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Volumn 367, Issue 5, 2007, Pages 1312-1329

Alternative S2 Hinge Regions of the Myosin Rod Differentially Affect Muscle Function, Myofibril Dimensions and Myosin Tail Length

Author keywords

Drosophila; indirect flight muscle; myofibril; myosin; S2 hinge

Indexed keywords

ISOPROTEIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; MYOSIN SUBFRAGMENT;

EID: 33947150032     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.01.045     Document Type: Article
Times cited : (30)

References (79)
  • 1
    • 0019975166 scopus 로고
    • Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle
    • McLachlan A.D., and Karn J. Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature 299 (1982) 226-231
    • (1982) Nature , vol.299 , pp. 226-231
    • McLachlan, A.D.1    Karn, J.2
  • 2
    • 13444280378 scopus 로고    scopus 로고
    • Coupling between phosphate release and force generation in muscle actomyosin
    • Takagi Y., Shuman H., and Goldman Y.E. Coupling between phosphate release and force generation in muscle actomyosin. Phil. Trans. Roy. Soc. ser. B 359 (2004) 1913-1920
    • (2004) Phil. Trans. Roy. Soc. ser. B , vol.359 , pp. 1913-1920
    • Takagi, Y.1    Shuman, H.2    Goldman, Y.E.3
  • 3
    • 0021103673 scopus 로고
    • Periodic features in the amino acid sequence of nematode myosin rod
    • McLachlan A.D., and Karn J. Periodic features in the amino acid sequence of nematode myosin rod. J. Mol. Biol. 164 (1983) 605-626
    • (1983) J. Mol. Biol. , vol.164 , pp. 605-626
    • McLachlan, A.D.1    Karn, J.2
  • 4
    • 26244466046 scopus 로고    scopus 로고
    • Skip residues and charge interactions in myosin II coiled-coils: implications for molecular packing
    • Straussman R., Squire J.M., Ben-Ya'acov A., and Ravid S. Skip residues and charge interactions in myosin II coiled-coils: implications for molecular packing. J. Mol. Biol. 353 (2005) 613-628
    • (2005) J. Mol. Biol. , vol.353 , pp. 613-628
    • Straussman, R.1    Squire, J.M.2    Ben-Ya'acov, A.3    Ravid, S.4
  • 5
    • 0022419381 scopus 로고
    • Negative staining of myosin molecules
    • Walker M., Knight P., and Trinick J. Negative staining of myosin molecules. J. Mol. Biol. 184 (1985) 535-542
    • (1985) J. Mol. Biol. , vol.184 , pp. 535-542
    • Walker, M.1    Knight, P.2    Trinick, J.3
  • 6
    • 0025601653 scopus 로고
    • Skip residues correlate with bends in the myosin tail
    • Offer G. Skip residues correlate with bends in the myosin tail. J. Mol. Biol. 216 (1990) 213-218
    • (1990) J. Mol. Biol. , vol.216 , pp. 213-218
    • Offer, G.1
  • 7
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • Huxley H.E. The mechanism of muscular contraction. Science 164 (1969) 1356-1365
    • (1969) Science , vol.164 , pp. 1356-1365
    • Huxley, H.E.1
  • 9
    • 0021095262 scopus 로고
    • Stability and melting kinetics of structural domains in the myosin rod
    • Tsong T.Y., Himmelfarb S., and Harrington W.F. Stability and melting kinetics of structural domains in the myosin rod. J. Mol. Biol. 164 (1983) 431-450
    • (1983) J. Mol. Biol. , vol.164 , pp. 431-450
    • Tsong, T.Y.1    Himmelfarb, S.2    Harrington, W.F.3
  • 10
    • 0017336444 scopus 로고
    • Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility
    • Weeds A.G., and Pope B. Studies on the chymotryptic digestion of myosin. Effects of divalent cations on proteolytic susceptibility. J. Mol. Biol. 111 (1977) 129-157
    • (1977) J. Mol. Biol. , vol.111 , pp. 129-157
    • Weeds, A.G.1    Pope, B.2
  • 11
    • 0014693726 scopus 로고
    • Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation
