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Volumn 4, Issue 9, 2003, Pages 679-689

Titin: Properties and family relationships

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; MUSCLE PROTEIN;

EID: 0042839620     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1198     Document Type: Review
Times cited : (294)

References (125)
  • 1
    • 0017185581 scopus 로고
    • New elastic protein from muscle
    • Maruyama, K., Natori, R. & Nonomura, Y. New elastic protein from muscle. Nature 262, 58-60 (1976).
    • (1976) Nature , vol.262 , pp. 58-60
    • Maruyama, K.1    Natori, R.2    Nonomura, Y.3
  • 2
    • 0011450535 scopus 로고
    • Titin: Major myofibrillar components of striated muscle
    • Wang, K., McClure, J. & Tu, A. Titin: major myofibrillar components of striated muscle. Proc. Natl Acad. Sci. USA 76, 3698-3702 (1979).
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 3698-3702
    • Wang, K.1    McClure, J.2    Tu, A.3
  • 3
    • 0021279759 scopus 로고
    • Molecular size and shape of β-connectin, an elastic protein of striated muscle
    • Maruyama, K., Kimura, S., Yoshidomi, H., Sawada, H. & Kikuchi, M. Molecular size and shape of β-connectin, an elastic protein of striated muscle. J. Biochem. 95, 1423-1433 (1984).
    • (1984) J. Biochem. , vol.95 , pp. 1423-1433
    • Maruyama, K.1    Kimura, S.2    Yoshidomi, H.3    Sawada, H.4    Kikuchi, M.5
  • 4
    • 0021591504 scopus 로고
    • Purification and properties of native titin
    • Trinick, J., Knight, P. & Whiting, A. Purification and properties of native titin. J. Mol. Biol. 180, 331-356 (1984). Reports the first experimental evidence of the multi-domain structure of titin, as observed by electron microscopy of isolated molecules.
    • (1984) J. Mol. Biol. , vol.180 , pp. 331-356
    • Trinick, J.1    Knight, P.2    Whiting, A.3
  • 5
    • 0021452202 scopus 로고
    • Titin is an extraordinarily long, flexible, and slender myofibrillar protein
    • Wang, K., Ramirez-Mitchell, R. & Palter, D. Titin is an extraordinarily long, flexible, and slender myofibrillar protein. Proc. Natl Acad. Sci. USA 81, 3685-3689 (1984).
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 3685-3689
    • Wang, K.1    Ramirez-Mitchell, R.2    Palter, D.3
  • 6
    • 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., Furst, D. O. & Weber, K. 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). Demonstrates that titin spans half the sarcomere and shows straightened, polar molecules.
    • (1989) J. Cell Biol. , vol.109 , pp. 2177-2187
    • Nave, R.1    Furst, D.O.2    Weber, K.3
  • 7
    • 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, M. L. et al. 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).
    • (2001) Circ. Res. , vol.89 , pp. 1065-1072
    • Bang, M.L.1
  • 8
    • 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
  • 9
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S. & Koimerer, B. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270, 293-296 (1995). Complete titin sequence, including the discovery of splice isoforms.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Koimerer, B.2
  • 10
    • 18544406997 scopus 로고    scopus 로고
    • Series of exon-skipping events in the elastic spring region of titin as the structural basis for myofibrillar elastic diversity
    • Freiburg, A. et al. Series of exon-skipping events in the elastic spring region of titin as the structural basis for myofibrillar elastic diversity. Circ. Res. 86, 1114-1121 (2000).
    • (2000) Circ. Res. , vol.86 , pp. 1114-1121
    • Freiburg, A.1
  • 12
    • 0029892986 scopus 로고    scopus 로고
    • A 11.5-kb 5′-terminal CDNA sequence of chicken breast muscle connectin/titin reveals its Z line binding region
    • Yajima, H. et al. A 11.5-kb 5′-terminal CDNA sequence of chicken breast muscle connectin/titin reveals its Z line binding region. Biochem. Biophys. Res. Comm. 223, 160-164 (1996).
    • (1996) Biochem. Biophys. Res. Comm. , vol.223 , pp. 160-164
    • Yajima, H.1
  • 13
    • 0030076316 scopus 로고    scopus 로고
    • Molecular cloning of a partial cDNA clone encoding the C-terminal region of chicken breast muscle connectin
    • Yajima, H. et al. Molecular cloning of a partial cDNA clone encoding the C-terminal region of chicken breast muscle connectin. Zool. Sci. 13, 119-123 (1996).
    • (1996) Zool. Sci. , vol.13 , pp. 119-123
    • Yajima, H.1
  • 14
    • 0024422164 scopus 로고
    • Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans
    • Benian, G. M., Kiff, J. E., Neckelmann, N., Moerman, D. G. & Waterston, R. H. Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans. Nature 342, 45-50 (1989). First report of an intracellular muscle protein that was shown to be a member of the Ig superfamily.
    • (1989) Nature , vol.342 , pp. 45-50
    • Benian, G.M.1    Kiff, J.E.2    Neckelmann, N.3    Moerman, D.G.4    Waterston, R.H.5
  • 15
    • 0029644479 scopus 로고
    • Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin - A new member of the I-set
    • Pfuhl, M. & Pastore, A. Tertiary structure of an immunoglobulin-like domain from the giant muscle protein titin - a new member of the I-set. Structure 3, 391-401 (1995). Provided the first experimental confirmation of the Ig-like structure of titin domains.
    • (1995) Structure , vol.3 , pp. 391-401
    • Pfuhl, M.1    Pastore, A.2
  • 16
    • 0030584660 scopus 로고    scopus 로고
    • Immunoglobulin-like modules from titin I-band: Extensible components of muscle elasticity
    • Improta, S., Politou, A. S. & Pastore, A. Immunoglobulin-like modules from titin I-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
  • 17
    • 0038083197 scopus 로고    scopus 로고
    • The 3D structure of a type I module from titin: A prototype of intracellular fibronectin type III domains
    • Muhle-Goll, C., Pastore, A. & Nilges, M. The 3D structure of a type I module from titin: a prototype of intracellular fibronectin type III domains. Structure 6, 1291-1302 (1998).
