메뉴 건너뛰기




Volumn 10, Issue 1, 1999, Pages 135-149

Differential epitope tagging of actin in transformed Drosophila produces distinct effects on myofibril assembly and function of the indirect flight muscle

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 0032894399     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.1.135     Document Type: Article
Times cited : (20)

References (67)
  • 1
    • 0025783320 scopus 로고
    • Interference with myosin subfragment-1 binding by site directed mutagenesis
    • Aspenström, P., and Karlsson, R. (1991). Interference with myosin subfragment-1 binding by site directed mutagenesis. Eur. J. Biochem. 200, 35-41.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 35-41
    • Aspenström, P.1    Karlsson, R.2
  • 2
    • 0026520981 scopus 로고
    • Site-specific ammo-terminal mutants of yeast-expressed β-actin
    • Aspenström, P., Lindberg, U., and Karlsson, R. (1992). Site-specific ammo-terminal mutants of yeast-expressed β-actin. FEBS Lett. 303, 59-63.
    • (1992) FEBS Lett. , vol.303 , pp. 59-63
    • Aspenström, P.1    Lindberg, U.2    Karlsson, R.3
  • 3
    • 0027248807 scopus 로고
    • Mutations in β-actin: Influence on polymer formation and on interactions with myosin and profilin
    • Aspenström, P., Schutt, C., Lindberg, U., and Karlsson, R. (1993). Mutations in β-actin: influence on polymer formation and on interactions with myosin and profilin. FEBS Lett. 1, 163-170.
    • (1993) FEBS Lett. , vol.1 , pp. 163-170
    • Aspenström, P.1    Schutt, C.2    Lindberg, U.3    Karlsson, R.4
  • 4
    • 0023663064 scopus 로고
    • Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate
    • Ball, E., Karlik, C.C., Beall, C.J., Saville, D.L., Sparrow, J.C., Bullard, B., and Fyrberg, E.A. (1987). Arthrin, a myofibrillar protein of insect flight muscle, is an actin-ubiquitin conjugate. Cell 51, 221-228.
    • (1987) Cell , vol.51 , pp. 221-228
    • Ball, E.1    Karlik, C.C.2    Beall, C.J.3    Saville, D.L.4    Sparrow, J.C.5    Bullard, B.6    Fyrberg, E.A.7
  • 5
    • 0024617347 scopus 로고
    • Genetic dissection of Drosophila myofibril formation
    • Beall, C.J., Sepanski, M.A., and Fyrberg, E.A. (1989). Genetic dissection of Drosophila myofibril formation. Genes & Dev. 3, 131-140.
    • (1989) Genes & Dev. , vol.3 , pp. 131-140
    • Beall, C.J.1    Sepanski, M.A.2    Fyrberg, E.A.3
  • 6
    • 0030575783 scopus 로고    scopus 로고
    • The structure of an open state of β-actin at 2.65 Å resolution
    • Chik, J.K., Lindberg, U., and Schutt, C.E. (1996). The structure of an open state of β-actin at 2.65 Å resolution. J. Mol. Biol. 263, 607-623.
    • (1996) J. Mol. Biol. , vol.263 , pp. 607-623
    • Chik, J.K.1    Lindberg, U.2    Schutt, C.E.3
  • 7
    • 0021272952 scopus 로고
    • Phalloidin enhances actin assembly by preventing monomer dissociation
    • Collucio, L.M., and Tilney, L.G. (1984). Phalloidin enhances actin assembly by preventing monomer dissociation. J. Cell Biol. 99, 529-535.