    • Lowey S., Slayter H.S., Weeds A.G., and Baker H. Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. J. Mol. Biol. 42 (1969) 1-29
    • (1969) J. Mol. Biol. , vol.42 , pp. 1-29
    • Lowey, S.1    Slayter, H.S.2    Weeds, A.G.3    Baker, H.4
  • 12
    • 0021981596 scopus 로고
    • The amino acid sequence and stability predictions of the hinge region in myosin subfragment 2
    • Lu R.C., and Wong A. The amino acid sequence and stability predictions of the hinge region in myosin subfragment 2. J. Biol. Chem. 260 (1985) 3456-3461
    • (1985) J. Biol. Chem. , vol.260 , pp. 3456-3461
    • Lu, R.C.1    Wong, A.2
  • 13
    • 0023010840 scopus 로고
    • Electron microscope study of the effect of temperature on the length of the tail of the myosin molecule
    • Walker M., and Trinick J. Electron microscope study of the effect of temperature on the length of the tail of the myosin molecule. J. Mol. Biol. 192 (1986) 661-667
    • (1986) J. Mol. Biol. , vol.192 , pp. 661-667
    • Walker, M.1    Trinick, J.2
  • 14
    • 0022735554 scopus 로고
    • Melting of myosin rod as revealed by electron microscopy. II. Effects of temperature and pH on length and stability of myosin rod and its fragments
    • Walzthony D., Eppenberger H.M., Ueno H., Harrington W.F., and Wallimann T. Melting of myosin rod as revealed by electron microscopy. II. Effects of temperature and pH on length and stability of myosin rod and its fragments. Eur. J. Cell Biol. 41 (1986) 38-43
    • (1986) Eur. J. Cell Biol. , vol.41 , pp. 38-43
    • Walzthony, D.1    Eppenberger, H.M.2    Ueno, H.3    Harrington, W.F.4    Wallimann, T.5
  • 15
    • 12844288158 scopus 로고    scopus 로고
    • High flexibility of the actomyosin crossbridge resides in skeletal muscle myosin subfragment-2 as demonstrated by a new single molecule assay
    • Gundapaneni D., Xu J., and Root D.D. High flexibility of the actomyosin crossbridge resides in skeletal muscle myosin subfragment-2 as demonstrated by a new single molecule assay. J. Struct. Biol. 149 (2005) 117-126
    • (2005) J. Struct. Biol. , vol.149 , pp. 117-126
    • Gundapaneni, D.1    Xu, J.2    Root, D.D.3
  • 16
    • 11244260334 scopus 로고    scopus 로고
    • Mechanical properties of single myosin molecules probed with the photonic force microscope
    • Scholz T., Altmann S.M., Antognozzi M., Tischer C., Horber J.K., and Brenner B. Mechanical properties of single myosin molecules probed with the photonic force microscope. Biophys. J. 88 (2005) 360-371
    • (2005) Biophys. J. , vol.88 , pp. 360-371
    • Scholz, T.1    Altmann, S.M.2    Antognozzi, M.3    Tischer, C.4    Horber, J.K.5    Brenner, B.6
  • 17
    • 33646172749 scopus 로고    scopus 로고
    • Coiled-coil nanomechanics and uncoiling and unfolding of the superhelix and alpha-helices of myosin
    • Root D.D., Yadavalli V.K., Forbes J.G., and Wang K. Coiled-coil nanomechanics and uncoiling and unfolding of the superhelix and alpha-helices of myosin. Biophys. J. 90 (2006) 2852-2866
    • (2006) Biophys. J. , vol.90 , pp. 2852-2866
    • Root, D.D.1    Yadavalli, V.K.2    Forbes, J.G.3    Wang, K.4
  • 18
    • 0039892821 scopus 로고
    • On the origin of the contractile force in skeletal muscle
    • Harrington W.F. On the origin of the contractile force in skeletal muscle. Proc. Natl Acad. Sci. USA 76 (1979) 5066-5070
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 5066-5070
    • Harrington, W.F.1
  • 19
    • 0343721866 scopus 로고
    • Conformational transition in the myosin hinge upon activation of muscle
    • Ueno H., and Harrington W.F. Conformational transition in the myosin hinge upon activation of muscle. Proc. Natl Acad. Sci. USA 78 (1981) 6101-6105
