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Volumn 323, Issue 3, 2002, Pages 533-549

Titins in C. elegans with unusual features: Coiled-coil domains, novel regulation of kinase activity and two new possible elastic regions

Author keywords

C. elegans; Ig superfamily; Muscle; Repeating motifs; Titin

Indexed keywords

CONNECTIN; IMMUNOGLOBULIN; ISOPROTEIN; MUSCLE PROTEIN; PHOSPHOTRANSFERASE; POLYPEPTIDE; PROTEIN KINASE;

EID: 0036406568     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00970-1     Document Type: Article
Times cited : (41)

References (67)
  • 1
    • 0011450535 scopus 로고
    • Titin: Major myofibrillar components of striated muscle
    • Wang, K., McClure, J. & Tu, A. (1979). Titin: Major myofibrillar components 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
  • 2
    • 0017163222 scopus 로고
    • Connectin, an elastic protein from myofibrils
    • Maruyama, K. (1976). Connectin, an elastic protein from myofibrils. J. Biochem. 80, 405-407.
    • (1976) J. Biochem. , vol.80 , pp. 405-407
    • Maruyama, K.1
  • 5
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S. & 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
  • 6
    • 0032602766 scopus 로고    scopus 로고
    • Control of sarcomeric assembly: The flow of information on titin
    • Gautel, M., Mues, A. & Young, P. (1999). Control of sarcomeric assembly: The flow of information on titin. Rev. Physiol. Biochem. Pharmacol. 138, 98-137.
    • (1999) Rev. Physiol. Biochem. Pharmacol. , vol.138 , pp. 98-137
    • Gautel, M.1    Mues, A.2    Young, P.3
  • 7
    • 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. (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
  • 8
    • 0024961666 scopus 로고
    • Does titin regulate the length of muscle thick filaments?
    • Whiting, A., Wardale, J. & 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
  • 9
    • 0035941407 scopus 로고    scopus 로고
    • The complete gene sequence of titin, expression of an unusual ∼700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system
    • Bang, M.-L., Centner, T., Fornoff, F., Geach, A. J., Gotthardt, M., McNabb, M. et al. (2001). The complete gene sequence of titin, expression of an unusual ∼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
  • 10
    • 0031795571 scopus 로고    scopus 로고
    • A spring tale: New facts on titin elasticity
    • Linke, W. A. & 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
  • 11
    • 0036623918 scopus 로고    scopus 로고
    • Cardiac titin: An adjustable multi-functional spring
    • Granzier, H. & Labeit, S. (2002). Cardiac titin: An adjustable multi-functional spring. J. Physiol. 541.2, 335-342.
    • (2002) J. Physiol. , vol.5412 , pp. 335-342
    • Granzier, H.1    Labeit, S.2
  • 12
    • 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. (2000). Drosophila stretchin-MLCK is a novel member of the titin/myosin light chain kinase family. J. Mol. Biol. 300, 759-777.
    • (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
  • 13
    • 18544406997 scopus 로고    scopus 로고
    • Series of exon-skipping events in the elastic spring region of titin as the structural basis of myofibrillar elastic diversity
    • Freiburg, A., Trombitas, K., Hell, W., Cazorla, O., Fougerousse, F., Centner, T. et al. (2000). Series of exon-skipping events in the elastic spring region of titin as the structural basis of myofibrillar elastic diversity. Circ. Res. 86, 1114-1121.
    • (2000) Circ. Res. , vol.86 , pp. 1114-1121
    • Freiburg, A.1    Trombitas, K.2    Hell, W.3    Cazorla, O.4    Fougerousse, F.5    Centner, T.6
  • 14
    • 0035831554 scopus 로고    scopus 로고
    • Modular motif, structural folds and affinity profiles of PEVK segment of human fetal skeletal muscle titin
    • Gutierrez-Cruz, G., Van Heerden, A. & Wang, K. (2001). Modular motif, structural folds and affinity profiles of PEVK segment of human fetal skeletal muscle titin. J. Biol. Chem. 276, 7442-7449.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7442-7449
    • Gutierrez-Cruz, G.1    Van Heerden, A.2    Wang, K.3
  • 15
    • 0035342456 scopus 로고    scopus 로고
    • Identification of new repeating motifs in titin
    • Greaser, M. (2001). Identification of new repeating motifs in titin. Proteins: Struct. Funct. Genet. 43, 145-149.