    • (1998) Structure , vol.6 , pp. 1291-1302
    • Muhle-Goll, C.1    Pastore, A.2    Nilges, M.3
  • 18
    • 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. & Wilmanns, M. Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin. Structure 9, 331-340 (2001).
    • (2001) Structure , vol.9 , pp. 331-340
    • Mayans, O.1    Wuerges, J.2    Canela, S.3    Gautel, M.4    Wilmanns, M.5
  • 19
    • 0027246620 scopus 로고
    • Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts
    • Gautel, M., Leonard, K. & Labeit, S. Phosphorylation of KSP motifs in the C-terminal region of titin in differentiating myoblasts. EMBO J. 12, 3827-3834 (1993).
    • (1993) EMBO J. , vol.12 , pp. 3827-3834
    • Gautel, M.1    Leonard, K.2    Labeit, S.3
  • 20
    • 0029143271 scopus 로고
    • Characterization of a 5.4 kb cDNA fragment from the Z-line region of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases
    • Sebestyen, M. G., Wolff, J. A. & Greaser, M. L. Characterization of a 5.4 kb cDNA fragment from the Z-line region of rabbit cardiac titin reveals phosphorylation sites for proline-directed kinases. J. Cell Sci. 108, 3029-3037 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 3029-3037
    • Sebestyen, M.G.1    Wolff, J.A.2    Greaser, M.L.3
  • 21
    • 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
  • 22
    • 0033538417 scopus 로고    scopus 로고
    • Modularity and homology: Modelling of the type II module family from titin
    • Fraternali, F. & Pastore A. Modularity and homology: modelling of the type II module family from titin. J. Mol. Biol. 290, 581-593 (1999).
    • (1999) J. Mol. Biol. , vol.290 , pp. 581-593
    • Fraternali, F.1    Pastore, A.2
  • 23
    • 0035839094 scopus 로고    scopus 로고
    • Modularity and homology: Modelling of the titin type I modules and their interfaces
    • Amodeo, P., Fraternali, F., Lesk, A. M. & Pastore, A. Modularity and homology: modelling of the titin type I modules and their interfaces. J. Mol. Biol. 311, 283-296 (2001).
    • (2001) J. Mol. Biol. , vol.311 , pp. 283-296
    • Amodeo, P.1    Fraternali, F.2    Lesk, A.M.3    Pastore, A.4
  • 24
    • 0032538660 scopus 로고    scopus 로고
    • 2 terminus of titin spans the Z-disc: Its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity
    • 2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity. J. Cell Biol. 143, 1013-1027 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1013-1027
    • Gregorio, C.C.1
  • 25
    • 0031034775 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric M band: Mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin
    • Obermann, W. M. J., Gautel, M., Weber, K. & Furst, D. O. Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin. EMBO J. 16, 211-220 (1997).
    • (1997) EMBO J. , vol.16 , pp. 211-220
    • Obermann, W.M.J.1    Gautel, M.2    Weber, K.3    Furst, D.O.4
  • 26
    • 0029859276 scopus 로고    scopus 로고
    • The central Z-disk region of titin is assembled from a novel repeat in vadable copy numbers
    • Gautel, M., Goulding, D., Bullard, B., Weber, K. & Fürst, D. O. The central Z-disk region of titin is assembled from a novel repeat in vadable copy numbers. J. Cell Sci. 109, 2747-2754 (1996).
    • (1996) J. Cell Sci. , vol.109 , pp. 2747-2754
    • Gautel, M.1    Goulding, D.2    Bullard, B.3    Weber, K.4    Fürst, D.O.5
  • 27
    • 0029919189 scopus 로고    scopus 로고
    • Genomic organization of M line titin and its tissue-specific expression in two distinct isoforms
    • Kolmerer, B., Olivieri, N., Witt, C. C., Herrmann, B. G. & Labeit, S. Genomic organization of M line titin and its tissue-specific expression in two distinct isoforms. J. Mol. Biol. 256, 556-563 (1996).
    • (1996) J. Mol. Biol. , vol.256 , pp. 556-563
    • Kolmerer, B.1    Olivieri, N.2    Witt, C.C.3    Herrmann, B.G.4    Labeit, S.5
  • 28
    • 0031213849 scopus 로고    scopus 로고
    • Tissue-specific expression and α-actinin binding properties of the Z-disc titin: Implications for the nature of vertebrate Z-discs
    • Sorimachi, H. et al. Tissue-specific expression and α-actinin binding properties of the Z-disc titin: implications for the nature of vertebrate Z-discs. J. Mol. Biol. 270, 688-695 (1997).
    • (1997) J. Mol. Biol. , vol.270 , pp. 688-695
    • Sorimachi, H.1
  • 29
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of α-actinin
    • Young, P., Ferguson, C., Banuelos, S. & Gautel, M. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of α-actinin. EMBO J. 17, 1614-1624 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Banuelos, S.3    Gautel, M.4
  • 30
    • 0032557642 scopus 로고    scopus 로고
    • Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin
    • Mues, A., van der Ven, P. F. M., Young, P., Furst, D. O. & Gautel, M. Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin. FEBS Lett. 428, 111-114 (1998).
    • (1998) FEBS Lett. , vol.428 , pp. 111-114
    • Mues, A.1    Van der Ven, P.F.M.2    Young, P.3    Furst, D.O.4    Gautel, M.5
  • 31
    • 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. 154, 123-136 (2001).
    • (2001) J. Cell Biol. , vol.154 , pp. 123-136
    • Young, P.1    Ehler, E.2    Gautel, M.3
  • 32
    • 0030976481 scopus 로고    scopus 로고
    • Interaction between titin and thin filaments in intact cardiac muscle
    • Trombitas, K., Greaser, M. L. & Pollack, G. H. Interaction between titin and thin filaments in intact cardiac muscle. J. Muscle Res. Cell Motil. 18, 345-351 (1997).
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 345-351
    • Trombitas, K.1    Greaser, M.L.2    Pollack, G.H.3
  • 33
    • 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. 235, 317-323 (1996).