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 6101-6105
    • Ueno, H.1    Harrington, W.F.2
  • 20
    • 0020606278 scopus 로고
    • Crossbridge release and alpha-helix-coil transition in myosin and rod minifilaments
    • Applegate D., and Reisler E. Crossbridge release and alpha-helix-coil transition in myosin and rod minifilaments. J. Mol. Biol. 169 (1983) 455-468
    • (1983) J. Mol. Biol. , vol.169 , pp. 455-468
    • Applegate, D.1    Reisler, E.2
  • 21
    • 0021764812 scopus 로고
    • An enzyme-probe study of motile domains in the subfragment-2 region of myosin
    • Ueno H., and Harrington W.F. An enzyme-probe study of motile domains in the subfragment-2 region of myosin. J. Mol. Biol. 180 (1984) 667-701
    • (1984) J. Mol. Biol. , vol.180 , pp. 667-701
    • Ueno, H.1    Harrington, W.F.2
  • 22
    • 0023042513 scopus 로고
    • Temperature-dependence of local melting in the myosin subfragment-2 region of the rigor cross-bridge
    • Ueno H., and Harrington W.F. Temperature-dependence of local melting in the myosin subfragment-2 region of the rigor cross-bridge. J. Mol. Biol. 190 (1986) 59-68
    • (1986) J. Mol. Biol. , vol.190 , pp. 59-68
    • Ueno, H.1    Harrington, W.F.2
  • 23
    • 0022477829 scopus 로고
    • Local melting in the subfragment-2 region of myosin in activated muscle and its correlation with contractile force
    • Ueno H., and Harrington W.F. Local melting in the subfragment-2 region of myosin in activated muscle and its correlation with contractile force. J. Mol. Biol. 190 (1986) 69-82
    • (1986) J. Mol. Biol. , vol.190 , pp. 69-82
    • Ueno, H.1    Harrington, W.F.2
  • 24
    • 0025328912 scopus 로고
    • Effects of ions and pH on the thermal stability of thin and thick filaments of skeletal muscle: high-sensitivity differential scanning calorimetric study
    • Bertazzon A., and Tsong T.Y. Effects of ions and pH on the thermal stability of thin and thick filaments of skeletal muscle: high-sensitivity differential scanning calorimetric study. Biochemistry 29 (1990) 6447-6452
    • (1990) Biochemistry , vol.29 , pp. 6447-6452
    • Bertazzon, A.1    Tsong, T.Y.2
  • 26
    • 0026769955 scopus 로고
    • Contraction characteristics and ATPase activity of skeletal muscle fibers in the presence of antibody to myosin subfragment 2
    • Sugi H., Kobayashi T., Gross T., Noguchi K., Karr T., and Harrington W.F. Contraction characteristics and ATPase activity of skeletal muscle fibers in the presence of antibody to myosin subfragment 2. Proc. Natl Acad. Sci. USA 89 (1992) 6134-6137
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 6134-6137
    • Sugi, H.1    Kobayashi, T.2    Gross, T.3    Noguchi, K.4    Karr, T.5    Harrington, W.F.6
  • 27
    • 0024785576 scopus 로고
    • Full-length rat alpha and beta cardiac myosin heavy chain sequences. Comparisons suggest a molecular basis for functional differences
    • McNally E.M., Kraft R., Bravo-Zehnder M., Taylor D.A., and Leinwand L.A. Full-length rat alpha and beta cardiac myosin heavy chain sequences. Comparisons suggest a molecular basis for functional differences. J. Mol. Biol. 210 (1989) 665-671
    • (1989) J. Mol. Biol. , vol.210 , pp. 665-671
    • McNally, E.M.1    Kraft, R.2    Bravo-Zehnder, M.3    Taylor, D.A.4    Leinwand, L.A.5
  • 28
    • 0024440446 scopus 로고
    • Complete nucleotide sequence of full length cDNA for rat alpha cardiac myosin heavy chain
    • McNally E.M., Gianola K.M., and Leinwand L.A. Complete nucleotide sequence of full length cDNA for rat alpha cardiac myosin heavy chain. Nucl. Acids Res. 17 (1989) 7527-7528
    • (1989) Nucl. Acids Res. , vol.17 , pp. 7527-7528
    • McNally, E.M.1    Gianola, K.M.2    Leinwand, L.A.3