    • (1984) J. Cell Biol. , vol.99 , pp. 529-535
    • Collucio, L.M.1    Tilney, L.G.2
  • 8
    • 0026794025 scopus 로고
    • Removal of the amino-terminal acidic residues of yeast actin
    • Cook, R.K, Blake, W.T., and Rubenstein, P.A. (1992). Removal of the amino-terminal acidic residues of yeast actin. J. Biol. Chem. 267, 9430-9436.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9430-9436
    • Cook, R.K.1    Blake, W.T.2    Rubenstein, P.A.3
  • 9
    • 0026075785 scopus 로고
    • Unusual metabolism of the yeast actin amino terminus
    • Cook, R.K., Sheff, D.R., and Rubenstein, P.A. (1991). Unusual metabolism of the yeast actin amino terminus. J. Biol. Chem. 266, 16825-16833.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16825-16833
    • Cook, R.K.1    Sheff, D.R.2    Rubenstein, P.A.3
  • 10
    • 0020533805 scopus 로고
    • Pyrene actin: Documentation of the validity of a sensitive assay for actin polymerization
    • Cooper, J.A., Walker, S.B., and Pollard, T.D. (1983). Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J. Muscle Res. Cell Motil. 4, 253-262.
    • (1983) J. Muscle Res. Cell Motil. , vol.4 , pp. 253-262
    • Cooper, J.A.1    Walker, S.B.2    Pollard, T.D.3
  • 11
    • 0027931534 scopus 로고
    • Transformation of Drosophila melanogaster with the wild-type myosin heavy-chain gene: Rescue of mutant phenotypes and analysis of defects caused by overexpression
    • Cripps, R.M., Becker, K.D., Mardahl, M., Kronert, W.A., Hodges, D., and Bernstein, S.I. (1994). Transformation of Drosophila melanogaster with the wild-type myosin heavy-chain gene: rescue of mutant phenotypes and analysis of defects caused by overexpression. J. Cell Biol. 126, 689-699.
    • (1994) J. Cell Biol. , vol.126 , pp. 689-699
    • Cripps, R.M.1    Becker, K.D.2    Mardahl, M.3    Kronert, W.A.4    Hodges, D.5    Bernstein, S.I.6
  • 12
    • 0027967683 scopus 로고
    • Structural connectivity in actin: Effects of C-terminal modifications on the properties of actin
    • Crosbie, R.H., Miller, C., Cheung, P., Goodnight, T., Muhlrad, A., and Reisler, E. (1994). Structural connectivity in actin: effects of C-terminal modifications on the properties of actin. Biophys. J. 67, 1957-1964.
    • (1994) Biophys. J. , vol.67 , pp. 1957-1964
    • Crosbie, R.H.1    Miller, C.2    Cheung, P.3    Goodnight, T.4    Muhlrad, A.5    Reisler, E.6
  • 13
    • 0025794119 scopus 로고
    • Characterization of missense mutations in the Act88F gene of Drosophila melanogaster
    • Drummond, D.R., Hennessey, E.S., and Sparrow, J.C. (1991). Characterization of missense mutations in the Act88F gene of Drosophila melanogaster. Mol. Gen. Genet. 226, 70-80.
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 70-80
    • Drummond, D.R.1    Hennessey, E.S.2    Sparrow, J.C.3
  • 14
    • 0026768578 scopus 로고
    • The binding of mutant actins to profilin, ATP and DNase I
    • Drummond, D.R., Hennessey, E.S., and Sparrow, J.C. (1992). The binding of mutant actins to profilin, ATP and DNase I. Eur. J. Biochem. 209, 171-179.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 171-179
    • Drummond, D.R.1    Hennessey, E.S.2    Sparrow, J.C.3
  • 15
    • 0025258860 scopus 로고
    • Alteration in cross-bridge kinetics caused by mutations in actin
    • Drummond, D.R., Peckham, M., Sparrow, J.C., and White, D.C.S. (1990). Alteration in cross-bridge kinetics caused by mutations in actin. Nature 348, 440-442.
    • (1990) Nature , vol.348 , pp. 440-442
    • Drummond, D.R.1    Peckham, M.2    Sparrow, J.C.3    White, D.C.S.4
  • 16
    • 0019519177 scopus 로고
    • Mechanism of action of phalloidin on the polymerization of muscle actin
    • Estes, J.E., Selden, L.A., and Gershman, L.C. (1981). Mechanism of action of phalloidin on the polymerization of muscle actin. Biochemistry 20, 708-712.