    • (2001) Proteins: Struct. Funct. Genet. , vol.43 , pp. 145-149
    • Greaser, M.1
  • 16
    • 0035957219 scopus 로고    scopus 로고
    • Polyproline II helix is a key structural motif of the elastic PEVK segment of titin
    • Ma, K., Kan, L. & Wang, K. (2001). Polyproline II helix is a key structural motif of the elastic PEVK segment of titin. Biochemistry, 40, 3427-3438.
    • (2001) Biochemistry , vol.40 , pp. 3427-3438
    • Ma, K.1    Kan, L.2    Wang, K.3
  • 17
    • 0034811015 scopus 로고    scopus 로고
    • Titin-actin interaction in mouse myocardium: Passive tension modulation and its regulation by calcium/S100A1
    • Yamasaki, R., Berri, M., Wu, Y., Trombitas, K., McNabb, M., Kellermayer, M. S. Z. et al. (2001). Titin-actin interaction in mouse myocardium: Passive tension modulation and its regulation by calcium/S100A1. Biophys. J. 81, 2297-2313.
    • (2001) Biophys. J. , vol.81 , pp. 2297-2313
    • Yamasaki, R.1    Berri, M.2    Wu, Y.3    Trombitas, K.4    McNabb, M.5    Kellermayer, M.S.Z.6
  • 19
    • 0036478897 scopus 로고    scopus 로고
    • Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy
    • Gerull, B., Gramlich, M., Atherton, J., McNabb, M., Trombitas, K., Sasse-Klaassen, S. et al. (2002). Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy. Nature Genet. 30, 201-204.
    • (2002) Nature Genet. , vol.30 , pp. 201-204
    • Gerull, B.1    Gramlich, M.2    Atherton, J.3    McNabb, M.4    Trombitas, K.5    Sasse-Klaassen, S.6
  • 21
    • 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., Vihola, A., Haravuori, H., Marchand, S., Sarparanta, J., de Seze, J. et al. (2002). 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) Am. J. Hum. Genet. , vol.71 , pp. 492-500
    • Hackman, P.1    Vihola, A.2    Haravuori, H.3    Marchand, S.4    Sarparanta, J.5    De Seze, J.6
  • 22
    • 0032550178 scopus 로고    scopus 로고
    • Human autoantibodies reveal titin as a chromosomal protein
    • Machado, C., Sunkel, C. E. & Andrew, D. J. (1998). Human autoantibodies reveal titin as a chromosomal protein. J. Cell Biol. 141, 321-333.
    • (1998) J. Cell Biol. , vol.141 , pp. 321-333
    • Machado, C.1    Sunkel, C.E.2    Andrew, D.J.3
  • 23
    • 0034735537 scopus 로고    scopus 로고
    • D-TITIN: A giant protein with dual roles in chromosomes and muscles
    • Machado, C. & Andrew, D. J. (2000). D-TITIN: A giant protein with dual roles in chromosomes and muscles. J. Cell Biol. 151, 639-651.
    • (2000) J. Cell Biol. , vol.151 , pp. 639-651
    • Machado, C.1    Andrew, D.J.2
  • 24
    • 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. (1989). Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans. Nature, 342, 45-50.
    • (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
  • 25
    • 0027237468 scopus 로고
    • Additional sequence complexity in the muscle gene unc-22 and its encoded protein, twitchin, of C. elegans
    • Benian, G. M., L'Hernault, S. W. & Morris, M. E. (1993). Additional sequence complexity in the muscle gene unc-22 and its encoded protein, twitchin, of C. elegans. Genetics, 134, 1097-1104.
    • (1993) Genetics , vol.134 , pp. 1097-1104
    • Benian, G.M.1    L'Hernault, S.W.2    Morris, M.E.3
  • 26
    • 0018961312 scopus 로고
    • Mutants with altered muscle structure in C. elegans
    • Waterston, R. H., Thomson, J. N. & Brenner, S. (1980). Mutants with altered muscle structure in C. elegans. Dev. Biol. 77, 271-302.
