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Volumn 121, Issue 19, 2010, Pages 2137-2145

Cardiac titin: A multifunctional giant

Author keywords

Cardiomyopathy; Diastole; Hypertrophy; Myocardium; Titin

Indexed keywords

CONNECTIN; LIM PROTEIN; PROTEIN KINASE C ALPHA;

EID: 77952481131     PISSN: 00097322     EISSN: 15244539     Source Type: Journal    
DOI: 10.1161/CIRCULATIONAHA.109.860171     Document Type: Review
Times cited : (194)

References (99)
  • 1
    • 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
    • Furst DO, 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. 1988;106: 1563-1572.
    • (1988) J Cell Biol , vol.106 , pp. 1563-1572
    • Furst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 2
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultra-structure and elasticity
    • Labeit S, Kolmerer B. Titins: giant proteins in charge of muscle ultra-structure and elasticity. Science. 1995;270:293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 3
    • 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, Granzier H. Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: titin is an adjustable spring. Circ Res. 1999;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
  • 4
    • 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. 1996;33:123-134.
    • (1996) Adv Biophys , vol.33 , pp. 123-134
    • Wang, K.1
  • 5
    • 0028091960 scopus 로고
    • Titin and nebulin: Protein rulers in muscle?
    • Trinick J. Titin and nebulin: protein rulers in muscle? Trends Biochem Sci. 1994;19:405-409.
    • (1994) Trends Biochem Sci , vol.19 , pp. 405-409
    • Trinick, J.1
  • 8
    • 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 WM, Gautel M, Steiner F, van der Ven PF, Weber K, Furst DO. 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. 1996;134: 1441-1453.
    • (1996) J Cell Biol , vol.134 , pp. 1441-1453
    • Obermann, W.M.1    Gautel, M.2    Steiner, F.3    Van Der Ven, P.F.4    Weber, K.5    Furst, D.O.6
  • 9
    • 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, Labeit S. 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. 2001;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
  • 10
    • 1242281665 scopus 로고    scopus 로고
    • Developmental control of titin isoform expression and passive stiffness in fetal and neonatal myocardium
    • Lahmers S, Wu Y, Call DR, Labeit S, Granzier H. Developmental control of titin isoform expression and passive stiffness in fetal and neonatal myocardium. Circ Res. 2004;94:505-513.
    • (2004) Circ Res , vol.94 , pp. 505-513
    • Lahmers, S.1    Wu, Y.2    Call, D.R.3    Labeit, S.4    Granzier, H.5
  • 11
    • 1842830381 scopus 로고    scopus 로고
    • Develop-mentally regulated switching of titin size alters myofibrillar stiffness in the perinatal heart
    • Opitz CA, Leake MC, Makarenko I, Benes V, Linke WA. Develop-mentally regulated switching of titin size alters myofibrillar stiffness in the perinatal heart. Circ Res. 2004;94:967-975.
    • (2004) Circ Res , vol.94 , pp. 967-975
    • Opitz, C.A.1    Leake, M.C.2    Makarenko, I.3    Benes, V.4    Linke, W.A.5
  • 12
    • 33745698386 scopus 로고    scopus 로고
    • Developmental changes in rat cardiac titin/connectin: Transitions in normal animals and in mutants with a delayed pattern of isoform transition
    • Greaser ML, Krzesinski PR, Warren CM, Kirkpatrick B, Campbell KS, Moss RL. Developmental changes in rat cardiac titin/connectin: transitions in normal animals and in mutants with a delayed pattern of isoform transition. J Muscle Res Cell Motil. 2005;26:325-332.
    • (2005) J Muscle Res Cell Motil , vol.26 , pp. 325-332
    • Greaser, M.L.1    Krzesinski, P.R.2    Warren, C.M.3    Kirkpatrick, B.4    Campbell, K.S.5    Moss, R.L.6
  • 13
    • 0029143981 scopus 로고
    • The mechanically active domain of titin in cardiac muscle
    • Trombitas K, Jin JP, Granzier H. The mechanically active domain of titin in cardiac muscle. Circ Res. 1995;77:856-861.