    • (1981) Biochemistry , vol.20 , pp. 708-712
    • Estes, J.E.1    Selden, L.A.2    Gershman, L.C.3
  • 17
    • 0025325694 scopus 로고
    • Molecular genetics of Drosophila α-actinin: Mutant alleles disrupt Z disk integrity and muscle insertions
    • Fyrberg, E., Kelly, M., Ball, E., Fyrberg, C., and Reedy, M.C. (1990). Molecular genetics of Drosophila α-actinin: mutant alleles disrupt Z disk integrity and muscle insertions. J. Cell Biol. 110, 1999-2011.
    • (1990) J. Cell Biol. , vol.110 , pp. 1999-2011
    • Fyrberg, E.1    Kelly, M.2    Ball, E.3    Fyrberg, C.4    Reedy, M.C.5
  • 18
    • 0020581716 scopus 로고
    • Transcript of the six Drosophila actin genes accumulate in a stage-and tissue-specific manner
    • Fyrberg, E.A., Mahaffey, J.W., Bond, J., and Davidson, N. (1983). Transcript of the six Drosophila actin genes accumulate in a stage-and tissue-specific manner. Cell 33, 115-123.
    • (1983) Cell , vol.33 , pp. 115-123
    • Fyrberg, E.A.1    Mahaffey, J.W.2    Bond, J.3    Davidson, N.4
  • 20
    • 0030727339 scopus 로고    scopus 로고
    • Evidence for a conformational change in actin induced by fimbrin (N375) binding
    • Hanein, D., Matsudaira, P., and DeRosier, D.J. (1997). Evidence for a conformational change in actin induced by fimbrin (N375) binding. J. Cell Biol. 139, 387-396.
    • (1997) J. Cell Biol. , vol.139 , pp. 387-396
    • Hanein, D.1    Matsudaira, P.2    DeRosier, D.J.3
  • 21
    • 0001089240 scopus 로고
    • Actin gene mutations in Drosophila; heat shock activation in the indirect flight muscles
    • Hiromi, Y., and Hotta, Y. (1985). Actin gene mutations in Drosophila; heat shock activation in the indirect flight muscles. EMBO J. 4, 1681-1687.
    • (1985) EMBO J. , vol.4 , pp. 1681-1687
    • Hiromi, Y.1    Hotta, Y.2
  • 22
    • 0022552545 scopus 로고
    • Germline transformation with Drosophila mutant actin genes induces constitutive expression of heat shock genes
    • Hiromi, Y., Okamoto, H., Gehring, W.J., and Hotta, Y. (1986). Germline transformation with Drosophila mutant actin genes induces constitutive expression of heat shock genes. Cell 44, 293-301.
    • (1986) Cell , vol.44 , pp. 293-301
    • Hiromi, Y.1    Okamoto, H.2    Gehring, W.J.3    Hotta, Y.4
  • 23
    • 0025075839 scopus 로고
    • Atomic model of the actin filament
    • Holmes, K.C., Popp, D., Gebhard, W., and Kabsch, W. (1990). Atomic model of the actin filament. Nature 347, 44-49.
    • (1990) Nature , vol.347 , pp. 44-49
    • Holmes, K.C.1    Popp, D.2    Gebhard, W.3    Kabsch, W.4
  • 24
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R.M., Hunt, H.D., Ho, S.N., Pullen, J.K., and Pease, L.R. (1989). Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77, 61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 26
    • 0031439662 scopus 로고    scopus 로고
    • Isoform specificity in the relationship of actin to dendritic spines
    • Kaech, S., Fischer, M., Doll, T., and Matus, A. (1997). Isoform specificity in the relationship of actin to dendritic spines. J. Neurosci. 24, 9565-9572.