    • (1980) Dev. Biol. , vol.77 , pp. 271-302
    • Waterston, R.H.1    Thomson, J.N.2    Brenner, S.3
  • 27
    • 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., Schreifer, L. & Waterston, R. H. (1988). Identification and intracellular localization of the unc-22 gene product of C. elegans. Genes Dev. 2, 93-105.
    • (1988) Genes Dev. , vol.2 , pp. 93-105
    • Moerman, D.G.1    Benian, G.M.2    Barstead, R.J.3    Schreifer, L.4    Waterston, R.H.5
  • 28
    • 0028168572 scopus 로고
    • cAMP-dependent phosphorylation of Aplysia twitchin may mediate modulation of muscle contractions by neuropeptide cotransmitters
    • Probst, W. C., Cropper, E. C., Heierhorst, J., Hooper, S. L., Jaffe, H., Vilim, F. et al. (1994). cAMP-dependent phosphorylation of Aplysia twitchin may mediate modulation of muscle contractions by neuropeptide cotransmitters. Proc. Natl. Acad. Sci. USA, 91, 8487-8491.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8487-8491
    • Probst, W.C.1    Cropper, E.C.2    Heierhorst, J.3    Hooper, S.L.4    Jaffe, H.5    Vilim, F.6
  • 29
    • 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., Funabara, D., Kinoshita, S., Watabe, S., Hartshorne, D. J. & Butler, T. M. (1998). 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) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5383-5388
    • Siegman, M.J.1    Funabara, D.2    Kinoshita, S.3    Watabe, S.4    Hartshorne, D.J.5    Butler, T.M.6
  • 30
    • 0029978282 scopus 로고    scopus 로고
    • The C. 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. & Borodovsky, M. (1996). The C. 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) J. Cell Biol. , vol.132 , pp. 835-848
    • Benian, G.M.1    Tinley, T.L.2    Tang, X.3    Borodovsky, M.4
  • 31
    • 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. (1999). The genetics and molecular biology of the titin/connectin-like proteins of invertebrates. Rev. Physiol. Biochem. Pharmacol. 138, 235-268.
    • (1999) Rev. Physiol. Biochem. Pharmacol. , vol.138 , pp. 235-268
    • Benian, G.M.1    Ayme-Southgate, A.2    Tinley, T.L.3
  • 32
    • 0000461349 scopus 로고    scopus 로고
    • RNA processing and gene structure
    • Riddle, D., Blumenthal, T., Meyer, B. J. & Priess, J. R., eds, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Blumenthal, T. & Steward, K. (1997). RNA processing and gene structure. In C. elegans II (Riddle, D., Blumenthal, T., Meyer, B. J. & Priess, J. R., eds), pp. 117-145, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1997) C. elegans II , pp. 117-145
    • Blumenthal, T.1    Steward, K.2
  • 33
    • 0033601287 scopus 로고    scopus 로고
    • A mutation in the C. elegans EXP-2 potassium channel that alters feeding behaviour
    • Davis, M. W., Fleischhauer, R., Dent, J. A., Joho, R. H. & Avery, L. (1999). A mutation in the C. elegans EXP-2 potassium channel that alters feeding behaviour. Science, 286, 2501-2504.
    • (1999) Science , vol.286 , pp. 2501-2504
    • Davis, M.W.1    Fleischhauer, R.2    Dent, J.A.3    Joho, R.H.4    Avery, L.5
  • 34
    • 0024319166 scopus 로고
    • The basal component of the nematode dense-body is vinculin
    • Barstead, R. J. & Waterston, R. H. (1989). The basal component of the nematode dense-body is vinculin. J. Biol. Chem. 264, 10177-10185.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10177-10185
    • Barstead, R.J.1    Waterston, R.H.2
  • 35
    • 0035801351 scopus 로고    scopus 로고
    • Invertebrate connectin spans as much as 3.5 mm in the giant sarcomeres of crayfish claw muscle
    • Fukuzawa, A., Shimamura, J., Takemori, S., Kanzawa, N., Yamaguchi, M., Sun, P. et al. (2001). Invertebrate connectin spans as much as 3.5 mm in the giant sarcomeres of crayfish claw muscle. EMBO J. 20, 4826-4835.