    • (1995) Circ Res , vol.77 , pp. 856-861
    • Trombitas, K.1    Jin, J.P.2    Granzier, H.3
  • 15
    • 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, Gregorio CC. I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure. J Cell Biol. 1999;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
  • 19
    • 18744374455 scopus 로고    scopus 로고
    • Different molecular mechanics displayed by titin's constitutively and differentially expressed tandem Ig segments
    • Watanabe K, Muhle-Goll C, Kellermayer MS, Labeit S, Granzier H. Different molecular mechanics displayed by titin's constitutively and differentially expressed tandem Ig segments. J Struct Biol. 2002;137: 248-258.
    • (2002) J Struct Biol , vol.137 , pp. 248-258
    • Watanabe, K.1    Muhle-Goll, C.2    Kellermayer, M.S.3    Labeit, S.4    Granzier, H.5
  • 20
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer MS, Smith SB, Granzier HL, Bustamante C. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science. 1997;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
  • 22
    • 0031795571 scopus 로고    scopus 로고
    • A spring tale: New facts on titin elasticity
    • Linke WA, Granzier H. A spring tale: new facts on titin elasticity. Biophys J. 1998;75:2613-2614.
    • (1998) Biophys J , vol.75 , pp. 2613-2614
    • Linke, W.A.1    Granzier, H.2
  • 23
    • 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
    • Trombitas K, Redkar A, Centner T, Wu Y, Labeit S, Granzier H. Extensibility of isoforms of cardiac titin: variation in contour length of molecular subsegments provides a basis for cellular passive stiffness diversity. Biophys J. 2000;79:3226-3234.
    • (2000) Biophys J , vol.79 , pp. 3226-3234
    • Trombitas, K.1    Redkar, A.2    Centner, T.3    Wu, Y.4    Labeit, S.5    Granzier, H.6
  • 25
    • 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, Granzier H. Changes in titin and collagen underlie diastolic stiffness diversity of cardiac muscle. J Mol Cell Cardiol. 2000;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
  • 28
    • 0037076791 scopus 로고    scopus 로고
    • Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes
    • Yamasaki R, Wu Y, McNabb M, Greaser M, Labeit S, Granzier H. Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes. Circ Res. 2002;90: 1181-1188.
    • (2002) Circ Res , vol.90 , pp. 1181-1188
    • Yamasaki, R.1    Wu, Y.2    McNabb, M.3    Greaser, M.4    Labeit, S.5    Granzier, H.6
  • 29
    • 15244348075 scopus 로고    scopus 로고
    • Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner
    • Fukuda N, Wu Y, Nair P, Granzier HL. Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner. J Gen Physiol. 2005;125:257-271.
    • (2005) J Gen Physiol , vol.125 , pp. 257-271
    • Fukuda, N.1    Wu, Y.2    Nair, P.3    Granzier, H.L.4
  • 30
    • 33748329623 scopus 로고    scopus 로고
    • Protein kinase-A phosphorylates titin in human heart muscle and reduces myofibrillar passive tension
    • Kruger M, Linke WA. Protein kinase-A phosphorylates titin in human heart muscle and reduces myofibrillar passive tension. J Muscle Res Cell Motil. 2006;27:435-444.
    • (2006) J Muscle Res Cell Motil , vol.27 , pp. 435-444
    • Kruger, M.1    Linke, W.A.2
  • 32
    • 35348870623 scopus 로고    scopus 로고
    • Cyclic GMP and protein kinase-G in myocardial ischaemia-reperfusion: Opportunities and obstacles for survival signaling
    • Burley DS, Ferdinandy P, Baxter GF. Cyclic GMP and protein kinase-G in myocardial ischaemia-reperfusion: opportunities and obstacles for survival signaling. Br J Pharmacol. 2007;152:855-869.
    • (2007) Br J Pharmacol , vol.152 , pp. 855-869
    • Burley, D.S.1    Ferdinandy, P.2    Baxter, G.F.3
  • 33
    • 70349668973 scopus 로고    scopus 로고
    • PKC phosphorylation of titin's PEVK element: A novel and conserved pathway for modulating myocardial stiffness
    • Hidalgo C, Hudson B, Bogomolovas J, Zhu Y, Anderson B, Greaser M, Labeit S, Granzier H. PKC phosphorylation of titin's PEVK element: a novel and conserved pathway for modulating myocardial stiffness. Circ Res. 2009;105:631-638.
    • (2009) Circ Res , vol.105 , pp. 631-638
    • Hidalgo, C.1    Hudson, B.2    Bogomolovas, J.3    Zhu, Y.4    Anderson, B.5    Greaser, M.6    Labeit, S.7    Granzier, H.8
  • 34
    • 68849089514 scopus 로고    scopus 로고
    • Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2-B unique sequence
    • Grutzner A, Garcia-Manyes S, Kotter S, Badilla CL, Fernandez JM, Linke WA. Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2-B unique sequence. Biophys J. 2009;97:825-834.