    • (1997) J. Neurosci. , vol.24 , pp. 9565-9572
    • Kaech, S.1    Fischer, M.2    Doll, T.3    Matus, A.4
  • 27
    • 0023404166 scopus 로고
    • Two missense alleles of the Drosophila melanogaster act88F actin gene are strongly antimorphic but only weakly induce synthesis of heat shock proteins
    • Karlik, C.C., Saville, D.L., and Fyrberg, E.A. (1987). Two missense alleles of the Drosophila melanogaster act88F actin gene are strongly antimorphic but only weakly induce synthesis of heat shock proteins. Mol. Cell. Biol. 7, 3084-3091.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3084-3091
    • Karlik, C.C.1    Saville, D.L.2    Fyrberg, E.A.3
  • 28
    • 0023665624 scopus 로고
    • The white gene as a marker in a new P-element vector for gene transfer in Drosophila
    • Klemenz, R., Weber, U., and Gehring, W.J. (1987). The white gene as a marker in a new P-element vector for gene transfer in Drosophila. Nucleic Acids Res. 15, 3947-3959.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 3947-3959
    • Klemenz, R.1    Weber, U.2    Gehring, W.J.3
  • 29
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodo-acetamide-labeled F-actin
    • Kouyama, T., and Mihashi, K. (1981). Fluorimetry study of N-(1-pyrenyl)iodo-acetamide-labeled F-actin. Eur. J. Biochem. 114, 33-38.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 30
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    • Kreis, T.E. (1986). Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO J. 5, 931-941.
    • (1986) EMBO J. , vol.5 , pp. 931-941
    • Kreis, T.E.1
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., Popp, D., and Holmes, K.C. (1993). Refinement of the F-actin model against x-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234, 826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 34
    • 0019129296 scopus 로고
    • An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actin
    • Lubit, B.W., and Schwartz, J.H. (1980). An antiactin antibody that distinguishes between cytoplasmic and skeletal muscle actin. J. Cell Biol. 86, 891-897.
    • (1980) J. Cell Biol. , vol.86 , pp. 891-897
    • Lubit, B.W.1    Schwartz, J.H.2
  • 35
  • 36
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough, A., Pope, B., Chiu, W., and Weeds, A. (1997). Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138, 771-781.
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 37
    • 0028176006 scopus 로고
    • Determination of the a-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis
    • McGough, A., Way, M., and DeRosier, D. (1994). Determination of the a-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis. J. Cell Biol. 126, 433-443.
    • (1994) J. Cell Biol. , vol.126 , pp. 433-443
    • McGough, A.1    Way, M.2    DeRosier, D.3
  • 38
    • 0026535887 scopus 로고
    • Structure of actin observed by fluorescence resonance energy transfer spectroscopy
    • Miki, M., O'Donoghue, S.I., and Dos Remedios, C.G. (1992). Structure of actin observed by fluorescence resonance energy transfer spectroscopy. J. Muscle Res. Cell Motil. 13, 132-145.
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 132-145
    • Miki, M.1    O'Donoghue, S.I.2    Dos Remedios, C.G.3
  • 39
    • 0030449743 scopus 로고    scopus 로고
    • Mutational analysis of the role of the N terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle
    • Miller, C.J., Wong, W.W., Bobkova, E., Rubenstein, P.A., and Reisler, E. (1996). Mutational analysis of the role of the N terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle. Biochemistry 35, 16557-16565.
    • (1996) Biochemistry , vol.35 , pp. 16557-16565
    • Miller, C.J.1    Wong, W.W.2    Bobkova, E.3    Rubenstein, P.A.4    Reisler, E.5
  • 40
    • 0030048070 scopus 로고    scopus 로고
    • Protein-protein interactions in the rigor actomyosin complex
    • Milligan, R.A. (1996). Protein-protein interactions in the rigor actomyosin complex. Proc. Natl. Acad. Sci. USA 93, 21-26.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 21-26
    • Milligan, R.A.1
  • 41
    • 0025052483 scopus 로고
    • Molecular structure of F-actin and location of surface binding sites
    • Milligan, R.A., Whittaker, M., and Safer, D. (1990). Molecular structure of F-actin and location of surface binding sites. Nature 348, 217-221.