  • 29
    • 0028574171 scopus 로고
    • Scallop striated and smooth muscle myosin heavy-chain isoforms are produced by alternative RNA splicing from a single gene
    • Nyitray L., Jancso A., Ochiai Y., Graf L., and Szent-Gyorgyi A.G. Scallop striated and smooth muscle myosin heavy-chain isoforms are produced by alternative RNA splicing from a single gene. Proc. Natl Acad. Sci. USA 91 (1994) 12686-12690
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12686-12690
    • Nyitray, L.1    Jancso, A.2    Ochiai, Y.3    Graf, L.4    Szent-Gyorgyi, A.G.5
  • 30
    • 0024711230 scopus 로고
    • Ultrastructural and molecular analyses of homozygous-viable Drosophila melanogaster muscle mutants indicate there is a complex pattern of myosin heavy-chain isoform distribution
    • O'Donnell P.T., Collier V.L., Mogami K., and Bernstein S.I. Ultrastructural and molecular analyses of homozygous-viable Drosophila melanogaster muscle mutants indicate there is a complex pattern of myosin heavy-chain isoform distribution. Genes, Dev. 3 (1989) 1233-1246
    • (1989) Genes, Dev. , vol.3 , pp. 1233-1246
    • O'Donnell, P.T.1    Collier, V.L.2    Mogami, K.3    Bernstein, S.I.4
  • 31
    • 0025836145 scopus 로고
    • Myosin functional domains encoded by alternative exons are expressed in specific thoracic muscles of Drosophila
    • Hastings G.A., and Emerson Jr. C.P. Myosin functional domains encoded by alternative exons are expressed in specific thoracic muscles of Drosophila. J. Cell Biol. 114 (1991) 263-276
    • (1991) J. Cell Biol. , vol.114 , pp. 263-276
    • Hastings, G.A.1    Emerson Jr., C.P.2
  • 32
    • 0029790426 scopus 로고    scopus 로고
    • Myosin heavy chain isoforms regulate muscle function but not myofibril assembly
    • Wells L., Edwards K.A., and Bernstein S.I. Myosin heavy chain isoforms regulate muscle function but not myofibril assembly. EMBO J. 15 (1996) 4454-4459
    • (1996) EMBO J. , vol.15 , pp. 4454-4459
    • Wells, L.1    Edwards, K.A.2    Bernstein, S.I.3
  • 33
    • 0035119730 scopus 로고    scopus 로고
    • Spatially and temporally regulated expression of myosin heavy chain alternative exons during Drosophila embryogenesis
    • Zhang S., and Bernstein S.I. Spatially and temporally regulated expression of myosin heavy chain alternative exons during Drosophila embryogenesis. Mech. Dev. 101 (2001) 35-45
    • (2001) Mech. Dev. , vol.101 , pp. 35-45
    • Zhang, S.1    Bernstein, S.I.2
  • 34
    • 0024366590 scopus 로고
    • Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons
    • George E.L., Ober M.B., and Emerson Jr. C.P. Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons. Mol. Cell Biol. 9 (1989) 2957-2974
    • (1989) Mol. Cell Biol. , vol.9 , pp. 2957-2974
    • George, E.L.1    Ober, M.B.2    Emerson Jr., C.P.3
  • 35
    • 0025291420 scopus 로고
    • Alternative myosin hinge regions are utilized in a tissue-specific fashion that correlates with muscle contraction speed
    • Collier V.L., Kronert W.A., O'Donnell P.T., Edwards K.A., and Bernstein S.I. Alternative myosin hinge regions are utilized in a tissue-specific fashion that correlates with muscle contraction speed. Genes Dev. 4 (1990) 885-895
    • (1990) Genes Dev. , vol.4 , pp. 885-895
    • Collier, V.L.1    Kronert, W.A.2    O'Donnell, P.T.3    Edwards, K.A.4    Bernstein, S.I.5
  • 36
    • 0020446736 scopus 로고
    • Coiled-coils in alpha-helix-containing proteins: analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins
    • Parry D.A. Coiled-coils in alpha-helix-containing proteins: analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins. Biosci. Rep. 2 (1982) 1017-1024
    • (1982) Biosci. Rep. , vol.2 , pp. 1017-1024