    • (2001) EMBO J. , vol.20 , pp. 4826-4835
    • Fukuzawa, A.1    Shimamura, J.2    Takemori, S.3    Kanzawa, N.4    Yamaguchi, M.5    Sun, P.6
  • 36
    • 0027990826 scopus 로고
    • Protein kinase domain of twitchin has protein kinase activity and an autoinhibitory region
    • Lei, J., Tang, X., Chambers, T. C., Pohl, J. & Benian, G. M. (1994). Protein kinase domain of twitchin has protein kinase activity and an autoinhibitory region. J. Biol. Chem. 269, 21078-21085.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21078-21085
    • Lei, J.1    Tang, X.2    Chambers, T.C.3    Pohl, J.4    Benian, G.M.5
  • 37
    • 0022345717 scopus 로고
    • Muscle organization in C. elegans: Localization of proteins implicated in thin filament attachment and I-band organization
    • Francis, G. R. & Waterston, R. H. (1985). Muscle organization in C. elegans: Localization of proteins implicated in thin filament attachment and I-band organization. J. Cell Biol. 101, 1532-1549.
    • (1985) J. Cell Biol. , vol.101 , pp. 1532-1549
    • Francis, G.R.1    Waterston, R.H.2
  • 38
    • 0025997389 scopus 로고
    • Cloning, sequencing and mapping of an alpha-actinin gene from the nematode C. elegans
    • Barstead, R. J., Kleiman, L. & Waterston, R. H. (1991). Cloning, sequencing and mapping of an alpha-actinin gene from the nematode C. elegans. Cell Motil. Cytoskel. 20, 69-78.
    • (1991) Cell Motil. Cytoskel. , vol.20 , pp. 69-78
    • Barstead, R.J.1    Kleiman, L.2    Waterston, R.H.3
  • 39
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics
    • Ono, S. & Ono, K. (2002). Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics. J. Cell Biol. 156, 1065-1076.
    • (2002) J. Cell Biol. , vol.156 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 40
    • 0027237826 scopus 로고
    • Myosin and paramyosin of C. elegans embryos assemble into nascent structures distinct from thick filaments and multi-filament assemblages
    • Epstein, H. F., Casey, D. L. & Ortiz, I. (1993). Myosin and paramyosin of C. elegans embryos assemble into nascent structures distinct from thick filaments and multi-filament assemblages. J. Cell Biol. 122, 845-858.
    • (1993) J. Cell Biol. , vol.122 , pp. 845-858
    • Epstein, H.F.1    Casey, D.L.2    Ortiz, I.3
  • 41
    • 0028055026 scopus 로고
    • Assembly of body wall muscle and muscle cell attachment structures in Caenorhabditis elegans
    • Hresko, M. C., Williams, B. D. & Waterston, R. H. (1994). Assembly of body wall muscle and muscle cell attachment structures in Caenorhabditis elegans. J. Cell Biol. 124, 491-506.
    • (1994) J. Cell Biol. , vol.124 , pp. 491-506
    • Hresko, M.C.1    Williams, B.D.2    Waterston, R.H.3
  • 42
    • 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. (2000). 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) J. Cell Biol. , vol.148 , pp. 101-114
    • Hakeda, S.1    Endo, S.2    Saigo, K.3
  • 43
    • 0033824709 scopus 로고    scopus 로고
    • Drosophila D-titin is required for myoblast fusion and skeletal muscle striation
    • Zhang, Y., Featherstone, D., Davis, W., Rushton, E. & Broadie, K. (2000). Drosophila D-titin is required for myoblast fusion and skeletal muscle striation. J. Cell Sci. 113, 3103-3115.