    • (2009) Biophys J , vol.97 , pp. 825-834
    • Grutzner, A.1    Garcia-Manyes, S.2    Kotter, S.3    Badilla, C.L.4    Fernandez, J.M.5    Linke, W.A.6
  • 35
    • 0030022007 scopus 로고    scopus 로고
    • Calcium-dependent inhibition of in vitro thin-filament motility by native titin
    • Kellermayer MS, Granzier HL. Calcium-dependent inhibition of in vitro thin-filament motility by native titin. FEBS Lett. 1996;380:281-286.
    • (1996) FEBS Lett , vol.380 , pp. 281-286
    • Kellermayer, M.S.1    Granzier, H.L.2
  • 40
    • 0029823455 scopus 로고    scopus 로고
    • Titin develops restoring force in rat cardiac myocytes
    • Helmes M, Trombitas K, Granzier H. Titin develops restoring force in rat cardiac myocytes. Circ Res. 1996;79:619-626.
    • (1996) Circ Res , vol.79 , pp. 619-626
    • Helmes, M.1    Trombitas, K.2    Granzier, H.3
  • 43
    • 33750874300 scopus 로고    scopus 로고
    • Effects of dobutamine on left ventricular restoring forces
    • Bell SP, Fabian J, LeWinter MM. Effects of dobutamine on left ventricular restoring forces. Am J Physiol. 1998;275:H190-H194.
    • (1998) Am J Physiol , vol.275
    • Bell, S.P.1    Fabian, J.2    Lewinter, M.M.3
  • 44
    • 33646144466 scopus 로고    scopus 로고
    • An X-ray diffraction study on mouse cardiac cross-bridge function in vivo: Effects of adrenergic [beta]-stimulation
    • Toh R, Shinohara M, Takaya T, Yamashita T, Masuda S, Kawashima S, Yokoyama M, Yagi N. An X-ray diffraction study on mouse cardiac cross-bridge function in vivo: effects of adrenergic [beta]-stimulation. Biophys J. 2006;90:1723-1728.
    • (2006) Biophys J , vol.90 , pp. 1723-1728
    • Toh, R.1    Shinohara, M.2    Takaya, T.3    Yamashita, T.4    Masuda, S.5    Kawashima, S.6    Yokoyama, M.7    Yagi, N.8
  • 45
    • 36349031141 scopus 로고    scopus 로고
    • Cardiac troponin i threonine 144: Role in myofilament length dependent activation
    • Tachampa K, Wang H, Farman GP, de Tombe PP. Cardiac troponin I threonine 144: role in myofilament length dependent activation. Circ Res. 2007;101:1081-1083.
    • (2007) Circ Res , vol.101 , pp. 1081-1083
    • Tachampa, K.1    Wang, H.2    Farman, G.P.3    De Tombe, P.P.4
  • 46
    • 0033151961 scopus 로고    scopus 로고
    • Length modulation of active force in rat cardiac myocytes: Is titin the sensor?
    • Cazorla O, Vassort G, Garnier D, Le Guennec JY. Length modulation of active force in rat cardiac myocytes: is titin the sensor? J Mol Cell Cardiol. 1999;31:1215-1227.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 1215-1227
    • Cazorla, O.1    Vassort, G.2    Garnier, D.3    Le Guennec, J.Y.4
  • 47
    • 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, Granzier H. Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes. Circ Res. 2001;88:1028-1035.
    • (2001) Circ Res , vol.88 , pp. 1028-1035
    • Cazorla, O.1    Wu, Y.2    Irving, T.C.3    Granzier, H.4
  • 48
    • 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, Kurihara S. Length dependence of tension generation in rat skinned cardiac muscle: role of titin in the Frank-Starling mechanism of the heart. Circulation. 2001;104: 1639-1645. (Pubitemid 32947527)
    • (2001) Circulation , vol.104 , Issue.14 , pp. 1639-1645
    • Fukuda, N.1    Sasaki, D.2    Ishiwata, S.3    Kurihara, S.4
  • 49
    • 0344896768 scopus 로고    scopus 로고
    • Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle
    • Fukuda N, Wu Y, Farman G, Irving TC, Granzier H. Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle. J Physiol. 2003;553:147-154.