    • Parry, D.A.1
  • 37
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A., Van Dyke M., and Stock J. Predicting coiled coils from protein sequences. Science 252 (1991) 1162-1164
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 38
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled coil structures
    • Lupas A. Prediction and analysis of coiled coil structures. Methods Enzymol. 266 (1996) 513-525
    • (1996) Methods Enzymol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 39
    • 0020825822 scopus 로고
    • Differential localization of two myosins within nematode thick filaments
    • Miller III D.M., Ortiz I., Berliner G.C., and Epstein H.F. Differential localization of two myosins within nematode thick filaments. Cell 34 (1983) 477-490
    • (1983) Cell , vol.34 , pp. 477-490
    • Miller III, D.M.1    Ortiz, I.2    Berliner, G.C.3    Epstein, H.F.4
  • 40
    • 0034665602 scopus 로고    scopus 로고
    • Determining structure/function relationships for sarcomeric myosin heavy chain by genetic and transgenic manipulation of Drosophila
    • Swank D.M., Wells L., Kronert W.A., Morrill G.E., and Bernstein S.I. Determining structure/function relationships for sarcomeric myosin heavy chain by genetic and transgenic manipulation of Drosophila. Microsc. Res. Tech. 50 (2000) 430-442
    • (2000) Microsc. Res. Tech. , vol.50 , pp. 430-442
    • Swank, D.M.1    Wells, L.2    Kronert, W.A.3    Morrill, G.E.4    Bernstein, S.I.5
  • 41
    • 0024349052 scopus 로고
    • Tissue-specific expression of the alternately processed Drosophila myosin heavy-chain messenger RNAs
    • Kazzaz J.A., and Rozek C.E. Tissue-specific expression of the alternately processed Drosophila myosin heavy-chain messenger RNAs. Dev. Biol. 133 (1989) 550-561
    • (1989) Dev. Biol. , vol.133 , pp. 550-561
    • Kazzaz, J.A.1    Rozek, C.E.2
  • 42
    • 0028372246 scopus 로고
    • Tissue specific distribution of Drosophila sarcomeric myosin heavy-chain protein isoforms
    • Crough E.M., Kazzaz J.A., and Rozek C.E. Tissue specific distribution of Drosophila sarcomeric myosin heavy-chain protein isoforms. Insect Mol. Biol. 3 (1994) 15-26
    • (1994) Insect Mol. Biol. , vol.3 , pp. 15-26
    • Crough, E.M.1    Kazzaz, J.A.2    Rozek, C.E.3
  • 43
    • 0028926032 scopus 로고
    • Impairment of muscle function caused by mutations of phosphorylation sites in myosin regulatory light chain
    • Tohtong R., Yamashita H., Graham M., Haeberle J., Simcox A., and Maughan D. Impairment of muscle function caused by mutations of phosphorylation sites in myosin regulatory light chain. Nature 374 (1995) 650-653
    • (1995) Nature , vol.374 , pp. 650-653
    • Tohtong, R.1    Yamashita, H.2    Graham, M.3    Haeberle, J.4    Simcox, A.5    Maughan, D.6
  • 44
    • 3042631880 scopus 로고    scopus 로고
    • Cytokines, growth factors and sprouting at the neuromuscular junction
    • English A.W. Cytokines, growth factors and sprouting at the neuromuscular junction. J. Neurocytol. 32 (2003) 943-960
    • (2003) J. Neurocytol. , vol.32 , pp. 943-960
    • English, A.W.1
  • 45
    • 0021240963 scopus 로고
    • Mutations altering synaptic connectivity between identified neurons in Drosophila
    • Thomas J.B., and Wyman R.J. Mutations altering synaptic connectivity between identified neurons in Drosophila. J. Neurosci. 4 (1984) 530-538
    • (1984) J. Neurosci. , vol.4 , pp. 530-538
    • Thomas, J.B.1    Wyman, R.J.2
  • 46
    • 0029986094 scopus 로고    scopus 로고
    • Altered habituation of an identified escape circuit in Drosophila memory mutants
    • Engel J.E., and Wu C.F. Altered habituation of an identified escape circuit in Drosophila memory mutants. J. Neurosci. 16 (1996) 3486-3499