    • (1996) Eur. J. Biochem. , vol.235 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 34
    • 0035342456 scopus 로고    scopus 로고
    • Identification of new repeating motifs in titin
    • Greaser, M. Identification of new repeating motifs in titin. Proteins 43, 145-149 (2001).
    • (2001) Proteins , vol.43 , pp. 145-149
    • Greaser, M.1
  • 35
    • 0035831554 scopus 로고    scopus 로고
    • Modular motif, structural folds and affinity profiles of the PEVK segment of human fetal skeletal muscle titin
    • Gutierrez-Cruz, G., Van Heerden, A. H. & Wang, K. Modular motif, structural folds and affinity profiles of the PEVK segment of human fetal skeletal muscle titin. J. Biol. Chem. 276, 7442-7449 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 7442-7449
    • Gutierrez-Cruz, G.1    Van Heerden, A.H.2    Wang, K.3
  • 36
    • 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). Evidence of the preferred conformation of the PEVK polypeptide.
    • (2001) Biochemistry , vol.40 , pp. 3427-3438
    • Ma, K.1    Kan, L.S.2    Wang, K.3
  • 37
    • 0031707518 scopus 로고    scopus 로고
    • Myosin rod-packing schemes in vertebrate muscle thick filaments
    • Squire, J. et al. Myosin rod-packing schemes in vertebrate muscle thick filaments. J. Struct. Biol. 122, 128-138 (1998).
    • (1998) J. Struct. Biol. , vol.122 , pp. 128-138
    • Squire, J.1
  • 38
    • 0033962880 scopus 로고    scopus 로고
    • Differential expression of cardiac titin isoforms and modulation of cellular stiffness
    • Cazorla, O. et al. Differential expression of cardiac titin isoforms and modulation of cellular stiffness. Circ. Res. 86, 59-67 (2000). Evidence for expression of multiple titin isoforms in cardiac muscles.
    • (2000) Circ. Res. , vol.86 , pp. 59-67
    • Cazorla, O.1
  • 40
    • 0032459586 scopus 로고    scopus 로고
    • Muscle thick filaments are rigid coupled tubules, not flexible ropes
    • Schmid, M. F. & Epstein, H. F. Muscle thick filaments are rigid coupled tubules, not flexible ropes. Cell Motil. Cytoskeleton 41, 195-201 (1998).
    • (1998) Cell Motil. Cytoskeleton , vol.41 , pp. 195-201
    • Schmid, M.F.1    Epstein, H.F.2
  • 41
    • 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-Stading mechanism of the heart
    • Muhle-Goll, C. et al. Structural and functional studies of titin's fn3 modules reveal conserved surface patterns and binding to myosin S1 - a possible role in the Frank-Stading mechanism of the heart. J. Mol. Biol. 313, 431-447 (2001).
    • (2001) J. Mol. Biol. , vol.313 , pp. 431-447
    • Muhle-Goll, C.1
  • 42
    • 0024961666 scopus 로고
    • Does titin regulate the length of muscle thick filaments?
    • Whiting, A., Wardale, J. & Trinick, J. Does titin regulate the length of muscle thick filaments? J. Mol. Biol. 205, 263-268 (1989). The protein-ruler model of titin control of thick-filament assembly.
    • (1989) J. Mol. Biol. , vol.205 , pp. 263-268
    • Whiting, A.1    Wardale, J.2    Trinick, J.3
  • 43
    • 0032831174 scopus 로고    scopus 로고
    • Thick filament assembly occurs after the formation of a cytoskeletal scaffold
    • Van der Ven, P. F., Ehler, E., Perriard, J. C. & Furst, D. O. Thick filament assembly occurs after the formation of a cytoskeletal scaffold. J. Muscle Res. Cell Motil. 20, 569-579 (1999).
    • (1999) J. Muscle Res. Cell Motil. , vol.20 , pp. 569-579
    • Van der Ven, P.F.1    Ehler, E.2    Perriard, J.C.3    Furst, D.O.4
  • 44
    • 0034010296 scopus 로고    scopus 로고
    • A functional knock-out of titin results in defective myofibril assembly
    • Van der Ven, P. F., Bartsch, J. W., Gautel, M. Jockusch, H. & Furst, D. O. A functional knock-out of titin results in defective myofibril assembly. J. Cell Sci. 113, 1405-1414 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 1405-1414
    • Van der Ven, P.F.1    Bartsch, J.W.2    Gautel, M.3    Jockusch, H.4    Furst, D.O.5
  • 45
    • 0023047016 scopus 로고
    • A physiological role for titin and nebulin in skeletal muscle
    • Horowits, R., Kempner, E. S., Bisher, M. E. & Podolsky, R. J. A physiological role for titin and nebulin in skeletal muscle, Nature 323, 160-164 (1986). Evidence of how titin centres thick filaments in the sarcomere.
    • (1986) Nature , vol.323 , pp. 160-164
    • Horowits, R.1    Kempner, E.S.2    Bisher, M.E.3    Podolsky, R.J.4
  • 46
    • 0036623918 scopus 로고    scopus 로고
    • Cardiac titin: An adjustable multi-functional spring
    • Granzier, H. & Labeit, S. Cardiac titin: an adjustable multi-functional spring. J. Physiol. 541, 335-342 (2000).
    • (2000) J. Physiol. , vol.541 , pp. 335-342
    • Granzier, H.1    Labeit, S.2
  • 48
    • 0028028999 scopus 로고
    • Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin
    • Erickson, H. P. Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin. Proc. Natl Acad. Sci. USA 91, 10114-10118 (1994). The first theoretical consideration of mechanical unfolding in titin domains.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10114-10118
    • Erickson, H.P.1
  • 50
    • 0031809493 scopus 로고    scopus 로고
    • Characterizing titin's I-band 19 domain region as an entropic spring
    • Unke, W. A., Stockmeier, M. R., Ivemeyer, M., Hosser, H. & Mundel, P. Characterizing titin's I-band 19 domain region as an entropic spring. J. Cell Sci. 111, 1567-1574 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 1567-1574
    • Unke, W.A.1    Stockmeier, M.R.2    Ivemeyer, M.3    Hosser, H.4    Mundel, P.5
  • 51
    • 0031691961 scopus 로고    scopus 로고
    • PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10
    • Trombitas, K., Greaser, M., French, G. & Granzier, H. PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10. J. Struct. Biol. 122, 188-196 (1998).
