메뉴 건너뛰기




Volumn 266, Issue 2, 1997, Pages 317-330

A 29 residue region of the sarcomeric myosin rod is necessary for filament formation

Author keywords

Assembly; Myosin; Sarcomeric; Thick filament; Vertebrate

Indexed keywords

MYOSIN; MYOSIN HEAVY CHAIN;

EID: 0031581843     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0790     Document Type: Article
Times cited : (137)

References (69)
  • 1
    • 0025779542 scopus 로고
    • Expression in Escherichia coli of fragments of the coiled-coil rod domain of rabbit myosin: Influence of different regions of the molecule on aggregation and paracrystal formation
    • Atkinson S. J., Stewart M. Expression in Escherichia coli of fragments of the coiled-coil rod domain of rabbit myosin: influence of different regions of the molecule on aggregation and paracrystal formation. J. Cell Sci. 99:1991a;823-836.
    • (1991) J. Cell Sci , vol.99 , pp. 823-836
    • Atkinson, S.J.1    Stewart, M.2
  • 2
    • 0025989690 scopus 로고
    • Molecular basis of myosin assembly: Coiled-coil interactions and the role of charge periodicities
    • Atkinson S. J., Stewart M. Molecular basis of myosin assembly: coiled-coil interactions and the role of charge periodicities. J. Cell Sci. (Suppl.). 14:1991b;7-10.
    • (1991) J. Cell Sci. (Suppl.) , vol.14 , pp. 7-10
    • Atkinson, S.J.1    Stewart, M.2
  • 3
    • 0026772937 scopus 로고
    • Molecular interactions in myosin assembly. Role of the 28 residue charge repeat in the rod
    • Atkinson S. J., Stewart M. Molecular interactions in myosin assembly. Role of the 28 residue charge repeat in the rod. J. Mol. Biol. 226:1992;7-13.
    • (1992) J. Mol. Biol. , vol.226 , pp. 7-13
    • Atkinson, S.J.1    Stewart, M.2
  • 4
    • 0025155340 scopus 로고
    • Localization of myosin IC and myosin II in Acanthameoba castellanii by indirect immunofluoresence and immunogold electron microscopy
    • Baines I. C., Korn E. D. Localization of myosin IC and myosin II in Acanthameoba castellanii by indirect immunofluoresence and immunogold electron microscopy. J. Cell. Biol. 111:1990;1985-1904.
    • (1990) J. Cell. Biol. , vol.111 , pp. 1985-1904
    • Baines, I.C.1    Korn, E.D.2
  • 5
    • 0019887723 scopus 로고
    • The structure of spindle-shaped paracrystals of light meromyosin
    • Bennett P. M. The structure of spindle-shaped paracrystals of light meromyosin. J. Mol. Biol. 146:1981;201-221.
    • (1981) J. Mol. Biol. , vol.146 , pp. 201-221
    • Bennett, P.M.1
  • 6
    • 0022751327 scopus 로고
    • Alternative RNA splicing generates transcripts encoding a thorax-specific isoform of Drosophilia melanogaster myosin heavy chain
    • Bernstein S. I., Hansen C. J., Becker K. D., Wassenberg D. R. II, Roche E. S., Donady J. J., Emerson C. P. Jr. Alternative RNA splicing generates transcripts encoding a thorax-specific isoform of Drosophilia melanogaster myosin heavy chain. Mol. Cell. Biol. 6:1986;2511-2519.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2511-2519
    • Bernstein, S.I.1    Hansen, C.J.2    Becker, K.D.3    Wassenberg D.R. II4    Roche, E.S.5    Donady, J.J.6    Emerson C.P. Jr7
  • 7
    • 0027530939 scopus 로고
    • CDNA sequence of non-muscle myosin heavy chain gene of Xenopus laevis
    • Bhatia-Dey N., Adelstein R. S., Dawid I. B. cDNA sequence of non-muscle myosin heavy chain gene of Xenopus laevis. Proc. Natl Acad. Sci. USA. 90:1993;2856-2859.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2856-2859
    • Bhatia-Dey, N.1    Adelstein, R.S.2    Dawid, I.B.3
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 9
    • 0025272940 scopus 로고
    • Alpha-helical coiled coils and bundles: How to design an alpha-helical
    • Cohen C., Parry D. A. Alpha-helical coiled coils and bundles: how to design an alpha-helical. Proteins: Struct. Funct. Genet. 7:1990;1-5.
    • (1990) Proteins: Struct. Funct. Genet. , vol.7 , pp. 1-5
    • Cohen, C.1    Parry, D.A.2
  • 10
    • 0015222691 scopus 로고
    • Paramyosin and the filaments of Molluscan "catch" muscles I. Paramyosin: Structure and assembly
