메뉴 건너뛰기




Volumn 279, Issue 1, 1998, Pages 201-210

Structure of the Drosophila projectin protein: Isoforms and implication for projectin filament assembly

Author keywords

Drosophila; Muscle; Projectin; Titin; Twitchin

Indexed keywords

ISOPROTEIN; MUSCLE PROTEIN;

EID: 0032577314     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1756     Document Type: Article
Times cited : (32)

References (72)
  • 2
    • 0012016970 scopus 로고
    • Locus 67B of Drosophila melanogaster contains seven, not four, closely related heat shock genes
    • Ayme A., Tissieres A. Locus 67B of Drosophila melanogaster contains seven, not four, closely related heat shock genes. EMBO J. 4:1985;2949-2954
    • (1985) EMBO J , vol.4 , pp. 2949-2954
    • Ayme, A.1    Tissieres, A.2
  • 4
    • 0028897497 scopus 로고
    • Both synchronous and asynchronous muscle isoforms of projectin (the Drosophila bent locus product) contain functional kinase domains
    • Ayme-Southgate A., Southgate R., Saide J., Benian G., Pardue M.L. Both synchronous and asynchronous muscle isoforms of projectin (the Drosophila bent locus product) contain functional kinase domains. J. Cell Biol. 128:1995;393-403
    • (1995) J. Cell Biol , vol.128 , pp. 393-403
    • Ayme-Southgate, A.1    Southgate, R.2    Saide, J.3    Benian, G.4    Pardue, M.L.5
  • 5
    • 0028199717 scopus 로고
    • Myofibrillogenesis in primary tissue culture of adult human skeletal muscle: Expression of desmin, titin and nebulin
    • Behr T., Fisher P., Muller-Felber W., Schmidt-Achert M., Pongratz D. Myofibrillogenesis in primary tissue culture of adult human skeletal muscle expression of desmin, titin and nebulin. Clin. Investig. 72:1994;150-155
    • (1994) Clin. Investig , vol.72 , pp. 150-155
    • Behr, T.1    Fisher, P.2    Muller-Felber, W.3    Schmidt-Achert, M.4    Pongratz, D.5
  • 6
    • 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. 342:1989;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
  • 7
    • 0027237468 scopus 로고
    • Additional sequence complexity in the muscle gene, unc22 and its encoded protein twitchin of Caenorhabditis elegans
    • Benian G.M., L'Hernault S.W., Morris M.E. Additional sequence complexity in the muscle gene, unc22 and its encoded protein twitchin of Caenorhabditis elegans. Genetics. 134:1993;1097-1104
    • (1993) Genetics , vol.134 , pp. 1097-1104
    • Benian, G.M.1    L'Hernault, S.W.2    Morris, M.E.3
  • 8
    • 0029978282 scopus 로고    scopus 로고
    • The Caenorhabditis 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. The Caenorhabditis gene unc 89, required for muscle M-line assembly, encodes a giant modular protein composed of Ig and signal transduction domains. J. Cell Biol. 132:1996;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
  • 9
    • 0020678384 scopus 로고
    • Drosophila muscle MHC is encoded by a single gene located in a cluster of muscle mutations
    • Bernstein S., Mogami K., Donady J.J., Emerson C.P. Drosophila muscle MHC is encoded by a single gene located in a cluster of muscle mutations. Nature. 302:1983;393-397
    • (1983) Nature , vol.302 , pp. 393-397
    • Bernstein, S.1    Mogami, K.2    Donady, J.J.3    Emerson, C.P.4
  • 10
    • 0017667843 scopus 로고
    • The site of paramyosin in insect flight muscle and the presence of an unidentified protein between myosin filaments and Z line