    • (1998) J. Struct. Biol. , vol.122 , pp. 188-196
    • Trombitas, K.1    Greaser, M.2    French, G.3    Granzier, H.4
  • 52
    • 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. et al. 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).
    • (2000) Biophys. J. , vol.79 , pp. 3226-3234
    • Trombitas, K.1
  • 53
    • 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
  • 54
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer, M. S., 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.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 55
    • 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. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature 387, 308-312 (1997). One of the first measurements of the force-extension relationship of single titin molecules. Unfolding of Ig domains after fast stretches is illustrated (see also references 54 and 58).
    • (1997) Nature , vol.387 , pp. 308-312
    • Tskhovrebova, L.1    Trinick, J.2    Sleep, J.A.3    Simmons, R.4
  • 56
    • 0035845557 scopus 로고    scopus 로고
    • Multiple conformations of PEVK proteins detected by single-molecule techniques
    • Li, H. et al. Multiple conformations of PEVK proteins detected by single-molecule techniques. Proc. Natl Acad. Sci. USA 98, 10682-10686 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10682-10686
    • Li, H.1
  • 57
    • 0037192845 scopus 로고    scopus 로고
    • Molecular mechanics of cardiac titin's PEVK and N2B spring elements
    • Watanabe, K. et al. Molecular mechanics of cardiac titin's PEVK and N2B spring elements. J. Biol. Chem. 277, 11549-11558 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 11549-11558
    • Watanabe, K.1
  • 58
    • 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
  • 60
    • 0037194788 scopus 로고    scopus 로고
    • Reverse engineering of the giant muscle protein titin
    • Li, H. et al. Reverse engineering of the giant muscle protein titin. Nature 418, 998-1002 (2002).
    • (2002) Nature , vol.418 , pp. 998-1002
    • Li, H.1
  • 61
    • 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, M. S. Z., Labeit, S. & Granzier, H. Different molecular mechanics displayed by titin's constitutively and differentially expressed tandem Ig segments. J. Struct. Biol. 137, 248-258 (2002).
    • (2002) J. Struct. Biol. , vol.137 , pp. 248-258
    • Watanabe, K.1    Muhle-Goll, C.2    Kellermayer, M.S.Z.3    Labeit, S.4    Granzier, H.5
  • 62
    • 0035726723 scopus 로고    scopus 로고
    • Sarcomeric visco-elasticity of chemically skinned skeletal muscle fibres of the rabbit at rest
    • Ranatunga, K. W. Sarcomeric visco-elasticity of chemically skinned skeletal muscle fibres of the rabbit at rest. J. Muscle Res. Cell Motil. 22, 399-414 (2001).
    • (2001) J. Muscle Res. Cell Motil. , vol.22 , pp. 399-414
    • Ranatunga, K.W.1
  • 63
    • 0030841266 scopus 로고    scopus 로고
    • A survey of in situ sarcomere extension in mouse skeletal muscle
    • Goulding, D., Bullard, B. & Gautel, M. A survey of in situ sarcomere extension in mouse skeletal muscle. J. Muscle Res. Cell Motil. 18, 465-472 (1997).
    • (1997) J. Muscle Res. Cell Motil. , vol.18 , pp. 465-472
    • Goulding, D.1    Bullard, B.2    Gautel, M.3
  • 64
    • 0036280490 scopus 로고    scopus 로고
    • The effect of core destabilization on the mechanical resistance of 127
    • Brockwell, D. J. et al. The effect of core destabilization on the mechanical resistance of 127. Biophys. J. 83, 458-472 (2002).
    • (2002) Biophys. J. , vol.83 , pp. 458-472
    • Brockwell, D.J.1
  • 65
    • 0037468835 scopus 로고    scopus 로고
    • Hidden complexity in the mechanical properties of titin
    • Williams, P. M. et al. Hidden complexity in the mechanical properties of titin. Nature 422, 446-449 (2003).
    • (2003) Nature , vol.422 , pp. 446-449
    • Williams, P.M.1
  • 66
    • 0035798418 scopus 로고    scopus 로고
    • Specific interaction of the potassium channel β-subunit mink with the sarcomerie protein T-cap suggests a T-tubule-myofibril linking system
    • Furukawa, T. et al. Specific interaction of the potassium channel β-subunit mink with the sarcomerie protein T-cap suggests a T-tubule-myofibril linking system. J. Mol. Biol. 313, 775-784 (2001).
    • (2001) J. Mol. Biol. , vol.313 , pp. 775-784
    • Furukawa, T.1
  • 67
    • 0035793703 scopus 로고    scopus 로고
    • Identification of muscle specific RING finger proteins as potential regulators of the titin kinase domain
    • Cenmer, T. et al. Identification of muscle specific RING finger proteins as potential regulators of the titin kinase domain. J. Mol. Biol. 306, 717-726 (2001).
    • (2001) J. Mol. Biol. , vol.306 , pp. 717-726
    • Cenmer, T.1
  • 68
    • 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, A. S., Kakinuma, K., Sorimachi, H., Labeit, S. & Gregorio, C. C. 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).
    • (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
  • 69
    • 0032578901 scopus 로고    scopus 로고
    • Structural basis for activation of the titin kinase domain during myofibrillogenesis
    • Mayans, O. et al. Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature 395, 863-869 (1998).
    • (1998) Nature , vol.395 , pp. 863-869
    • Mayans, O.1
  • 70
    • 0036406568 scopus 로고    scopus 로고
    • Titins in C. elegans with unusual features: Coiled-coil domains, novel regulation of kinase activity and two new possible elastic regions
    • Flaherty. D. B. et al. Titins in C. elegans with unusual features: coiled-coil domains, novel regulation of kinase activity and two new possible elastic regions. J. Mol. Biol. 323, 533-549 (2002).