    • (1996) J. Neurosci. , vol.16 , pp. 3486-3499
    • Engel, J.E.1    Wu, C.F.2
  • 47
    • 0029813848 scopus 로고    scopus 로고
    • Influence of general anesthetics on a specific neural pathway in Drosophila melanogaster
    • Lin M., and Nash H.A. Influence of general anesthetics on a specific neural pathway in Drosophila melanogaster. Proc. Natl Acad. Sci. USA 93 (1996) 10446-10451
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10446-10451
    • Lin, M.1    Nash, H.A.2
  • 48
    • 0018941056 scopus 로고
    • Motor outputs of giant nerve fiber in Drosophila
    • Tanouye M.A., and Wyman R.J. Motor outputs of giant nerve fiber in Drosophila. J. Neurophysiol. 44 (1980) 405-421
    • (1980) J. Neurophysiol. , vol.44 , pp. 405-421
    • Tanouye, M.A.1    Wyman, R.J.2
  • 50
    • 33845397160 scopus 로고    scopus 로고
    • Passive stiffness in Drosophila indirect flight muscle reduced by disrupting paramyosin phosphorylation, but not by embryonic myosin S2 hinge substitution
    • Hao Y., Miller M.S., Swank D.M., Liu H., Bernstein S.I., Maughan D.W., and Pollack G.H. Passive stiffness in Drosophila indirect flight muscle reduced by disrupting paramyosin phosphorylation, but not by embryonic myosin S2 hinge substitution. Biophys. J. 91 (2006) 4500-4506
    • (2006) Biophys. J. , vol.91 , pp. 4500-4506
    • Hao, Y.1    Miller, M.S.2    Swank, D.M.3    Liu, H.4    Bernstein, S.I.5    Maughan, D.W.6    Pollack, G.H.7
  • 51
    • 0018094336 scopus 로고
    • Shape and flexibility of the myosin molecule
    • Elliott A., and Offer G. Shape and flexibility of the myosin molecule. J. Mol. Biol. 123 (1978) 505-519
    • (1978) J. Mol. Biol. , vol.123 , pp. 505-519
    • Elliott, A.1    Offer, G.2
  • 52
    • 0033118853 scopus 로고    scopus 로고
    • Assembly of thick filaments and myofibrils occurs in the absence of the myosin head
    • Cripps R.M., Suggs J.A., and Bernstein S.I. Assembly of thick filaments and myofibrils occurs in the absence of the myosin head. EMBO J. 18 (1999) 1793-1804
    • (1999) EMBO J. , vol.18 , pp. 1793-1804
    • Cripps, R.M.1    Suggs, J.A.2    Bernstein, S.I.3
  • 53
    • 0034739846 scopus 로고    scopus 로고
    • Flightin is essential for thick filament assembly and sarcomere stability in Drosophila flight muscles
    • Reedy M.C., Bullard B., and Vigoreaux J.O. Flightin is essential for thick filament assembly and sarcomere stability in Drosophila flight muscles. J. Cell Biol. 151 (2000) 1483-1500
    • (2000) J. Cell Biol. , vol.151 , pp. 1483-1500
    • Reedy, M.C.1    Bullard, B.2    Vigoreaux, J.O.3
  • 54
    • 33748286733 scopus 로고    scopus 로고
    • Electron tomography of swollen rigor fibers of insect flight muscle reveals a short and variably angled S2 domain
    • Liu J., Wu S., Reedy M.C., Winkler H., Lucaveche C., Cheng Y., et al. Electron tomography of swollen rigor fibers of insect flight muscle reveals a short and variably angled S2 domain. J. Mol. Biol. 362 (2006) 844-860
    • (2006) J. Mol. Biol. , vol.362 , pp. 844-860
    • Liu, J.1    Wu, S.2    Reedy, M.C.3    Winkler, H.4    Lucaveche, C.5    Cheng, Y.6
  • 55
    • 0024230185 scopus 로고
    • Molecular and ultrastructural defects in a Drosophila myosin heavy chain mutant: differential effects on muscle function produced by similar thick filament abnormalities
    • O'Donnell P.T., and Bernstein S.I. Molecular and ultrastructural defects in a Drosophila myosin heavy chain mutant: differential effects on muscle function produced by similar thick filament abnormalities. J. Cell Biol. 107 (1988) 2601-2612
    • (1988) J. Cell Biol. , vol.107 , pp. 2601-2612