    • Bullard B., Hammond K.S., Luke B.M. The site of paramyosin in insect flight muscle and the presence of an unidentified protein between myosin filaments and Z line. J. Mol. Biol. 115:1977;417-440
    • (1977) J. Mol. Biol , vol.115 , pp. 417-440
    • Bullard, B.1    Hammond, K.S.2    Luke, B.M.3
  • 11
    • 0025015322 scopus 로고
    • The early expression of myofibrillar proteins in round postmitotic myoblasts of embryonic skeletal muscle
    • Colley N.J., Tokuyasu K.T., Singer S.J. The early expression of myofibrillar proteins in round postmitotic myoblasts of embryonic skeletal muscle. J. Cell Sci. 95:1990;11-22
    • (1990) J. Cell Sci , vol.95 , pp. 11-22
    • Colley, N.J.1    Tokuyasu, K.T.2    Singer, S.J.3
  • 12
    • 0001063013 scopus 로고
    • The morphology and development of the Drosophila muscular system
    • M. Asburner, Wright T.R.F. London: Academic Press Ltd
    • Crossley A.C. The morphology and development of the Drosophila muscular system. Asburner M., Wright T.R.F. The Genetics and Biology of Drosophila. vol. 2B:1978;499-559 Academic Press Ltd, London
    • (1978) The Genetics and Biology of Drosophila , vol.2 , pp. 499-559
    • Crossley, A.C.1
  • 13
    • 0030573054 scopus 로고    scopus 로고
    • Structure and stability of an immunoglobulin domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans
    • Fong S., Hamill S.J., Proctor M., Freund S.M.V., Benian G.M., Chothia C., Bycroft M., Clarke J. Structure and stability of an immunoglobulin domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans. J. Mol. Biol. 264:1996;624-639
    • (1996) J. Mol. Biol , vol.264 , pp. 624-639
    • Fong, S.1    Hamill, S.J.2    Proctor, M.3    Freund, S.M.V.4    Benian, G.M.5    Chothia, C.6    Bycroft, M.7    Clarke, J.8
  • 14
    • 0030989899 scopus 로고    scopus 로고
    • Organization of proteins and mRNA for titin and other myofibril components during myofibrillogenesis in cultured chicken skeletal muscle
    • Fulton A.B., Alftine C. Organization of proteins and mRNA for titin and other myofibril components during myofibrillogenesis in cultured chicken skeletal muscle. Cell Struct. Funct. 22:1997;15-58
    • (1997) Cell Struct. Funct , vol.22 , pp. 15-58
    • Fulton, A.B.1    Alftine, C.2
  • 15
    • 0026147304 scopus 로고
    • Titin, a huge elastic sarcomeric protein with a probable role in morphogenesis
    • Fulton A.B., Isaacs W.B. Titin, a huge elastic sarcomeric protein with a probable role in morphogenesis. BioEssays. 13:1991;157-161
    • (1991) BioEssays , vol.13 , pp. 157-161
    • Fulton, A.B.1    Isaacs, W.B.2
  • 16
    • 0025062549 scopus 로고
    • Elastic filaments in skeletal muscles revealed by selective removal of thin filaments with plasma gelsolin
    • Funatsu T., Higuchi H., Ishiwata S. Elastic filaments in skeletal muscles revealed by selective removal of thin filaments with plasma gelsolin. J. Cell Biol. 110:1990;53-62
    • (1990) J. Cell Biol , vol.110 , pp. 53-62
    • Funatsu, T.1    Higuchi, H.2    Ishiwata, S.3
  • 17
    • 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 D.O., 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. 106:1988;1563-1572
    • (1988) J. Cell Biol , vol.106 , pp. 1563-1572
    • Furst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 18
    • 0020581716 scopus 로고
    • Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner
    • Fyrberg E.A., Mahaffey W.J., Bond B.J., Davidson N. Transcripts of the six Drosophila actin genes accumulate in a stage- and tissue-specific manner. Cell. 33:1983;115-123