    • (2002) J. Mol. Biol. , vol.323 , pp. 533-549
    • Flaherty, D.B.1
  • 71
    • 0026655609 scopus 로고
    • Association of titin and myosin heavy chain in developing skeletal muscle
    • Isaacs, W. B., Kim, I. S., Struve, A. & Fulton, A. B. Association of titin and myosin heavy chain in developing skeletal muscle. Proc. Natl Acad. Sci. USA 89, 7496-7500 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7496-7500
    • Isaacs, W.B.1    Kim, I.S.2    Struve, A.3    Fulton, A.B.4
  • 72
    • 0027279203 scopus 로고
    • Dynamics of actin and assembly of connectin (titin) during myofibrillogenesis in embryonic chick cardiac muscle cells in vitro
    • Komiayama, M., Kouchi, K., Maruyama, K. & Shimada, Y. Dynamics of actin and assembly of connectin (titin) during myofibrillogenesis in embryonic chick cardiac muscle cells in vitro. Dev. Dynam. 196, 291-299 (1993).
    • (1993) Dev. Dynam. , vol.196 , pp. 291-299
    • Komiayama, M.1    Kouchi, K.2    Maruyama, K.3    Shimada, Y.4
  • 73
    • 0032968629 scopus 로고    scopus 로고
    • Organization of connectin/titin filaments in sarcomeres of differentiating chicken skeletal muscle cells
    • Soeno, Y. et al. Organization of connectin/titin filaments in sarcomeres of differentiating chicken skeletal muscle cells. Mol. Cell Biochem. 190, 125-131 (1999).
    • (1999) Mol. Cell Biochem. , vol.190 , pp. 125-131
    • Soeno, Y.1
  • 74
    • 0030913881 scopus 로고    scopus 로고
    • Constitutive and variable regions of Z-disk titin/connectin in myofibril formation: A dominant-negative screen
    • Peckham, M., Young, P. & Gautel, M. Constitutive and variable regions of Z-disk titin/connectin in myofibril formation: a dominant-negative screen. Cell Struct. Funct. 22, 95-101 (1997).
    • (1997) Cell Struct. Funct. , vol.22 , pp. 95-101
    • Peckham, M.1    Young, P.2    Gautel, M.3
  • 75
    • 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. et al. 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).
    • (2002) J. Cell Sci. , vol.115 , pp. 4469-4482
    • Pizon, V.1
  • 76
    • 0036779359 scopus 로고    scopus 로고
    • Titin-Cap associates with, and regulates secretion of myostatin
    • Nicholas, G. et al. Titin-Cap associates with, and regulates secretion of myostatin. J. Cell. Physiol. 193, 120-131 (2002).
    • (2002) J. Cell. Physiol. , vol.193 , pp. 120-131
    • Nicholas, G.1
  • 77
    • 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, R. J. The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin. J. Biol. Chem. 278, 3985-3991 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 3985-3991
    • Kontrogianni-Konstantopoulos, A.1    Bloch, R.J.2
  • 78
    • 0037455559 scopus 로고    scopus 로고
    • Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated mucles
    • Bagnato, P., Barone, V., Giacomello, E., Rossi, D. & Sorrentino, V. Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated mucles. J. Cell Biol. 160, 245-253 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 245-253
    • Bagnato, P.1    Barone, V.2    Giacomello, E.3    Rossi, D.4    Sorrentino, V.5
  • 79
    • 0037458739 scopus 로고    scopus 로고
    • Conditional expression of mutant M-line titins results in cardiomyopathy with altered sarcomere structure
    • Gotthardt, M. et al. Conditional expression of mutant M-line titins results in cardiomyopathy with altered sarcomere structure. J. Biol. Chem. 278, 6059-6065 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 6059-6065
    • Gotthardt, M.1
  • 80
    • 0036478894 scopus 로고    scopus 로고
    • Cardiomyopathy in zebrafish due to mutation in an alternatively spliced exon of titin
    • Xu, X. et al. Cardiomyopathy in zebrafish due to mutation in an alternatively spliced exon of titin. Nature Genet. 30, 205-209 (2002).
    • (2002) Nature Genet. , vol.30 , pp. 205-209
    • Xu, X.1
  • 81
    • 0036478897 scopus 로고    scopus 로고
    • Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy
    • Gerull, B. et al. Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy. Nature Genet. 30, 201-204 (2002).
    • (2002) Nature Genet. , vol.30 , pp. 201-204
    • Gerull, B.1
  • 82
    • 18444408379 scopus 로고    scopus 로고
    • Titin mutations as the molecular basis for dilated cardiomyopathy
    • Itoh-Satoh, M. et al. Titin mutations as the molecular basis for dilated cardiomyopathy. Biochem. Biophys. Res. Comm. 291, 385-393 (2002).
    • (2002) Biochem. Biophys. Res. Comm. , vol.291 , pp. 385-393
    • Itoh-Satoh, M.1
  • 83
    • 0036723943 scopus 로고    scopus 로고
    • Tibial muscular dystrophy is a titinopathy caused by mutations in TTN, the gene encoding the giant skeletal-muscle protein titin
    • Hackman, P. et al. Tibial muscular dystrophy is a titinopathy caused by mutations in TTN, the gene encoding the giant skeletal-muscle protein titin. Am. J. Hum. Genet. 71, 492-500 (2002).
    • (2002) Am. J. Hum. Genet. , vol.71 , pp. 492-500
    • Hackman, P.1
  • 84
    • 0035707910 scopus 로고    scopus 로고
    • The muscular dystrophy with myositis (mdm) mouse mutation disrupts a skeletal muscle-specific domain of titin
    • Garvey, S. M., Rajan, C., Lerner, A. P., Frankel, W. N. & Cox, G. A. The muscular dystrophy with myositis (mdm) mouse mutation disrupts a skeletal muscle-specific domain of titin. Genomics 79, 146-149 (2002).