    • (2003) J Physiol , vol.553 , pp. 147-154
    • Fukuda, N.1    Wu, Y.2    Farman, G.3    Irving, T.C.4    Granzier, H.5
  • 50
    • 13744262391 scopus 로고    scopus 로고
    • Titin-based modulation of active tension and interfilament lattice spacing in skinned rat cardiac muscle
    • Fukuda N, Wu Y, Farman G, Irving TC, Granzier H. Titin-based modulation of active tension and interfilament lattice spacing in skinned rat cardiac muscle. Pflugers Arch. 2005;449:449-457.
    • (2005) Pflugers Arch , vol.449 , pp. 449-457
    • Fukuda, N.1    Wu, Y.2    Farman, G.3    Irving, T.C.4    Granzier, H.5
  • 52
    • 45349086526 scopus 로고    scopus 로고
    • Physiological functions of the giant elastic protein titin in mammalian striated muscle
    • Fukuda N, Granzier HL, Ishiwata S, Kurihara S. Physiological functions of the giant elastic protein titin in mammalian striated muscle. J Physiol Sci. 2008;58:151-159.
    • (2008) J Physiol Sci , vol.58 , pp. 151-159
    • Fukuda, N.1    Granzier, H.L.2    Ishiwata, S.3    Kurihara, S.4
  • 53
    • 0037423366 scopus 로고    scopus 로고
    • The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin
    • Kontrogianni-Konstantopoulos A, Bloch RJ. The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin. J Biol Chem. 2003;278:3985-3991.
    • (2003) J Biol Chem , vol.278 , pp. 3985-3991
    • Kontrogianni-Konstantopoulos, A.1    Bloch, R.J.2
  • 56
    • 0029859276 scopus 로고    scopus 로고
    • The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers
    • Gautel M, Goulding D, Bullard B, Weber K, Furst DO. The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers. J Cell Sci. 1996;109(pt 11):2747-2754.
    • (1996) J Cell Sci , vol.109 , Issue.PART 11 , pp. 2747-2754
    • Gautel, M.1    Goulding, D.2    Bullard, B.3    Weber, K.4    Furst, D.O.5
  • 57
    • 0035798418 scopus 로고    scopus 로고
    • Specific interaction of the potassium channel beta-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system
    • Furukawa T, Ono Y, Tsuchiya H, Katayama Y, Bang ML, Labeit D, Labeit S, Inagaki N, Gregorio CC. Specific interaction of the potassium channel beta-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system. J Mol Biol. 2001;313:775-784.
    • (2001) J Mol Biol , vol.313 , pp. 775-784
    • Furukawa, T.1    Ono, Y.2    Tsuchiya, H.3    Katayama, Y.4    Bang, M.L.5    Labeit, D.6    Labeit, S.7    Inagaki, N.8    Gregorio, C.C.9
  • 59
    • 62449236060 scopus 로고    scopus 로고
    • Back to square one: What do we know about the functions of muscle LIM protein in the heart?
    • Gehmlich K, Geier C, Milting H, Furst D, Ehler E. Back to square one: what do we know about the functions of muscle LIM protein in the heart? J Muscle Res Cell Motil. 2008;29:155-158.
    • (2008) J Muscle Res Cell Motil , vol.29 , pp. 155-158
    • Gehmlich, K.1    Geier, C.2    Milting, H.3    Furst, D.4    Ehler, E.5
  • 61
    • 0036951869 scopus 로고    scopus 로고
    • Desmin filaments and cardiac disease: Establishing causality
    • Wang X, Osinska H, Gerdes AM, Robbins J. Desmin filaments and cardiac disease: establishing causality. J Card Fail. 2002;8:S287-S292.
    • (2002) J Card Fail , vol.8
    • Wang, X.1    Osinska, H.2    Gerdes, A.M.3    Robbins, J.4
  • 62
    • 67649399290 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of the cardiac titin N2B element: Effects of the molecular chaperone alphaB-crystallin with disease-causing mutations
    • Zhu Y, Bogomolovas J, Labeit S, Granzier H. Single molecule force spectroscopy of the cardiac titin N2B element: effects of the molecular chaperone alphaB-crystallin with disease-causing mutations. J Biol Chem. 2009;284:13914-13923.