    • (2000) J. Cell Sci. , vol.113 , pp. 3103-3115
    • Zhang, Y.1    Featherstone, D.2    Davis, W.3    Rushton, E.4    Broadie, K.5
  • 44
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K. & Hunter, T. (1995). The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 45
    • 0028841580 scopus 로고
    • Phosphorylation of myosin regulatory light chains by the molluscan twitchin kinase
    • Heierhorst, J., Probst, W. C., Kohanski, R. A., Buku, A. & Weiss, K. R. (1995). Phosphorylation of myosin regulatory light chains by the molluscan twitchin kinase. Eur. J. Biochem. 233, 426-431.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 426-431
    • Heierhorst, J.1    Probst, W.C.2    Kohanski, R.A.3    Buku, A.4    Weiss, K.R.5
  • 46
    • 0032578901 scopus 로고    scopus 로고
    • Structural basis for activation of the titin kinase domain during myofibrillogenesis
    • Mayans, O., van der Ven, P. F. M., Wilm, M., Mues, A., Young, P., Furst, D. O. et al. (1998). Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature, 395, 863-869.
    • (1998) Nature , vol.395 , pp. 863-869
    • Mayans, O.1    Van der Ven, P.F.M.2    Wilm, M.3    Mues, A.4    Young, P.5    Furst, D.O.6
  • 47
    • 0033954004 scopus 로고    scopus 로고
    • Limb-girdle muscular dystrophy type 2G is caused by mutations in the gene encoding the sarcomeric protein telethonin
    • Moreira, E. S., Wiltshire, T. J., Faulkner, G., Nilforoushan, A., Vainzof, M., Suzuki, O. T. et al. (2000). Limb-girdle muscular dystrophy type 2G is caused by mutations in the gene encoding the sarcomeric protein telethonin. Nature Genet. 24, 163-166.
    • (2000) Nature Genet. , vol.24 , pp. 163-166
    • Moreira, E.S.1    Wiltshire, T.J.2    Faulkner, G.3    Nilforoushan, A.4    Vainzof, M.5    Suzuki, O.T.6
  • 48
    • 0031004299 scopus 로고    scopus 로고
    • An N-terminal fragment of titin coupled to GFP localizes to the Z-bands in living muscle cells: Overexpression leads to myofibril disassembly
    • Turnacioglu, K. K., Mittal, B., Dabiri, G. A., Sanger, J. M. & Sanger, J. W. (1997). An N-terminal fragment of titin coupled to GFP localizes to the Z-bands in living muscle cells: Overexpression leads to myofibril disassembly. Mol. Biol. Cell, 8, 705-717.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 705-717
    • Turnacioglu, K.K.1    Mittal, B.2    Dabiri, G.A.3    Sanger, J.M.4    Sanger, J.W.5
  • 49
    • 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, D. O. (1996). The central Z-disk region of titin is assembled from a novel repeat in variable copy numbers. J. Cell Sci. 109, 2747-2754.
    • (1996) J. Cell Sci. , vol.109 , pp. 2747-2754
    • Gautel, M.1    Goulding, D.2    Bullard, B.3    Weber, K.4    Furst, D.O.5
  • 50
    • 0031027371 scopus 로고    scopus 로고
    • Binding of the N-terminal 63 kDa portion of connectin/titin to α-actinin as revealed by the yeast two-hybrid system
    • Ohtsuka, H., Yajima, H., Maruyama, K. & Kimura, S. (1997). Binding of the N-terminal 63 kDa portion of connectin/titin to α-actinin as revealed by the yeast two-hybrid system. FEBS Letters, 401, 65-67.
    • (1997) FEBS Letters , vol.401 , pp. 65-67
    • Ohtsuka, H.1    Yajima, H.2    Maruyama, K.3    Kimura, S.4
  • 51
    • 0031560933 scopus 로고    scopus 로고
    • The N-terminal Z repeat 5 of connectin/titin binds to the C-terminal region of α-actinin
    • Ohtsuka, H., Yajima, H., Maruyama, K. & Kimura, S. (1997). The N-terminal Z repeat 5 of connectin/titin binds to the C-terminal region of α-actinin. Biochem. Biophys. Res. Commun. 235, 1-3.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 1-3
    • Ohtsuka, H.1    Yajima, H.2    Maruyama, K.3    Kimura, S.4
  • 52
    • 0031213849 scopus 로고    scopus 로고
    • Tissue-specific expression and alpha-actinin binding properties of the Z disc titin. Implications for the nature of vertebrate Z discs
    • Sorimachi, H., Freiburg, A., Kolmerer, B., Ishiura, S., Stier, G., Gregorio, C. C. et al. (1997). Tissue-specific expression and alpha-actinin binding properties of the Z disc titin. Implications for the nature of vertebrate Z discs. J. Mol. Biol. 270, 688-695.