    • (2002) Genomics , vol.79 , pp. 146-149
    • Garvey, S.M.1    Rajan, C.2    Lerner, A.P.3    Frankel, W.N.4    Cox, G.A.5
  • 85
    • 0034627831 scopus 로고    scopus 로고
    • Requirements of Kettin, a giant muscle protein highly conserved in overall structure in evolution, for normal muscle function, viability, and flight activity of Drosophila
    • Hakeda, S., Endo, S. & Saigo, K. Requirements of Kettin, a giant muscle protein highly conserved in overall structure in evolution, for normal muscle function, viability, and flight activity of Drosophila. J. Cell Biol. 148, 101-114 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 101-114
    • Hakeda, S.1    Endo, S.2    Saigo, K.3
  • 86
    • 0034681283 scopus 로고    scopus 로고
    • Sequence and expression of the kettin gene in Drosophila melanogaster and Caenorhabditis elegans
    • Kolmerer, B. et al. Sequence and expression of the kettin gene in Drosophila melanogaster and Caenorhabditis elegans. J. Mol. Biol. 296, 435-448 (2000).
    • (2000) J. Mol. Biol. , vol.296 , pp. 435-448
    • Kolmerer, B.1
  • 87
    • 0034735537 scopus 로고    scopus 로고
    • D-titin: A giant protein with dual roles in chromosomes and muscles
    • Machado, C. & Andrew, D. J. D-titin: a giant protein with dual roles in chromosomes and muscles. J. Cell Biol. 151, 639-651 (2000).
    • (2000) J. Cell Biol. , vol.151 , pp. 639-651
    • Machado, C.1    Andrew, D.J.2
  • 88
    • 0033824709 scopus 로고    scopus 로고
    • Drosophila D-tilin is required for myoblast fusion and skeletal muscle striation
    • Zhang, Y., Featherstone, D., Davis, W., Rushton, E. & Broadie, K. Drosophila D-tilin is required for myoblast fusion and skeletal muscle striation. J. Cell Sci. 113, 3103-3115 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 3103-3115
    • Zhang, Y.1    Featherstone, D.2    Davis, W.3    Rushton, E.4    Broadie, K.5
  • 89
    • 0035801351 scopus 로고    scopus 로고
    • Invertebrate connectin spans as much as 3.5 μm in the giant sarcomeres of crayfish claw muscle
    • Fukuzawa, A. et al. Invertebrate connectin spans as much as 3.5 μm in the giant sarcomeres of crayfish claw muscle. EMBO J. 20, 4826-4835 (2001). Provides data on a titin-related protein in giant invertebrate muscle sarcomeres and evidence for multiple, unique sequence regions that are related to PEVK.
    • (2001) EMBO J. , vol.20 , pp. 4826-4835
    • Fukuzawa, A.1
  • 90
    • 0034697978 scopus 로고    scopus 로고
    • Drosophila stretchin-MLCK is a novel member of the titin/myosin light chain kinase family
    • Champagne, M. B., Edwards, K. A., Erickson, H. P. & Kiehart, D. P. Drosophila stretchin-MLCK is a novel member of the titin/myosin light chain kinase family. J. Mol. Biol. 300, 759-777 (2000).
    • (2000) J. Mol. Biol. , vol.300 , pp. 759-777
    • Champagne, M.B.1    Edwards, K.A.2    Erickson, H.P.3    Kiehart, D.P.4
  • 91
    • 0035834468 scopus 로고    scopus 로고
    • Alternative splicing of an amino-terminal PEVK-like region generates multiple isoforms of Drosophila projectin
    • Southgate, R. & Ayme-Southgate, A. Alternative splicing of an amino-terminal PEVK-like region generates multiple isoforms of Drosophila projectin. J. Mol. Biol. 313, 1035-1043 (2001).
    • (2001) J. Mol. Biol. , vol.313 , pp. 1035-1043
    • Southgate, R.1    Ayme-Southgate, A.2
  • 92
    • 0035802120 scopus 로고    scopus 로고
    • Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle
    • Kulke, M. et al. Kettin, a major source of myofibrillar stiffness in Drosophila indirect flight muscle. J. Cell Biol. 154, 1045-1057 (2001). Experimental evidence that the smallest titin-related invertebrate proteins might contribute to passive elasticity of muscle.
    • (2001) J. Cell Biol. , vol.154 , pp. 1045-1057
    • Kulke, M.1
  • 93
    • 0033613918 scopus 로고    scopus 로고
    • Association of kettin with actin in the Z-disc of insect flight muscle
    • Van Straaten, M. et al. Association of kettin with actin in the Z-disc of insect flight muscle. J. Mol. Biol. 285, 1549-1562 (1999).
    • (1999) J. Mol. Biol. , vol.285 , pp. 1549-1562
    • Van Straaten, M.1
  • 94
    • 0025636028 scopus 로고
    • Projectin is an invertebrate connectin (titin): Isolation from crayfish claw muscle and localization in crayfish claw muscle and insect flight muscle
    • Hu, D. H. et al. Projectin is an invertebrate connectin (titin): isolation from crayfish claw muscle and localization in crayfish claw muscle and insect flight muscle. J. Muscle Res. Cell Motil. 11, 497-511 (1990).
    • (1990) J. Muscle Res. Cell Motil. , vol.11 , pp. 497-511
    • Hu, D.H.1
  • 95
    • 0025727841 scopus 로고
    • Purification and physical properties of nematode mini-titins and their relation to twitchin
    • Nave, R., Furst, D., Vinkemeier, U. & Weber, K. Purification and physical properties of nematode mini-titins and their relation to twitchin. J. Cell Sci. 98, 491-496 (1991).
    • (1991) J. Cell Sci. , vol.98 , pp. 491-496
    • Nave, R.1    Furst, D.2    Vinkemeier, U.3    Weber, K.4
  • 96
    • 0027748233 scopus 로고
    • Mini-titins in striated and smooth molluscan muscles: Structure, location and immunological crossreactivity
    • Vibert, P., Edelstein, S. M., Castellani, L. & Elliott, B. W. Mini-titins in striated and smooth molluscan muscles: structure, location and immunological crossreactivity. J. Muscle Res. Cell Motil. 14, 598-607 (1993).