    • (1990) Nature , vol.348 , pp. 217-221
    • Milligan, R.A.1    Whittaker, M.2    Safer, D.3
  • 42
    • 0019741511 scopus 로고
    • Isolation of Drosophila flightless mutants which affect myofibrillar proteins of indirect flight muscles
    • Mogami, K., and Hotta, Y. (1981). Isolation of Drosophila flightless mutants which affect myofibrillar proteins of indirect flight muscles. Mol. Gen. Genet. 183, 409-417.
    • (1981) Mol. Gen. Genet. , vol.183 , pp. 409-417
    • Mogami, K.1    Hotta, Y.2
  • 44
    • 0027452835 scopus 로고
    • Proteolitic removal of three C-terminal residues of actin alters the monomer-monomer interactions
    • Mossakowska, M., Moraczewska, J., Khaitlina, S., and Strzelecka-Golaszewska, H. (1993). Proteolitic removal of three C-terminal residues of actin alters the monomer-monomer interactions. Biochem. J. 289, 897-902.
    • (1993) Biochem. J. , vol.289 , pp. 897-902
    • Mossakowska, M.1    Moraczewska, J.2    Khaitlina, S.3    Strzelecka-Golaszewska, H.4
  • 45
    • 0030909829 scopus 로고    scopus 로고
    • Transfected muscle and nonmuscle actins are differentially sorted by cultured smooth muscle and nonmuscle cells
    • Mounier, N., Perriard, J.-C, Gabbiani, G., and Chaponnier, C. (1997). Transfected muscle and nonmuscle actins are differentially sorted by cultured smooth muscle and nonmuscle cells. J. Cell Sci. 110, 839-846.
    • (1997) J. Cell Sci. , vol.110 , pp. 839-846
    • Mounier, N.1    Perriard, J.-C.2    Gabbiani, G.3    Chaponnier, C.4
  • 46
    • 0026558989 scopus 로고
    • Removing the two C-terminal residues of actin affects the filament structure
    • O'Donoghue, S.I., Miki, M., and dos Remedies, C.G. (1992). Removing the two C-terminal residues of actin affects the filament structure. Arch. Biochem. Biophys. 293, 110-116.
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 110-116
    • O'Donoghue, S.I.1    Miki, M.2    Dos Remedies, C.G.3
  • 47
    • 0000519384 scopus 로고
    • Molecular characterization of mutant actin genes which induce heat-shock proteins in Drosophila flight muscles
    • Okamoto, H., Hiromi, Y., Ishikawa, E., Yamada, T., Isoda, K., Maekawa, H., and Hotta, Y. (1986). Molecular characterization of mutant actin genes which induce heat-shock proteins in Drosophila flight muscles. EMBO J. 5, 589-596.
    • (1986) EMBO J. , vol.5 , pp. 589-596
    • Okamoto, H.1    Hiromi, Y.2    Ishikawa, E.3    Yamada, T.4    Isoda, K.5    Maekawa, H.6    Hotta, Y.7
  • 48
    • 0031571664 scopus 로고    scopus 로고
    • Modulation of yeast F-actin structure by a mutation in the nucleotide-binding cleft
    • Orlova, A., Chen, X., Rubenstein, P.A., and Egelman, E.D. (1997). Modulation of yeast F-actin structure by a mutation in the nucleotide-binding cleft. J. Mol. Biol. 271, 235-243.
    • (1997) J. Mol. Biol. , vol.271 , pp. 235-243
    • Orlova, A.1    Chen, X.2    Rubenstein, P.A.3    Egelman, E.D.4
  • 50
    • 0027133588 scopus 로고
    • Ultrastructure of developing flight muscle in Drosophila. I. Assembly of myofibrils
    • Reedy, M.C., and Beall, C. (1993). Ultrastructure of developing flight muscle in Drosophila. I. Assembly of myofibrils. Dev. Biol. 160, 443-465.