    • (2009) J Biol Chem , vol.284 , pp. 13914-13923
    • Zhu, Y.1    Bogomolovas, J.2    Labeit, S.3    Granzier, H.4
  • 64
    • 0034234785 scopus 로고    scopus 로고
    • Expression patterns of FHL/SLIM family members suggest important functional roles in skeletal muscle and cardiovascular system
    • Chu PH, Ruiz-Lozano P, Zhou Q, Cai C, Chen J. Expression patterns of FHL/SLIM family members suggest important functional roles in skeletal muscle and cardiovascular system. Mech Dev. 2000;95:259-265.
    • (2000) Mech Dev , vol.95 , pp. 259-265
    • Chu, P.H.1    Ruiz-Lozano, P.2    Zhou, Q.3    Cai, C.4    Chen, J.5
  • 70
    • 0032033322 scopus 로고    scopus 로고
    • Expression of genes (CAPN3, SGCA, SGCB, and TTN) involved in progressive muscular dystrophies during early human development
    • Fougerousse F, Durand M, Suel L, Pourquie O, Delezoide AL, Romero NB, Abitbol M, Beckmann JS. Expression of genes (CAPN3, SGCA, SGCB, and TTN) involved in progressive muscular dystrophies during early human development. Genomics. 1998;48:145-156.
    • (1998) Genomics , vol.48 , pp. 145-156
    • Fougerousse, F.1    Durand, M.2    Suel, L.3    Pourquie, O.4    Delezoide, A.L.5    Romero, N.B.6    Abitbol, M.7    Beckmann, J.S.8
  • 71
    • 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. 1996;235: 317-323.
    • (1996) Eur J Biochem , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 72
    • 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, Granzier H. 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. 2001;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
  • 73
    • 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. 1992;11:1711-1716.
    • (1992) EMBO J , vol.11 , pp. 1711-1716
    • Labeit, S.1    Gautel, M.2    Lakey, A.3    Trinick, J.4
  • 75
    • 33646798022 scopus 로고    scopus 로고
    • M line-deficient titin causes cardiac lethality through impaired maturation of the sarcomere
    • Weinert S, Bergmann N, Luo X, Erdmann B, Gotthardt M. M line-deficient titin causes cardiac lethality through impaired maturation of the sarcomere. J Cell Biol. 2006;173:559-570.
    • (2006) J Cell Biol , vol.173 , pp. 559-570
    • Weinert, S.1    Bergmann, N.2    Luo, X.3    Erdmann, B.4    Gotthardt, M.5
  • 76
  • 77
    • 20544438018 scopus 로고    scopus 로고
    • MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: Towards understanding MURF-dependent muscle ubiquitination
    • Witt SH, Granzier H, Witt CC, Labeit S. MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: towards understanding MURF-dependent muscle ubiquitination. J Mol Biol. 2005;350: 713-722.
    • (2005) J Mol Biol , vol.350 , pp. 713-722
    • Witt, S.H.1    Granzier, H.2    Witt, C.C.3    Labeit, S.4
  • 78
    • 4344598187 scopus 로고    scopus 로고
    • Muscle-specific RING finger-2 (MURF-2) is important for microtubule, intermediate filament and sarcomeric M-line maintenance in striated muscle development
    • McElhinny AS, Perry CN, Witt CC, Labeit S, Gregorio CC. Muscle-specific RING finger-2 (MURF-2) is important for microtubule, intermediate filament and sarcomeric M-line maintenance in striated muscle development. J Cell Sci. 2004;117:3175-3188.
    • (2004) J Cell Sci , vol.117 , pp. 3175-3188
    • McElhinny, A.S.1    Perry, C.N.2    Witt, C.C.3    Labeit, S.4    Gregorio, C.C.5
  • 80
    • 0031172869 scopus 로고    scopus 로고
    • Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, A unique region flanked by two immunoglobulin C2 motifs
    • Kinbara K, Sorimachi H, Ishiura S, Suzuki K. Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs. Arch Biochem Biophys. 1997;342:99-107.
    • (1997) Arch Biochem Biophys , vol.342 , pp. 99-107
    • Kinbara, K.1    Sorimachi, H.2    Ishiura, S.3    Suzuki, K.4
  • 81
    • 0035833261 scopus 로고    scopus 로고
    • Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly
    • Young P, Ehler E, Gautel M. Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly. J Cell Biol. 2001;154:123-136.