    • (1983) Cell , vol.33 , pp. 115-123
    • Fyrberg, E.A.1    Mahaffey, W.J.2    Bond, B.J.3    Davidson, N.4
  • 19
    • 0026768103 scopus 로고
    • Drosophila projectin: Relatedness to titin and twitchin and correlation with lethal (4) 102CDa and bent-dominant mutants
    • Fyrberg C.C., Labeit S., Bullard B., Leonard K., Fyrberg E.A. Drosophila projectin relatedness to titin and twitchin and correlation with lethal (4) 102CDa and bent-dominant mutants. Proc. Roy. Soc. London. ser. B. 249:1992;33-40
    • (1992) Proc. Roy. Soc. London. Ser. B , vol.249 , pp. 33-40
    • Fyrberg, C.C.1    Labeit, S.2    Bullard, B.3    Leonard, K.4    Fyrberg, E.A.5
  • 20
    • 0029824116 scopus 로고    scopus 로고
    • The super-repeats of titin/connectin and their interactions: Glimpses at sarcomeric assembly
    • Gautel M. The super-repeats of titin/connectin and their interactions glimpses at sarcomeric assembly. Advan. Biophys. 33:1996;27-37
    • (1996) Advan. Biophys , vol.33 , pp. 27-37
    • Gautel, M.1
  • 21
    • 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. 12:1993;3827-3834
    • (1993) EMBO J , vol.12 , pp. 3827-3834
    • Gautel, M.1    Leonard, K.2    Labeit, S.3
  • 22
    • 0028361540 scopus 로고
    • Many of the immunoglobulin superfamily domains in cell adhesion and surface receptors belong to a new structural set which is close to that containing variable domains
    • Harpaz Y., Chothia C. Many of the immunoglobulin superfamily domains in cell adhesion and surface receptors belong to a new structural set which is close to that containing variable domains. J. Mol. Biol. 238:1994;528-539
    • (1994) J. Mol. Biol , vol.238 , pp. 528-539
    • Harpaz, Y.1    Chothia, C.2
  • 23
    • 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. 323:1986;160-164
    • (1986) Nature , vol.323 , pp. 160-164
    • Horowits, R.1    Kempner, E.S.2    Bisher, M.E.3    Podolsky, R.J.4
  • 24
    • 0024426462 scopus 로고
    • Elastic behavior of connecting filaments during thick filament movement in activated skeletal muscle
    • Horowits R., Maruyama K., Podolsky R.J. Elastic behavior of connecting filaments during thick filament movement in activated skeletal muscle. J. Cell Biol. 109:1989;2169-2176
    • (1989) J. Cell Biol , vol.109 , pp. 2169-2176
    • Horowits, R.1    Maruyama, K.2    Podolsky, R.J.3
  • 25
  • 26
    • 0022548661 scopus 로고
    • Sodium dodecyl sulfate-gel electrophoresis of connectin-like high molecular weight proteins of various types of vertebrate and invertebrate muscles
    • Hu D.H., Kimura S., Maruyama K. Sodium dodecyl sulfate-gel electrophoresis of connectin-like high molecular weight proteins of various types of vertebrate and invertebrate muscles. J. Biochem. 99:1986;485-1492
    • (1986) J. Biochem , vol.99 , pp. 485-1492
    • Hu, D.H.1    Kimura, S.2    Maruyama, K.3
  • 27
    • 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., Matsuno A., Terakado K., Matsuura T., Kimura S., Maruyama K. 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. 11:1990;497-511
    • (1990) J. Muscle Res. Cell Motil , vol.11 , pp. 497-511
    • Hu, D.H.1    Matsuno, A.2    Terakado, K.3    Matsuura, T.4    Kimura, S.5    Maruyama, K.6
  • 28
    • 0024453411 scopus 로고
    • Biosynthesis of titin in cultured skeletal muscle cells