    • (1993) Dev. Biol. , vol.160 , pp. 443-465
    • Reedy, M.C.1    Beall, C.2
  • 51
    • 0024319494 scopus 로고
    • Formation of reverse rigor chevrons by myosin heads
    • Reedy, M.C., Beall, C., and Fyrberg, E. (1989). Formation of reverse rigor chevrons by myosin heads. Nature 339, 481-483.
    • (1989) Nature , vol.339 , pp. 481-483
    • Reedy, M.C.1    Beall, C.2    Fyrberg, E.3
  • 52
    • 0009526303 scopus 로고
    • Do variant residues among the six actin isoforms of Drosophila reflect functional specialization?
    • abstract
    • Reedy, M.C., Beall, C., and Fyrberg, E. (1991). Do variant residues among the six actin isoforms of Drosophila reflect functional specialization? Biophys. J. 59, 187a (abstract).
    • (1991) Biophys. J. , vol.59
    • Reedy, M.C.1    Beall, C.2    Fyrberg, E.3
  • 53
    • 0019945644 scopus 로고
    • Genetic transformation of Drosophila with transposable element vectors
    • Rubin, G.M., and Spradling, A.C. (1982). Genetic transformation of Drosophila with transposable element vectors. Science 218, 348-353.
    • (1982) Science , vol.218 , pp. 348-353
    • Rubin, G.M.1    Spradling, A.C.2
  • 54
    • 0025343153 scopus 로고
    • Actin with tumor-related mutation is antimorphic in Drosophila muscle: Two distinct modes of myofibrillar disruption by antimorphic actins
    • Sakai, U., Okamoto, H., Mogami, K., Yamada, T., and Hotta, Y. (1990). Actin with tumor-related mutation is antimorphic in Drosophila muscle: two distinct modes of myofibrillar disruption by antimorphic actins. J. Biochem. 107, 499-505.
    • (1990) J. Biochem. , vol.107 , pp. 499-505
    • Sakai, U.1    Okamoto, H.2    Mogami, K.3    Yamada, T.4    Hotta, Y.5
  • 55
    • 0021349790 scopus 로고
    • Analysis of myofibrillar structure and assembly using fluorescently-labeled contractile proteins
    • Sanger, J.W., Mittal, B., and Sanger, J.M. (1984). Analysis of myofibrillar structure and assembly using fluorescently-labeled contractile proteins. J. Cell Biol. 98, 825-833.
    • (1984) J. Cell Biol. , vol.98 , pp. 825-833
    • Sanger, J.W.1    Mittal, B.2    Sanger, J.M.3
  • 56
    • 0028115630 scopus 로고
    • Three-dimensional structure of a single filament in the Limulus acrosomal bundle: Scruin binds to homologous helix-loop-β motifs in actin
    • Schmid, M.F., Agris, J., Jakana, J., Matsudaira, P., and Chiu, W. (1994). Three-dimensional structure of a single filament in the Limulus acrosomal bundle: scruin binds to homologous helix-loop-β motifs in actin. J. Cell Biol. 124, 341-350.
    • (1994) J. Cell Biol. , vol.124 , pp. 341-350
    • Schmid, M.F.1    Agris, J.2    Jakana, J.3    Matsudaira, P.4    Chiu, W.5
  • 58
    • 0028933051 scopus 로고
    • Structural studies on the ribbon-to-helix transition in profilin:Actin crystals
    • Schutt, C.E., Rozycki, M.D., Chik, J., and Lindberg, U. (1995b). Structural studies on the ribbon-to-helix transition in profilin:actin crystals. Biophys. J. 68, 12s-18s.
    • (1995) Biophys. J. , vol.68
    • Schutt, C.E.1    Rozycki, M.D.2    Chik, J.3    Lindberg, U.4
  • 60
    • 0022881517 scopus 로고
    • A monoclonal antibody against α-smooth muscle actin: A new probe for smooth muscle differentiation
    • Skalli, O., Ropraz, P., Trzeciak, A., Benzonana, G., Gillessen, D., and Gabbiani, G. (1986). A monoclonal antibody against α-smooth muscle actin: a new probe for smooth muscle differentiation. J. Cell Biol. 103, 2787-2796.