    • Cohen C., Szent-Gyorgyi A. G., Kendrick-Jones J. Paramyosin and the filaments of Molluscan "catch" muscles I. Paramyosin: structure and assembly. J. Mol. Biol. 56:1971;223-237.
    • (1971) J. Mol. Biol. , vol.56 , pp. 223-237
    • Cohen, C.1    Szent-Gyorgyi, A.G.2    Kendrick-Jones, J.3
  • 11
    • 0015518578 scopus 로고
    • A tropomyosin-like protein from human platelets
    • Cohen I., Cohen C. J. A tropomyosin-like protein from human platelets. J. Mol. Biol. 68:1972;383-387.
    • (1972) J. Mol. Biol. , vol.68 , pp. 383-387
    • Cohen, I.1    Cohen, C.J.2
  • 12
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick F. H. C. The packing of α-helices: simple coiled-coils. Acta Crystallog. 6:1953;689-697.
    • (1953) Acta Crystallog , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 13
    • 0022544420 scopus 로고
    • Solubility-determining domain of smooth muscle myosin rod
    • Cross R. A., Vandekerckhove J. Solubility-determining domain of smooth muscle myosin rod. FEBS Letters. 200:1986;355-360.
    • (1986) FEBS Letters , vol.200 , pp. 355-360
    • Cross, R.A.1    Vandekerckhove, J.2
  • 14
    • 0023578928 scopus 로고
    • Expression in Escherichia coli of a functional Dictyostelium myosin tail fragment
    • DeLozanne A., Berlot C. H., Leinwand L., Spudich J. A. Expression in Escherichia coli of a functional Dictyostelium myosin tail fragment. J. Cell. Biol. 105:1987;2999-3005.
    • (1987) J. Cell. Biol. , vol.105 , pp. 2999-3005
    • Delozanne, A.1    Berlot, C.H.2    Leinwand, L.3    Spudich, J.A.4
  • 15
    • 0021878067 scopus 로고
    • Sequence analysis of mutations that affect the synthesis, assembly and enzymatic activity of the unc-54 myosin heavy chain of Caenorhabditis elegans
    • Dibb N. J., Brown D. M., Karn J., Moerman D. G., Bolten S. L., Waterston R. H. Sequence analysis of mutations that affect the synthesis, assembly and enzymatic activity of the unc-54 myosin heavy chain of Caenorhabditis elegans. J. Mol. Biol. 183:1985;543-551.
    • (1985) J. Mol. Biol. , vol.183 , pp. 543-551
    • Dibb, N.J.1    Brown, D.M.2    Karn, J.3    Moerman, D.G.4    Bolten, S.L.5    Waterston, R.H.6
  • 16
    • 0024513698 scopus 로고
    • Molecular genetic characterization of a developmentally regulated human perinatal myosin heavy chain
    • Fegahli R., Leinwand L. A. Molecular genetic characterization of a developmentally regulated human perinatal myosin heavy chain. J. Cell. Biol. 108:1989;1791-1797.
    • (1989) J. Cell. Biol. , vol.108 , pp. 1791-1797
    • Fegahli, R.1    Leinwand, L.A.2
  • 17
    • 0025064805 scopus 로고
    • Expression of actin in Escherichia coli
    • Frankel S., Condeelis J., Leinwand L. Expression of actin in Escherichia coli. J. Biol. Chem. 265:1990;17980-17987.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17980-17987
    • Frankel, S.1    Condeelis, J.2    Leinwand, L.3
  • 18
    • 0028950213 scopus 로고
    • Structural analysis of myosin heavy chain kinase A from Dictyostelium. Evidence for a highly divergent protein kinase domain, an amino-terminal coiled-coil domain, and a domain homologous to the beta subunit of heterotrimeric G proteins
    • Futey L. M., Medley Q. G., Cote G. P., Egelhoff T. T. Structural analysis of myosin heavy chain kinase A from Dictyostelium. Evidence for a highly divergent protein kinase domain, an amino-terminal coiled-coil domain, and a domain homologous to the beta subunit of heterotrimeric G proteins. J. Biol. Chem. 270:1995;523-529.
    • (1995) J. Biol. Chem. , vol.270 , pp. 523-529
    • Futey, L.M.1    Medley, Q.G.2    Cote, G.P.3    Egelhoff, T.T.4
  • 19
    • 0023587876 scopus 로고
    • Complete nucleotide sequence and deduced polypeotide sequence of a non-muscle myosin heavy chain gene fromAcanthamoeba : Evidence of a hinge in the rodlike tail
    • Hammer J. A. III, Bowers B., Paterson B. M., Korn E. D. Complete nucleotide sequence and deduced polypeotide sequence of a non-muscle myosin heavy chain gene fromAcanthamoeba : evidence of a hinge in the rodlike tail. J. Cell Biol. 105:1987;913-925.