    • Isaacs W.B., Kim I.S., Struve A., Fulton A.B. Biosynthesis of titin in cultured skeletal muscle cells. J. Cell Biol. 109:1989;2189-2195
    • (1989) J. Cell Biol , vol.109 , pp. 2189-2195
    • Isaacs, W.B.1    Kim, I.S.2    Struve, A.3    Fulton, A.B.4
  • 29
    • 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. 89:1992;7496-7500
    • (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
  • 30
    • 0001405930 scopus 로고
    • Oscillatory contraction of insect fibrillar muscle after glycerol extraction
    • Jewell B.R., Ruegg C. Oscillatory contraction of insect fibrillar muscle after glycerol extraction. Proc. Roy. Soc. London. ser. B. 164:1966;428-459
    • (1966) Proc. Roy. Soc. London. Ser. B , vol.164 , pp. 428-459
    • Jewell, B.R.1    Ruegg, C.2
  • 31
    • 0027279203 scopus 로고
    • Dynamics of actin and assembly of connectin (titin) during myofibrillogenesis in embryonic chick cardiac muscle cells in vitro
    • Komiyama 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. Dyn. 196:1993;291-299
    • (1993) Dev. Dyn , vol.196 , pp. 291-299
    • Komiyama, M.1    Kouchi, K.2    Maruyama, K.3    Shimada, Y.4
  • 32
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S., Kolmerer B. Titins giant proteins in charge of muscle ultrastructure and elasticity. Science. 270:1995;293-296
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 34
    • 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. 11:1992;1711-1716
    • (1992) EMBO J , vol.11 , pp. 1711-1716
    • Labeit, S.1    Gautel, M.2    Lakey, A.3    Trinick, J.4
  • 35
    • 0025131273 scopus 로고
    • Identification and localization of high molecular weight proteins in insect flight and leg muscles
    • Lakey A., Ferguson C., Labeit S., Reedy M., Larkins A., Butcher G., Leonard K., Bullard B. Identification and localization of high molecular weight proteins in insect flight and leg muscles. EMBO J. 9:1990;3459-3467
    • (1990) EMBO J , vol.9 , pp. 3459-3467
    • Lakey, A.1    Ferguson, C.2    Labeit, S.3    Reedy, M.4    Larkins, A.5    Butcher, G.6    Leonard, K.7    Bullard, B.8
  • 37
    • 0026603237 scopus 로고
    • Autophosphorylating protein kinase activity of titin-like arthropod projectin
    • Maroto M., Vinos J., Marco R., Cervera M. Autophosphorylating protein kinase activity of titin-like arthropod projectin. J. Mol. Biol. 224:1992;287-291
    • (1992) J. Mol. Biol , vol.224 , pp. 287-291
    • Maroto, M.1    Vinos, J.2    Marco, R.3    Cervera, M.4
  • 38
    • 0019522956 scopus 로고
    • Connectin, an elastic protein of muscle. Identification of 'titin' with connectin
    • Maruyama K., Kimura S., Ohashi K., Kuwano Y. Connectin, an elastic protein of muscle. Identification of 'titin' with connectin. J. Biochem. 89:1981;701-709
    • (1981) J. Biochem , vol.89 , pp. 701-709
    • Maruyama, K.1    Kimura, S.2    Ohashi, K.3    Kuwano, Y.4
  • 39
    • 0020156343 scopus 로고
    • Mutations in the unc54 myosin heavy chain gene of Caenorhabditis elegans that after contractility but not muscle structure
    • Moerman D.G., Plurad S., Waterston R.H., Baillie D.L. Mutations in the unc54 myosin heavy chain gene of Caenorhabditis elegans that after contractility but not muscle structure. Cell. 29:1982;773-781
    • (1982) Cell , vol.29 , pp. 773-781
    • Moerman, D.G.1    Plurad, S.2    Waterston, R.H.3    Baillie, D.L.4
  • 40
    • 0023776666 scopus 로고
    • Identification and intracellular localization of the unc-22 gene product of Caenorhabditis elegans