    • (1986) J. Cell Biol. , vol.103 , pp. 2787-2796
    • Skalli, O.1    Ropraz, P.2    Trzeciak, A.3    Benzonana, G.4    Gillessen, D.5    Gabbiani, G.6
  • 61
    • 0025917462 scopus 로고
    • Intracompartmental sorting of essential myosin light chains: Molecular dissection and in vivo monitoring by epitope tagging
    • Soldati, T., and Perriard, J.C. (1991). Intracompartmental sorting of essential myosin light chains: molecular dissection and in vivo monitoring by epitope tagging. Cell 66, 277-289.
    • (1991) Cell , vol.66 , pp. 277-289
    • Soldati, T.1    Perriard, J.C.2
  • 62
    • 0026332295 scopus 로고
    • Functional and ultrastructural effects of a missense mutation in the indirect flight muscle-specific actin gene of Drosophila melanogaster
    • Sparrow, J., Reedy, M., Ball, E., Kyrtatas, V., Molloy, J., Durston, J., Hennessey, E., and White, D. (1991). Functional and ultrastructural effects of a missense mutation in the indirect flight muscle-specific actin gene of Drosophila melanogaster. J. Mol. Biol. 222, 963-982.
    • (1991) J. Mol. Biol. , vol.222 , pp. 963-982
    • Sparrow, J.1    Reedy, M.2    Ball, E.3    Kyrtatas, V.4    Molloy, J.5    Durston, J.6    Hennessey, E.7    White, D.8
  • 63
    • 0025858239 scopus 로고
    • Site-directed mutations of Dictyostelium actin: Disruption of a negative charge cluster at the N-terminus
    • Sutoh, K., Ando, M., and Toyoshima, Y.Y. (1991). Site-directed mutations of Dictyostelium actin: disruption of a negative charge cluster at the N-terminus. Proc. Natl. Acad. Sci. USA 88, 7711-7714.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7711-7714
    • Sutoh, K.1    Ando, M.2    Toyoshima, Y.Y.3
  • 64
    • 0029615379 scopus 로고
    • Dominant negative effect of cytoplasmic actin isoproteins on cardiomyocyte cytoarchitecture and function
    • von Arx, P., Bantle, S., Soldati, T., and Perriard, J.C. (1995). Dominant negative effect of cytoplasmic actin isoproteins on cardiomyocyte cytoarchitecture and function. J. Cell Biol. 131, 1759-1773.
    • (1995) J. Cell Biol. , vol.131 , pp. 1759-1773
    • Von Arx, P.1    Bantle, S.2    Soldati, T.3    Perriard, J.C.4
  • 65
    • 0027062885 scopus 로고
    • Myosin light chain-2 mutation affects flight, wing beat frequency, and indirect flight muscle contraction kinetics in Drosophila
    • Warmke, J., Yamakawa, M., Molloy, J., Falkenthal, S., and Maughan, D. (1992). Myosin light chain-2 mutation affects flight, wing beat frequency, and indirect flight muscle contraction kinetics in Drosophila. J. Cell Biol. 119 (6), 1523-1539.
    • (1992) J. Cell Biol. , vol.119 , Issue.6 , pp. 1523-1539
    • Warmke, J.1    Yamakawa, M.2    Molloy, J.3    Falkenthal, S.4    Maughan, D.5
  • 67
    • 0029122824 scopus 로고
    • Detection of histidine-tagged fusion proteins by using a high-specific mouse monoclonal antihistidine tag antibody
    • Zentgraf, H., Frey, M., and Schwinn, S. (1995). Detection of histidine-tagged fusion proteins by using a high-specific mouse monoclonal antihistidine tag antibody. Nucleic Acids Res. 16, 3347-3348.
    • (1995) Nucleic Acids Res. , vol.16 , pp. 3347-3348
    • Zentgraf, H.1    Frey, M.2    Schwinn, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.