    • (1997) J. Mol. Biol. , vol.270 , pp. 688-695
    • Sorimachi, H.1    Freiburg, A.2    Kolmerer, B.3    Ishiura, S.4    Stier, G.5    Gregorio, C.C.6
  • 53
    • 0000823299 scopus 로고
    • Muscle
    • Wood, W. B., ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Waterston, R. H. (1988). Muscle. In The Nematode Caenorhabditis elegans (Wood, W. B., ed.), pp. 281-335, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) The Nematode Caenorhabditis elegans , pp. 281-335
    • Waterston, R.H.1
  • 55
    • 0019126256 scopus 로고
    • Paramyosin is necessary for determination of nematode thick filament length in vivo
    • Mackenzie, J. M. & Epstein, H. F. (1980). Paramyosin is necessary for determination of nematode thick filament length in vivo. Cell, 22, 747-755.
    • (1980) Cell , vol.22 , pp. 747-755
    • Mackenzie, J.M.1    Epstein, H.F.2
  • 56
    • 0035128859 scopus 로고    scopus 로고
    • Large-scale analysis of gene function in C. elegans by high-throughput RNAi
    • Maeda, I., Kohara, Y., Yamamoto, M. & Sugimoto, A. (2001). Large-scale analysis of gene function in C. elegans by high-throughput RNAi. Curr. Biol. 11, 171-176.
    • (2001) Curr. Biol. , vol.11 , pp. 171-176
    • Maeda, I.1    Kohara, Y.2    Yamamoto, M.3    Sugimoto, A.4
  • 58
    • 0034676448 scopus 로고    scopus 로고
    • Functional genomic analysis of cell division in C. elegans using RNAi of genes on chromosome III
    • Goncy, P., Echeverri, C., Oegema, K., Coulson, A., Jones, S. J. M., Copley, R. R. et al. (2000). Functional genomic analysis of cell division in C. elegans using RNAi of genes on chromosome III. Nature, 408, 331-336.
    • (2000) Nature , vol.408 , pp. 331-336
    • Goncy, P.1    Echeverri, C.2    Oegema, K.3    Coulson, A.4    Jones, S.J.M.5    Copley, R.R.6
  • 59
    • 0031732094 scopus 로고    scopus 로고
    • A computer program for aligning a cDNA sequence with a genomic DNA sequence
    • Florea, L., Hartzell, G., Zhang, Z., Rubin, G. M. & Miller, W. (1998). A computer program for aligning a cDNA sequence with a genomic DNA sequence. Genome Res. 8, 967-974.
    • (1998) Genome Res. , vol.8 , pp. 967-974
    • Florea, L.1    Hartzell, G.2    Zhang, Z.3    Rubin, G.M.4    Miller, W.5
  • 60
    • 0034333196 scopus 로고    scopus 로고
    • Rapid automatic detection and alignment of repeats in protein sequences
    • Heger, A. & Holm, L. (2000). Rapid automatic detection and alignment of repeats in protein sequences. Proteins: Struct. Funct. Genet. 41, 224-237.
    • (2000) Proteins: Struct. Funct. Genet. , vol.41 , pp. 224-237
    • Heger, A.1    Holm, L.2
  • 61
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider, T. D. & Stephens, R. M. (1990). Sequence logos: A new way to display consensus sequences. Nucl. Acids Res. 18, 6097-6100.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 65
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994). CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22, 4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 66
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in E. coli as fusions with glutathione S-transferase
    • Smith, D. B. & Johnson, K. S. (1988). Single-step purification of polypeptides expressed in E. coli as fusions with glutathione S-transferase. Gene, 67, 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.