus 로고
    • Detection of giant myofibrillar proteins connectin and nebulin by electrophoresis in 2% polyacrylamide slab gels strengthened with agarose
    • Tatsumi R and Hattori A (1995) Detection of giant myofibrillar proteins connectin and nebulin by electrophoresis in 2% polyacrylamide slab gels strengthened with agarose. Anal Biochem 224: 28-31.
    • (1995) Anal Biochem , vol.224 , pp. 28-31
    • Tatsumi, R.1    Hattori, A.2
  • 100
    • 0036089996 scopus 로고    scopus 로고
    • Passive tension of rat skeletal soleus muscle fibers: Effects of unloading conditions
    • Toursel T, Stevens L, Granzier H and Mounier Y (2002) Passive tension of rat skeletal soleus muscle fibers: effects of unloading conditions. J Appl Physiol 92: 1465-1472.
    • (2002) J Appl Physiol , vol.92 , pp. 1465-1472
    • Toursel, T.1    Stevens, L.2    Granzier, H.3    Mounier, Y.4
  • 101
    • 0021591504 scopus 로고
    • Purification and properties of native titin
    • Trinick J, Knight P and Whiting A (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
  • 102
  • 104
    • 0032559640 scopus 로고    scopus 로고
    • Titin extensibility in situ: Entropic elasticity of permanently folded and permanently unfolded molecular segments
    • Trombitas K, Greaser M, Labeit S, Jin JP, 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
    • Trombitas, K.1    Greaser, M.2    Labeit, S.3    Jin, J.P.4    Kellermayer, M.5    Helmes, M.6    Granzier, H.7
  • 105
    • 0030976481 scopus 로고    scopus 로고
    • Interaction between titin and thin filaments in intact cardiac muscle
    • Trombitas 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
    • Trombitas, K.1    Greaser, M.L.2    Pollack, G.H.3
  • 106
    • 0027447329 scopus 로고
    • Elastic properties of titin filaments demonstrated using a 'freeze-break' technique
    • Trombitas K, Pollack GH, Wright J and Wang K (1993) Elastic properties of titin filaments demonstrated using a 'freeze-break' technique. Cell Motil Cytoskeleton 24: 274-283.
    • (1993) Cell Motil Cytoskeleton , vol.24 , pp. 274-283
    • Trombitas, K.1    Pollack, G.H.2    Wright, J.3    Wang, K.4
  • 107
    • 0016273771 scopus 로고
    • Direct evidence for connecting C filaments in flight muscle of honey bee
    • Trombitas K and Tigyi-Sebes A (1974) Direct evidence for connecting C filaments in flight muscle of honey bee. Acta Biochim Biophys Acad Sci Hung 9: 243-253.
    • (1974) Acta Biochim Biophys Acad Sci Hung , vol.9 , pp. 243-253
    • Trombitas, K.1    Tigyi-Sebes, A.2
  • 109
    • 0031575403 scopus 로고    scopus 로고
    • Direct visualization of extensibility in isolated titin molecules
    • Tskhovrebova L and Trinick J (1997) Direct visualization of extensibility in isolated titin molecules. J Mol Biol 265: 100-106.
    • (1997) J Mol Biol , vol.265 , pp. 100-106
    • Tskhovrebova, L.1    Trinick, J.2
  • 110
    • 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
  • 112
    • 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
  • 114
    • 0025816649 scopus 로고
    • Regulation of skeletal muscle stiffness and elasticity by titin isoforms: A test of the segmental extension model of resting tension
    • Wang K, McCarter R, Wright J, Beverly J and Ramirez-Mitchell R (1991) Regulation of skeletal muscle stiffness and elasticity by titin isoforms: a test of the segmental extension model of resting tension. Proc Natl Acad Sci USA 88: 7101-7105.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7101-7105
    • Wang, K.1    McCarter, R.2    Wright, J.3    Beverly, J.4    Ramirez-Mitchell, R.5
  • 115
    • 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 R, Beverly J and Ramirez-Mitchell R (1993) 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) Biophys J , vol.64 , pp. 1161-1177
    • Wang, K.1    McCarter, R.2    Wright, R.3    Beverly, J.4    Ramirez-Mitchell, R.5
  • 116
    • 0011450535 scopus 로고
    • Titin: Major myofibrillar component of striated muscle
    • Wang K, McClure J and Tu A (1979) Titin: major myofibrillar component of striated muscle. Proc Natl Acad Sci USA 76: 3698-3702.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 3698-3702
    • Wang, K.1    McClure, J.2    Tu, A.3
  • 117
    • 0021452202 scopus 로고
    • Titin is an extraordinary long, flexible, and slender myofibrillar protein
    • Wang K, Ramirez-Mitchell R and Palter D (1984) Titin is an extraordinary 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
  • 120
    • 0024961666 scopus 로고
    • Does titin regulate the length of muscle thick filaments?
    • Whiting A, Wardale J and Trinick J (1989) Does titin regulate the length of muscle thick filaments? J Mol Biol 205: 263-268.
    • (1989) J Mol Biol , vol.205 , pp. 263-268
    • Whiting, A.1    Wardale, J.2    Trinick, J.3
  • 121
    • 0023925643 scopus 로고
    • The importance of stretch and contractile activity in the prevention of connective tissue accumulation in muscle
    • Williams PE, Catanese T, Lucey EG and Goldspink G (1988) The importance of stretch and contractile activity in the prevention of connective tissue accumulation in muscle. J Anat 158: 109-114.
    • (1988) J Anat , vol.158 , pp. 109-114
    • Williams, P.E.1    Catanese, T.2    Lucey, E.G.3    Goldspink, G.4
  • 122
    • 0037056103 scopus 로고    scopus 로고
    • Changes in titin isoform expression in pacing-induced cardiac failure give rise to increased passive muscle stiffness
    • Wu Y, Bell SP, Trombitas K, Witt CC, Labeit S, LeWinter MM and Granzier H (2002) Changes in titin isoform expression in pacing-induced cardiac failure give rise to increased passive muscle stiffness. Circulation 106: 1384-1389.
    • (2002) Circulation , vol.106 , pp. 1384-1389
    • Wu, Y.1    Bell, S.P.2    Trombitas, K.3    Witt, C.C.4    Labeit, S.5    LeWinter, M.M.6    Granzier, H.7
  • 123
    • 0034509442 scopus 로고    scopus 로고
    • Changes in titin and collagen underlie diastolic stiffness diversity of cardiac muscle
    • Wu Y, Cazorla O, Labeit D, Labeit S and Granzier H (2000) Changes in titin and collagen underlie diastolic stiffness diversity of cardiac muscle. J Mol Cell Cardiol 32: 2151-2162.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 2151-2162
    • Wu, Y.1    Cazorla, O.2    Labeit, D.3    Labeit, S.4    Granzier, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.