    • Moerman D.G., Benian G.M., Barstead R.J., Schrieffer L.A., Waterston R.H. Identification and intracellular localization of the unc-22 gene product of Caenorhabditis elegans. Genes Dev. 2:1988;93-105
    • (1988) Genes Dev , vol.2 , pp. 93-105
    • Moerman, D.G.1    Benian, G.M.2    Barstead, R.J.3    Schrieffer, L.A.4    Waterston, R.H.5
  • 41
    • 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. 95:1990;535-544
    • (1990) J. Cell Sci , vol.95 , pp. 535-544
    • Nave, R.1    Weber, K.2
  • 42
    • 0024440423 scopus 로고
    • Visualization of the polarity of isolated titin molecules: A single globular head 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 as the M band anchoring domain? J. Cell Biol. 109:1989;2177-2187
    • (1989) J. Cell Biol , vol.109 , pp. 2177-2187
    • Nave, R.1    Furst, D.O.2    Weber, K.3
  • 43
    • 0031027371 scopus 로고    scopus 로고
    • Binding of the N-terminal 63 kDa portion of connectin/titin to alpha-actinin as revealed by the yeast two-hybrid system
    • Ohtsuka H., Yajaima H., Maruyama K., Kimura S. Binding of the N-terminal 63 kDa portion of connectin/titin to alpha-actinin as revealed by the yeast two-hybrid system. FEBS Letters. 401:1997;65-67
    • (1997) FEBS Letters , vol.401 , pp. 65-67
    • Ohtsuka, H.1    Yajaima, H.2    Maruyama, K.3    Kimura, S.4
  • 44
    • 0027515217 scopus 로고
    • The major myosin-binding domain of skeletal muscle MyBP-C (C-protein) resides in the COOH-terminal, immunoglobulin C2 motif
    • Okagaki T., Weber F.E., Fischman D.A., Vaughan K.T., Mikawa T., Reinach F. The major myosin-binding domain of skeletal muscle MyBP-C (C-protein) resides in the COOH-terminal, immunoglobulin C2 motif. J. Cell Biol. 123:1993;619-626
    • (1993) J. Cell Biol , vol.123 , pp. 619-626
    • Okagaki, T.1    Weber, F.E.2    Fischman, D.A.3    Vaughan, K.T.4    Mikawa, T.5    Reinach, F.6
  • 45
    • 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. 3:1995;391-401
    • (1995) Structure , vol.3 , pp. 391-401
    • Pfuhl, M.1    Pastore, A.2
  • 46
    • 0018260965 scopus 로고
    • Stretch activation of muscle: Function and mechanism
    • Pringle F.R.S. Stretch activation of muscle function and mechanism. Proc. Roy. Soc. London ser. B. 201:1978;107-130
    • (1978) Proc. Roy. Soc. London Ser. B , vol.201 , pp. 107-130
    • Pringle, F.R.S.1
  • 48
    • 0028278854 scopus 로고
    • The premyofibril: Evidence for its role in myofibrillogenesis
    • Rhee D., Sanger J.M., Sanger J.W. The premyofibril evidence for its role in myofibrillogenesis. Cell Motil. Cytoskel. 28:1994;1-24
    • (1994) Cell Motil. Cytoskel , vol.28 , pp. 1-24
    • Rhee, D.1    Sanger, J.M.2    Sanger, J.W.3
  • 49
    • 0020658044 scopus 로고
    • Drosophila has one myosin heavy chain gene with three developmentally regulated transcripts
    • Rozek C.E., Davidson N. Drosophila has one myosin heavy chain gene with three developmentally regulated transcripts. Cell. 32:1983;23-34
    • (1983) Cell , vol.32 , pp. 23-34
    • Rozek, C.E.1    Davidson, N.2
  • 50
    • 0019882220 scopus 로고
    • Identification of a connecting filament protein in insect fibrillar flight muscle
    • Saide J.D. Identification of a connecting filament protein in insect fibrillar flight muscle. J. Mol. Biol. 133:1981;661-679
    • (1981) J. Mol. Biol , vol.133 , pp. 661-679
    • Saide, J.D.1
  • 53