    • (1987) J. Cell Biol , vol.105 , pp. 913-925
    • Hammer J.A. III1    Bowers, B.2    Paterson, B.M.3    Korn, E.D.4
  • 20
    • 0023655442 scopus 로고
    • Altered actin and troponin binding of amino-terminal variants of chicken striated muscle alpha-tropomyosin expressed inEscherichia coli
    • Hitchcok-Degregori S. E., Heald R. W. Altered actin and troponin binding of amino-terminal variants of chicken striated muscle alpha-tropomyosin expressed inEscherichia coli. J. Biol. Chem. 262:1987;9730-9735.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9730-9735
    • Hitchcok-Degregori, S.E.1    Heald, R.W.2
  • 21
    • 0029911120 scopus 로고    scopus 로고
    • Hydrophobicity variations along the surface of the coiled-coil rod may mediate striated muscle myosin assembly inCaenorhabditis elegans
    • Hoppe O., Waterston O. Hydrophobicity variations along the surface of the coiled-coil rod may mediate striated muscle myosin assembly inCaenorhabditis elegans. J. Cell Biol. 135:1996;371-382.
    • (1996) J. Cell Biol. , vol.135 , pp. 371-382
    • Hoppe, O.1    Waterston, O.2
  • 22
    • 85012414651 scopus 로고
    • Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle
    • Huxley H. E. Electron microscope studies on the structure of natural and synthetic protein filaments from striated muscle. J. Mol. Biol. 7:1963;281-308.
    • (1963) J. Mol. Biol. , vol.7 , pp. 281-308
    • Huxley, H.E.1
  • 23
    • 85010249552 scopus 로고
    • The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor
    • Huxley H. E., Brown W. The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J. Mol. Biol. 30:1967;383-434.
    • (1967) J. Mol. Biol. , vol.30 , pp. 383-434
    • Huxley, H.E.1    Brown, W.2
  • 24
  • 25
    • 0024974671 scopus 로고
    • Paramyosin gene (unc-15) of Caenorhabditis elegans Molecular cloning, nucleotide sequence and models for thick filament structure
    • Kagawa H., Gengyro K., McLachlan A. D., Brenner S., Karn J. Paramyosin gene (unc-15) of Caenorhabditis elegans Molecular cloning, nucleotide sequence and models for thick filament structure. J. Mol. Biol. 207:1989;311-333.
    • (1989) J. Mol. Biol. , vol.207 , pp. 311-333
    • Kagawa, H.1    Gengyro, K.2    McLachlan, A.D.3    Brenner, S.4    Karn, J.5
  • 26
    • 0024383686 scopus 로고
    • Expression and DNA sequence analysis of a human embryonic skeletal muscle myosin heavy chain gene
    • Karsch-Mizrachi I., Travis M., Blau H., Leinwand L. Expression and DNA sequence analysis of a human embryonic skeletal muscle myosin heavy chain gene. Nucl. Acids Res. 17:1989;6167-6179.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 6167-6179
    • Karsch-Mizrachi, I.1    Travis, M.2    Blau, H.3    Leinwand, L.4
  • 27
    • 0028898501 scopus 로고
    • Effect of caldesmon on the assembly of smooth muscle myosin
    • Katayama E., Scott-Woo G., Ikebe M. Effect of caldesmon on the assembly of smooth muscle myosin. J. Biol. Chem. 270:1995;3919-3925.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3919-3925
    • Katayama, E.1    Scott-Woo, G.2    Ikebe, M.3
  • 29
    • 0025180601 scopus 로고
    • The complete sequence of the Drosophilia non-myscle myosin heavy-chain transcript: Conserved sequences in the myosin tail and differential splicing in the 5′ untranslated sequence
    • Ketchum A. S., Stewart C. T., Stewart M., Kiehart D. P. The complete sequence of the Drosophilia non-myscle myosin heavy-chain transcript: conserved sequences in the myosin tail and differential splicing in the 5′ untranslated sequence. Proc. Natl Acad. Sci. USA. 87:1990;6316-6320.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 6316-6320
    • Ketchum, A.S.1    Stewart, C.T.2    Stewart, M.3    Kiehart, D.P.4
  • 30
    • 0024426480 scopus 로고
    • Complete nucleotide sequence of full length cDNA for rat β cardiac myosin heavy chain