    • O'Donnell, P.T.1    Bernstein, S.I.2
  • 56
    • 0025835226 scopus 로고
    • Structurally different Drosophila striated muscles utilize distinct variants of Z-band-associated proteins
    • Vigoreaux J.O., Saide J.D., and Pardue M.L. Structurally different Drosophila striated muscles utilize distinct variants of Z-band-associated proteins. J. Muscle Res. Cell Motil. 12 (1991) 340-354
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 340-354
    • Vigoreaux, J.O.1    Saide, J.D.2    Pardue, M.L.3
  • 59
    • 1842526983 scopus 로고    scopus 로고
    • Rates of force generation in Drosophila fast and slow muscle types have opposite responses to phosphate
    • Swank D.M., and Maughan D.W. Rates of force generation in Drosophila fast and slow muscle types have opposite responses to phosphate. Advan. Expt. Med. Biol. 538 (2003) 459-467
    • (2003) Advan. Expt. Med. Biol. , vol.538 , pp. 459-467
    • Swank, D.M.1    Maughan, D.W.2
  • 60
    • 0027276728 scopus 로고
    • Flightin, a novel myofibrillar protein of Drosophila stretch-activated muscles
    • Vigoreaux J.O., Saide J.D., Valgeirsdottir K., and Pardue M.L. Flightin, a novel myofibrillar protein of Drosophila stretch-activated muscles. J. Cell Biol. 121 (1993) 587-598
    • (1993) J. Cell Biol. , vol.121 , pp. 587-598
    • Vigoreaux, J.O.1    Saide, J.D.2    Valgeirsdottir, K.3    Pardue, M.L.4
  • 61
    • 0028580703 scopus 로고
    • Multiple isoelectric variants of flightin in Drosophila stretch-activated muscles are generated by temporally regulated phosphorylations
    • Vigoreaux J.O., and Perry L.M. Multiple isoelectric variants of flightin in Drosophila stretch-activated muscles are generated by temporally regulated phosphorylations. J. Muscle Res. Cell Motil. 15 (1994) 607-616
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 607-616
    • Vigoreaux, J.O.1    Perry, L.M.2
  • 62
    • 0027992658 scopus 로고
    • Alterations in flightin phosphorylation in Drosophila flight muscles are associated with myofibrillar defects engendered by actin and myosin heavy-chain mutant alleles
    • Vigoreaux J.O. Alterations in flightin phosphorylation in Drosophila flight muscles are associated with myofibrillar defects engendered by actin and myosin heavy-chain mutant alleles. Biochem. Genet. 32 (1994) 301-314
    • (1994) Biochem. Genet. , vol.32 , pp. 301-314
    • Vigoreaux, J.O.1
  • 63
    • 0346450472 scopus 로고    scopus 로고
    • Flightin is a myosin rod binding protein
    • Ayer G., and Vigoreaux J.O. Flightin is a myosin rod binding protein. Cell Biochem. Biophys. 38 (2003) 41-54
    • (2003) Cell Biochem. Biophys. , vol.38 , pp. 41-54
    • Ayer, G.1    Vigoreaux, J.O.2
  • 64
    • 0347358011 scopus 로고    scopus 로고
    • Mutations that affect flightin expression in Drosophila alter the viscoelastic properties of flight muscle fibers
    • Henkin J.A., Maughan D.W., and Vigoreaux J.O. Mutations that affect flightin expression in Drosophila alter the viscoelastic properties of flight muscle fibers. Am. J. Physiol. Cell Physiol. 286 (2004) C65-C72
    • (2004) Am. J. Physiol. Cell Physiol. , vol.286
    • Henkin, J.A.1    Maughan, D.W.2    Vigoreaux, J.O.3
  • 65
    • 28444467781 scopus 로고    scopus 로고
    • Stretchin-klp, a novel Drosophila indirect flight muscle protein, has both myosin dependent and independent isoforms
    • Patel S.R., and Saide J.D. Stretchin-klp, a novel Drosophila indirect flight muscle protein, has both myosin dependent and independent isoforms. J. Muscle Res. Cell Motil. 26 (2005) 213-224
    • (2005) J. Muscle Res. Cell Motil. , vol.26 , pp. 213-224
    • Patel, S.R.1    Saide, J.D.2
  • 66
    • 4444288620 scopus 로고    scopus 로고