    • (1993) J. Muscle Res. Cell Motil. , vol.14 , pp. 598-607
    • Vibert, P.1    Edelstein, S.M.2    Castellani, L.3    Elliott, B.W.4
  • 98
    • 0029584323 scopus 로고
    • Isolation and characterization of a kettin-like protein from crayfish daw muscle
    • Maki, S., Ohtani, Y., Kimura, S. & Maruyama, K. Isolation and characterization of a kettin-like protein from crayfish daw muscle. J. Muscle Res. Cell Motil. 16, 579-585 (1995).
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 579-585
    • Maki, S.1    Ohtani, Y.2    Kimura, S.3    Maruyama, K.4
  • 99
    • 0029827777 scopus 로고    scopus 로고
    • Modular proteins of insect muscle
    • Bullard, B. & Leonard, K. Modular proteins of insect muscle. Adv. Biophys. 33, 211-221 (1996).
    • (1996) Adv. Biophys. , vol.33 , pp. 211-221
    • Bullard, B.1    Leonard, K.2
  • 100
    • 0028017499 scopus 로고
    • Electron microscopic filament lengths of connectin and its fragments
    • Suzuki, J., Kimura, S. & Maruyama, K. Electron microscopic filament lengths of connectin and its fragments. J. Biochem. 116, 406-410 (1994).
    • (1994) J. Biochem. , vol.116 , pp. 406-410
    • Suzuki, J.1    Kimura, S.2    Maruyama, K.3
  • 101
    • 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
  • 102
    • 0022653410 scopus 로고
    • The molecular organization of myosin in stress fibers of cultured cells
    • Langanger, G. et al. The molecular organization of myosin in stress fibers of cultured cells. J. Cell Biol. 102, 200-209 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 200-209
    • Langanger, G.1
  • 103
    • 0024560126 scopus 로고
    • Periodic organization of the contractile apparatus in smooth muscle revealed by the motion of dense bodies in single cells
    • Kargacin, G. J., Cooke, P. H., Abramson, S. B. & Fay, F. S. Periodic organization of the contractile apparatus in smooth muscle revealed by the motion of dense bodies in single cells. J. Cell Biol. 108, 1465-1475 (1989).
    • (1989) J. Cell Biol. , vol.108 , pp. 1465-1475
    • Kargacin, G.J.1    Cooke, P.H.2    Abramson, S.B.3    Fay, F.S.4
  • 104
    • 0032616278 scopus 로고    scopus 로고
    • The genetics and molecular biology of the titin/connectin-like proteins of invertebrates
    • Benian, G. M., Ayme-Southgate, A. & Tinley, T. L. The genetics and molecular biology of the titin/connectin-like proteins of invertebrates. Rev. Physiol. Biochem. Pharmacol. 138, 235-268 (1999).
    • (1999) Rev. Physiol. Biochem. Pharmacol. , vol.138 , pp. 235-268
    • Benian, G.M.1    Ayme-Southgate, A.2    Tinley, T.L.3
  • 105
    • 0032550178 scopus 로고    scopus 로고
    • Human autoantibodies reveal titin as a chromosomal protein
    • Machado, C., Sunkel, C. E. & Andrew, D. J. Human autoantibodies reveal titin as a chromosomal protein. J. Cell Biol. 141, 321-333 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 321-333
    • Machado, C.1    Sunkel, C.E.2    Andrew, D.J.3
  • 106
    • 0032574850 scopus 로고    scopus 로고
    • Phosphorylation of a twitchin-related protein controls catch and calcium sensitivity of force production in invertebrate smooth muscle
    • Siegman, M. J. et al. Phosphorylation of a twitchin-related protein controls catch and calcium sensitivity of force production in invertebrate smooth muscle. Proc. Natl Acad. Sci. USA 95, 5383-5388 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5383-5388
    • Siegman, M.J.1
  • 107
    • 0026730042 scopus 로고
    • Identification and characterization of two huge protein components of the brush border cytoskeleton: Evidence for a cellular isoform of titin
    • Eilertsen, K. J. & Keller, T. C. Identification and characterization of two huge protein components of the brush border cytoskeleton: evidence for a cellular isoform of titin. J. Cell Biol. 119, 549-557 (1992).
    • (1992) J. Cell Biol. , vol.119 , pp. 549-557
    • Eilertsen, K.J.1    Keller, T.C.2
  • 108
    • 0027956823 scopus 로고
    • Cellular titin localization in stress fibers and interaction with myosin II filaments in vitro
    • Eilertsen, K. J., Kazmierski, S. T. & Keller, T. C. Cellular titin localization in stress fibers and interaction with myosin II filaments in vitro. J. Cell Biol. 126, 1201-1210 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 1201-1210
    • Eilertsen, K.J.1    Kazmierski, S.T.2    Keller, T.C.3
  • 109
    • 0037033791 scopus 로고    scopus 로고
    • Smitin, a novel smooth muscle titin-like protein, interacts with myosin filaments in vivo and in vitro
    • Kim, K. & Keller, T. C. Smitin, a novel smooth muscle titin-like protein, interacts with myosin filaments in vivo and in vitro. J. Cell Biol. 156, 101-111 (2002).
    • (2002) J. Cell Biol. , vol.156 , pp. 101-111
    • Kim, K.1    Keller, T.C.2
  • 110
    • 0031918744 scopus 로고    scopus 로고
    • The filament lattice of striated muscle
    • Millman, B. M. The filament lattice of striated muscle. Physiol. Rev. 78, 359-391 (1998).
    • (1998) Physiol. Rev. , vol.78 , pp. 359-391
    • Millman, B.M.1
  • 111
    • 0026668036 scopus 로고
    • Complete primary structure and tissue expression of chicken pectoralis M-protein
    • Noguchi, J. et al. Complete primary structure and tissue expression of chicken pectoralis M-protein. J. Biol. Chem. 267, 20302-20310 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 20302-20310
    • Noguchi, J.1
  • 112
    • 0033557437 scopus 로고    scopus 로고
    • M band proteins myomesin and skelemin are encoded by the same gene: Analysis of its organization and expression
    • Steiner, F., Weber, K., & Furst, D. O. M band proteins myomesin and skelemin are encoded by the same gene: analysis of its organization and expression. Genomics 56, 78-89 (1999).