    • 0027536473 scopus 로고
    • A survey of interactions made by the giant protein titin
    • Soteriou A., Gamage M., Trinick J. A survey of interactions made by the giant protein titin. J. Cell Sci. 104:1993;119-123
    • (1993) J. Cell Sci , vol.104 , pp. 119-123
    • Soteriou, A.1    Gamage, M.2    Trinick, J.3
  • 54
    • 0026596374 scopus 로고
    • Muscle filament lattices and stretch activation: The match-mismatch model reassessed
    • Squire J.M. Muscle filament lattices and stretch activation the match-mismatch model reassessed. J. Muscle Res. Cell Motil. 13:1992;183-189
    • (1992) J. Muscle Res. Cell Motil , vol.13 , pp. 183-189
    • Squire, J.M.1
  • 55
    • 0023551502 scopus 로고
    • Immuno cytochemical studies of cardiac myofibrillogenesis in early chick embryos. I: Presence of immunofluorescent titin spots in premyofibril stages
    • Tokuyasu K.T., Maher P.A. Immuno cytochemical studies of cardiac myofibrillogenesis in early chick embryos. I Presence of immunofluorescent titin spots in premyofibril stages. J. Cell Biol. 1987;1052781-1052793
    • (1987) J. Cell Biol , pp. 1052781-1052793
    • Tokuyasu, K.T.1    Maher, P.A.2
  • 56
    • 0029802371 scopus 로고    scopus 로고
    • Interactions of titin/connectin with the thick filament
    • Trinick J. Interactions of titin/connectin with the thick filament. Advan. Biophys. 33:1996;81-90
    • (1996) Advan. Biophys , vol.33 , pp. 81-90
    • Trinick, J.1
  • 57
    • 0021591504 scopus 로고
    • Purification and properties of native titin
    • Trinick J., Knight P., Whiting A. Purification and properties of native titin. J. Mol. Biol. 189:1984;331-356
    • (1984) J. Mol. Biol , vol.189 , pp. 331-356
    • Trinick, J.1    Knight, P.2    Whiting, A.3
  • 58
    • 0002236823 scopus 로고
    • Fine structure and mechanical properties of insect muscle
    • R.T. Tregear. North Holland, Amsterdam: Elsevier
    • Trombitas C., Tigyi-Sebes A. Fine structure and mechanical properties of insect muscle. Tregear R.T. Insect Flight Muscle. 1977;79-90 Elsevier, North Holland, Amsterdam
    • (1977) Insect Flight Muscle , pp. 79-90
    • Trombitas, C.1    Tigyi-Sebes, A.2
  • 60
    • 1842334510 scopus 로고    scopus 로고
    • Assembly of titin, myomesin and M-protein into the sarcomeric M band in differentiating human skeletal muscle cells in vitro
    • van der Ven P.F., Furst D.O. Assembly of titin, myomesin and M-protein into the sarcomeric M band in differentiating human skeletal muscle cells in vitro. Cell Struct. Funct. 22:1997;163-171
    • (1997) Cell Struct. Funct , vol.22 , pp. 163-171
    • Van Der Ven, P.F.1    Furst, D.O.2
  • 61
    • 0027515659 scopus 로고
    • Titin aggregates associated with intermediate filaments align along fiber-like structures during human skeletal muscle cell differentiation
    • van der Ven P.F., Schaart G., Croes H.J., Jap P.H., Ginssel L.A., Ramaekers F.C. Titin aggregates associated with intermediate filaments align along fiber-like structures during human skeletal muscle cell differentiation. J. Cell Sci. 106:1993;749-759
    • (1993) J. Cell Sci , vol.106 , pp. 749-759
    • Van Der Ven, P.F.1    Schaart, G.2    Croes, H.J.3    Jap, P.H.4    Ginssel, L.A.5    Ramaekers, F.C.6
  • 62
    • 0027748233 scopus 로고
    • Mini-titins in striated and smooth molluscan muscles: Structure, location and immunological crossreactivity