    • (2001) J Cell Biol , vol.154 , pp. 123-136
    • Young, P.1    Ehler, E.2    Gautel, M.3
  • 82
    • 46749123127 scopus 로고    scopus 로고
    • Interactions with titin and myomesin target obscurin and obscurin-like 1 to the M-band: Implications for hereditary myopathies
    • Fukuzawa A, Lange S, Holt M, Vihola A, Carmignac V, Ferreiro A, Udd B, Gautel M. Interactions with titin and myomesin target obscurin and obscurin-like 1 to the M-band: implications for hereditary myopathies. J Cell Sci. 2008;121:1841-1851.
    • (2008) J Cell Sci , vol.121 , pp. 1841-1851
    • Fukuzawa, A.1    Lange, S.2    Holt, M.3    Vihola, A.4    Carmignac, V.5    Ferreiro, A.6    Udd, B.7    Gautel, M.8
  • 83
    • 67650747244 scopus 로고    scopus 로고
    • Stressing the giant: A new approach to understanding dilated cardiomyopathy
    • Greaser ML. Stressing the giant: a new approach to understanding dilated cardiomyopathy. J Mol Cell Cardiol. 2009;47:347-349.
    • (2009) J Mol Cell Cardiol , vol.47 , pp. 347-349
    • Greaser, M.L.1
  • 86
    • 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, Granzier H. Changes in titin isoform expression in pacing-induced cardiac failure give rise to increased passive muscle stiffness. Circulation. 2002;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
  • 87
    • 61449149648 scopus 로고    scopus 로고
    • Titin isoforms, extracellular matrix, and global chamber remodeling in experimental dilated cardiomyopathy: Functional implications and mechanistic insight
    • Jaber WA, Maniu C, Krysiak J, Shapiro BP, Meyer DM, Linke WA, Redfield MM. Titin isoforms, extracellular matrix, and global chamber remodeling in experimental dilated cardiomyopathy: functional implications and mechanistic insight. Circ Heart Fail. 2008;1:192-199.
    • (2008) Circ Heart Fail , vol.1 , pp. 192-199
    • Jaber, W.A.1    Maniu, C.2    Krysiak, J.3    Shapiro, B.P.4    Meyer, D.M.5    Linke, W.A.6    Redfield, M.M.7
  • 91
    • 0036947533 scopus 로고    scopus 로고
    • Titin: An endosarcomeric protein that modulates myocardial stiffness in DCM
    • Wu Y, Labeit S, Lewinter MM, Granzier H. Titin: an endosarcomeric protein that modulates myocardial stiffness in DCM. J Card Fail. 2002; 8:S276-S286.
    • (2002) J Card Fail , vol.8
    • Wu, Y.1    Labeit, S.2    Lewinter, M.M.3    Granzier, H.4
  • 96
    • 33749537840 scopus 로고    scopus 로고
    • Diastolic dysfunction and diabetic cardiomyopathy: Evaluation by Doppler echocardiography
    • Galderisi M. Diastolic dysfunction and diabetic cardiomyopathy: evaluation by Doppler echocardiography. J Am Coll Cardiol. 2006;48: 1548-1551.
    • (2006) J Am Coll Cardiol , vol.48 , pp. 1548-1551
    • Galderisi, M.1
  • 97
    • 33845605523 scopus 로고    scopus 로고
    • Hypothyroidism leads to increased collagen-based stiffness and re-expression of large cardiac titin isoforms with high compliance
    • Wu Y, Peng J, Campbell KB, Labeit S, Granzier H. Hypothyroidism leads to increased collagen-based stiffness and re-expression of large cardiac titin isoforms with high compliance. J Mol Cell Cardiol. 2007;42:186-195.
    • (2007) J Mol Cell Cardiol , vol.42 , pp. 186-195
    • Wu, Y.1    Peng, J.2    Campbell, K.B.3    Labeit, S.4    Granzier, H.5
  • 98
    • 41949113903 scopus 로고    scopus 로고
    • Thyroid hormone regulates developmental titin isoform transitions via the phosphatidylinositol-3-kinase/AKT pathway
    • Kruger M, Sachse C, Zimmermann WH, Eschenhagen T, Klede S, Linke WA. Thyroid hormone regulates developmental titin isoform transitions via the phosphatidylinositol-3-kinase/AKT pathway. Circ Res. 2008;102: 439-447.
    • (2008) Circ Res , vol.102 , pp. 439-447
    • Kruger, M.1    Sachse, C.2    Zimmermann, W.H.3    Eschenhagen, T.4    Klede, S.5    Linke, W.A.6


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