    • Alternative N-terminal regions of Drosophila myosin heavy chain tune muscle kinetics for optimal power output
    • Swank D.M., Kronert W.A., Bernstein S.I., and Maughan D.W. Alternative N-terminal regions of Drosophila myosin heavy chain tune muscle kinetics for optimal power output. Biophys. J. 87 (2004) 1805-1814
    • (2004) Biophys. J. , vol.87 , pp. 1805-1814
    • Swank, D.M.1    Kronert, W.A.2    Bernstein, S.I.3    Maughan, D.W.4
  • 69
    • 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., and Gibson T.J. 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 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 72
    • 0019945644 scopus 로고
    • Genetic transformation of Drosophila with transposable element vectors
    • Rubin G.M., and Spradling A.C. Genetic transformation of Drosophila with transposable element vectors. Science 218 (1982) 348-353
    • (1982) Science , vol.218 , pp. 348-353
    • Rubin, G.M.1    Spradling, A.C.2
  • 73
    • 0038529926 scopus 로고    scopus 로고
    • Generation of transgenic Drosophila melanogaster by P element-mediated germline transformation
    • Norton P.A., and Steel L.F. (Eds), Eaton Publishing, Natick, MA
    • Cripps R.M., and Bernstein S.I. Generation of transgenic Drosophila melanogaster by P element-mediated germline transformation. In: Norton P.A., and Steel L.F. (Eds). Gene Transfer Methods: Introducing DNA into Living Cells and Organisms (2000), Eaton Publishing, Natick, MA 93-125
    • (2000) Gene Transfer Methods: Introducing DNA into Living Cells and Organisms , pp. 93-125
    • Cripps, R.M.1    Bernstein, S.I.2
  • 75
    • 0035805601 scopus 로고    scopus 로고
    • Alternative exon-encoded regions of Drosophila myosin heavy chain modulate ATPase rates and actin sliding velocity
    • Swank D.M., Bartoo M.L., Knowles A.F., Iliffe C., Bernstein S.I., Molloy J.E., and Sparrow J.C. Alternative exon-encoded regions of Drosophila myosin heavy chain modulate ATPase rates and actin sliding velocity. J. Biol. Chem. 276 (2001) 15117-15124
    • (2001) J. Biol. Chem. , vol.276 , pp. 15117-15124
    • Swank, D.M.1    Bartoo, M.L.2    Knowles, A.F.3    Iliffe, C.4    Bernstein, S.I.5    Molloy, J.E.6    Sparrow, J.C.7
  • 76
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 77
    • 0025794119 scopus 로고
    • Characterisation of missense mutations in the Act88F gene of Drosophila melanogaster
    • Drummond D.R., Hennessey E.S., and Sparrow J.C. Characterisation of missense mutations in the Act88F gene of Drosophila melanogaster. Mol. Gen. Genet. 226 (1991) 70-80
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 70-80
    • Drummond, D.R.1    Hennessey, E.S.2    Sparrow, J.C.3
  • 78
    • 23044517329 scopus 로고    scopus 로고
    • Drosophila CAKI/CMG protein, a homolog of human CASK, is essential for regulation of neurotransmitter vesicle release
    • Zordan M.A., Massironi M., Ducato M.G., Te Kronnie G., Costa R., Reggiani C., et al. Drosophila CAKI/CMG protein, a homolog of human CASK, is essential for regulation of neurotransmitter vesicle release. J. Neurophysiol. 94 (2005) 1074-1083
    • (2005) J. Neurophysiol. , vol.94 , pp. 1074-1083
    • Zordan, M.A.1    Massironi, M.2    Ducato, M.G.3    Te Kronnie, G.4    Costa, R.5    Reggiani, C.6
  • 79
    • 0021322086 scopus 로고
    • Length of myosin rod and its proteolytic fragments determined by electron microscopy
    • Stewart M., and Edwards P. Length of myosin rod and its proteolytic fragments determined by electron microscopy. FEBS Letters 168 (1984) 75-78
    • (1984) FEBS Letters , vol.168 , pp. 75-78
    • Stewart, M.1    Edwards, P.2


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