    • Vibert P., Edelstein S.M., Castellani L., Elliot B.W. Mini-titins in striated and smooth molluscan muscles structure, location and immunological crossreactivity. J. Muscle Res. Cell Motil. 14:1993;598-607
    • (1993) J. Muscle Res. Cell Motil , vol.14 , pp. 598-607
    • Vibert, P.1    Edelstein, S.M.2    Castellani, L.3    Elliot, B.W.4
  • 63
    • 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 Respectively. Cell Motil. 12:1991;340-354
    • (1991) J. Muscle Respectively. Cell Motil , vol.12 , pp. 340-354
    • Vigoreaux, J.O.1    Saide, J.D.2    Pardue, M.-L.3
  • 64
    • 0027374159 scopus 로고
    • The globular head domain of titin extends into the center of the sarcomeric M band: CDNA cloning, epitope mapping and immunoelectron microscopy of two titin-associated proteins
    • Vinkemeier U., Obermann W., Weber K., Furst D.O. The globular head domain of titin extends into the center of the sarcomeric M band cDNA cloning, epitope mapping and immunoelectron microscopy of two titin-associated proteins. J. Cell Sci. 106:1993;319-330
    • (1993) J. Cell Sci , vol.106 , pp. 319-330
    • Vinkemeier, U.1    Obermann, W.2    Weber, K.3    Furst, D.O.4
  • 65
    • 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. 76:1979;3698-3702
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 3698-3702
    • Wang, K.1    McClure, J.2    Tu, A.3
  • 66
    • 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. 81:1984;3685-3689
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 3685-3689
    • Wang, K.1    Ramirez-Mitchell, R.2    Palter, D.3
  • 67
    • 0025816649 scopus 로고
    • Regulation of skeletal muscle stiffness and elasticity by titin isoforms: A test of the segmental extension model of resting tension
    • Wang K., McCarter R., Wright J., Beverly J., Ramirez-Mitchell R. Regulation of skeletal muscle stiffness and elasticity by titin isoforms a test of the segmental extension model of resting tension. Proc. Natl Acad. Sci. USA. 88:1991;7101-7105
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7101-7105
    • Wang, K.1    McCarter, R.2    Wright, J.3    Beverly, J.4    Ramirez-Mitchell, R.5
  • 68
    • 0023690742 scopus 로고
    • Studies on cardiac myofibrillogenesis with antibodies to titin, actin, tropomyosin and myosin
    • Wang S.M., Greaser M.L., Schultz E., Bulinski J.C., Lin J.J.C., Lessard J.L. Studies on cardiac myofibrillogenesis with antibodies to titin, actin, tropomyosin and myosin. J. Cell Biol. 108:1988;1075-1083
    • (1988) J. Cell Biol , vol.108 , pp. 1075-1083
    • Wang, S.M.1    Greaser, M.L.2    Schultz, E.3    Bulinski, J.C.4    Lin, J.J.C.5    Lessard, J.L.6
  • 69
    • 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. 205:1989;263-268
    • (1989) J. Mol. Biol , vol.205 , pp. 263-268
    • Whiting, A.1    Wardale, J.2    Trinick, J.3
  • 70
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily-domains for cell surface recognition
    • Williams A.F., Barclay A.N. The immunoglobulin superfamily-domains for cell surface recognition. Annu. Rev. Immunol. 6:1988;381-405
    • (1988) Annu. Rev. Immunol , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 72
    • 0018580286 scopus 로고
    • Filament geometry and the activation of insect flight muscle
    • Wray J.S. Filament geometry and the activation of insect flight muscle. Nature. 280:1979;325-326
    • (1979) Nature , vol.280 , pp. 325-326
    • Wray, J.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.