    • (1999) Genomics , vol.56 , pp. 78-89
    • Steiner, F.1    Weber, K.2    Furst, D.O.3
  • 113
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • Djinovic-Carugo, K., Gautel, M., Ylannec, J. & Young, P. The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Lett. 513, 119-123 (2002).
    • (2002) FEBS Lett. , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylannec, J.3    Young, P.4
  • 114
    • 0030740644 scopus 로고    scopus 로고
    • Rexibility and fine structure of smooth-muscle α-actinin
    • Winkler, J., Lunsdorf, H. & Jockusch, B. M. Rexibility and fine structure of smooth-muscle α-actinin. Eur. J. Biochem. 248, 193-199 (1997).
    • (1997) Eur. J. Biochem. , vol.248 , pp. 193-199
    • Winkler, J.1    Lunsdorf, H.2    Jockusch, B.M.3
  • 115
    • 0027493032 scopus 로고
    • Skelemin, a cytoskeletal M-disc periphery protein, contains motifs of adhesion/recognition and intermediate filament proteins
    • Price, M. G. & Gomer, R. H. Skelemin, a cytoskeletal M-disc periphery protein, contains motifs of adhesion/recognition and intermediate filament proteins. J. Biol. Chem. 268, 21800-21810 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 21800-21810
    • Price, M.G.1    Gomer, R.H.2
  • 116
    • 0027083562 scopus 로고
    • cDNA cloning and sequence comparisons of human and chicken muscle C-protein and 86kD protein
    • Vaughan, K. T., Weber, F. E. & Fischman, D. A. cDNA cloning and sequence comparisons of human and chicken muscle C-protein and 86kD protein. Symp. Soc. Exp. Biol. 46, 167-177 (1992).
    • (1992) Symp. Soc. Exp. Biol. , vol.46 , pp. 167-177
    • Vaughan, K.T.1    Weber, F.E.2    Fischman, D.A.3
  • 117
    • 0029978282 scopus 로고    scopus 로고
    • The Caenorhabditis elegans gene unc-89, required for muscle M-line assembly, encodes a giant modular protein composed of Ig and signal transduction domains
    • Benian, G. M., Tinley, T. L., Tang, X. X. & Borodovsky, M. The Caenorhabditis elegans gene unc-89, required for muscle M-line assembly, encodes a giant modular protein composed of Ig and signal transduction domains. J. Cell Biol. 132, 835-848 (1996).
    • (1996) J. Cell Biol. , vol.132 , pp. 835-848
    • Benian, G.M.1    Tinley, T.L.2    Tang, X.X.3    Borodovsky, M.4
  • 118
    • 0027330127 scopus 로고
    • Molecular characterization of a multi-promoter gene encoding a chicken filamin protein
    • Barry, C. P., Xie, J., Lemmon, V. & Young, A. P. Molecular characterization of a multi-promoter gene encoding a chicken filamin protein. J. Biol. Chem. 268, 25577-25586 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 25577-25586
    • Barry, C.P.1    Xie, J.2    Lemmon, V.3    Young, A.P.4
  • 119
    • 0036447290 scopus 로고    scopus 로고
    • Towards a complete atomic structure of spectrin family proteins
    • Broderick, M. J. F. & Winder, S. J. Towards a complete atomic structure of spectrin family proteins. J. Struct. Biol. 137, 184-193 (2002).
    • (2002) J. Struct. Biol. , vol.137 , pp. 184-193
    • Broderick, M.J.F.1    Winder, S.J.2
  • 120
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • Rief, M., Pascual, J., Saraste, M. & Gaub, H. E. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286, 553-561 (1999).
    • (1999) J. Mol. Biol. , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 121
    • 0035370113 scopus 로고    scopus 로고
    • Mechanical unfolding of single filamin-A (ABP-280) molecules detected by atomic force microscopy
    • Furuike, S., Ito, T. & Yamazaki, M. Mechanical unfolding of single filamin-A (ABP-280) molecules detected by atomic force microscopy. FEBS Lett. 498, 72-75 (2001).
    • (2001) FEBS Lett. , vol.498 , pp. 72-75
    • Furuike, S.1    Ito, T.2    Yamazaki, M.3
  • 122
    • 0025308078 scopus 로고
    • A myofibrillar protein of insect muscle related to vertebrate titin connects Z-band and A-band - Purification and molecular characterization of invertebrate mini-titin
    • Nave, R. & Weber, K. A myofibrillar protein of insect muscle related to vertebrate titin connects Z-band and A-band - purification and molecular characterization of invertebrate mini-titin. J. Cell Sci. 95, 535-544 (1990).
    • (1990) J. Cell Sci. , vol.95 , pp. 535-544
    • Nave, R.1    Weber, K.2
  • 123
    • 0023776666 scopus 로고
    • Identification and intracellular localization of the unc-22 gene product of C. elegans
    • Moerman, D. G., Benian, G. M., Barstead R. J., Scheifer, L. & Waterson, R. H. Identification and intracellular localization of the unc-22 gene product of C. elegans. Genes Dev. 2, 93-105 (1988).
    • (1988) Genes Dev. , vol.2 , pp. 93-105
    • Moerman, D.G.1    Benian, G.M.2    Barstead, R.J.3    Scheifer, L.4    Waterson, R.H.5
  • 124
    • 0025835226 scopus 로고
    • Structurally different Drosophila striated muscles utilize distinct variants of Z-band-associated proteins
    • Vigoreaux, J. O., Saide, J. D. & Pardue, M. L. Structurally different Drosophila striated muscles utilize distinct variants of Z-band-associated proteins. J. Muscle Res. Cell Motil. 12, 340-354 (1991).
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 340-354
    • Vigoreaux, J.O.1    Saide, J.D.2    Pardue, M.L.3
  • 125
    • 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., Labelt, S. & Granzier, H. Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes. Circ. Res. 90, 1181-1188 (2002).
    • (2002) Circ. Res. , vol.90 , pp. 1181-1188
    • Yamasaki, R.1    Wu, Y.2    McNabb, M.3    Greaser, M.4    Labelt, S.5    Granzier, H.6


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