    • Kraft R., Bravo-Zehnder M., Taylor D. A., Leinwand L. A. Complete nucleotide sequence of full length cDNA for rat β cardiac myosin heavy chain. Nucl. Acids Res. 17:1989;7529-7530.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 7529-7530
    • Kraft, R.1    Bravo-Zehnder, M.2    Taylor, D.A.3    Leinwand, L.A.4
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0028007599 scopus 로고
    • Molecular genetic truncation analysis of filament assembly and phosphorylation domains of Dictyostelium myosin heavy chain
    • Lee R. J., Egelhoff T. T., Spudich J. A. Molecular genetic truncation analysis of filament assembly and phosphorylation domains of Dictyostelium myosin heavy chain. J. Cell Sci. 107:1994;2875-2886.
    • (1994) J. Cell Sci. , vol.107 , pp. 2875-2886
    • Lee, R.J.1    Egelhoff, T.T.2    Spudich, J.A.3
  • 33
    • 0027762693 scopus 로고
    • Cloning and in situ hybridization of type 2A and 2B rat skeletal muscle myosin tail region: Implications for filament assembly
    • Lieber R. L., Bodine S. C., Burkholder T. J., Pierotti D. J., Ryan A. F. Cloning and in situ hybridization of type 2A and 2B rat skeletal muscle myosin tail region: implications for filament assembly. Biochem. Biophys. Res. Commun. 197:1993;1312-1318.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1312-1318
    • Lieber, R.L.1    Bodine, S.C.2    Burkholder, T.J.3    Pierotti, D.J.4    Ryan, A.F.5
  • 34
    • 0014693726 scopus 로고
    • Substructure of the myosin molecule I. Subfragments of myosin by enzymic degradation
    • Lowey S., Slayter H. S., Weeds A. G., 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
  • 35
    • 0017639569 scopus 로고
    • An internal deletion mutant of a myosin heavy chain in Caenorhabditis elegans
    • MacLeod A. R., Waterston R. H., Brenner S. An internal deletion mutant of a myosin heavy chain in Caenorhabditis elegans. Proc. Natl Acad. Sci. USA. 74:1977;5336-5340.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 5336-5340
    • MacLeod, A.R.1    Waterston, R.H.2    Brenner, S.3
  • 36
    • 0024961625 scopus 로고
    • Expression of native rabbit light meromyosin in Escherichia coli: Observation of a powerful internal translation site
    • Maeda K., Sczakiel G., Hofmann W., Menetret J.-F., Wittinghofer A. Expression of native rabbit light meromyosin in Escherichia coli: observation of a powerful internal translation site. J. Mol. Biol. 205:1989;269-273.
    • (1989) J. Mol. Biol. , vol.205 , pp. 269-273
    • Maeda, K.1    Sczakiel, G.2    Hofmann, W.3    Menetret, J.-F.4    Wittinghofer, A.5
  • 38
    • 0025718558 scopus 로고
    • Complete sequence of human cardiac alpha-myosin heavy chaine gene and amino acid comparison to other myosins based on structural and functional differences
    • Matsuoka R., Beisel K. W., Furutani M., Arai S., Takao A. Complete sequence of human cardiac alpha-myosin heavy chaine gene and amino acid comparison to other myosins based on structural and functional differences. Am J. Med. Genet. 41:1991;537-547.
    • (1991) Am J. Med. Genet , vol.41 , pp. 537-547
    • Matsuoka, R.1    Beisel, K.W.2    Furutani, M.3    Arai, S.4    Takao, A.5
  • 39
    • 0019975166 scopus 로고
    • Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle
    • McLachlan A. D., Karn J. Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle. Nature. 299:1982;226-230.
    • (1982) Nature , vol.299 , pp. 226-230
    • McLachlan, A.D.1    Karn, J.2
  • 40
    • 0024440446 scopus 로고
    • Complete sequence of full-length cDNA for rat alpha cardiac myosin heavy chain
    • McNally E., Gianola K., Leinwand L. Complete 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.1    Gianola, K.2    Leinwand, L.3
  • 42
    • 0000199993 scopus 로고
    • Characterization of a mammalian smooth muscle myosin heavy chain cDNA clone and its expression on various smooth muscle types
    • Nagai R., Larson D. M., Periasam M. Characterization of a mammalian smooth muscle myosin heavy chain cDNA clone and its expression on various smooth muscle types. Proc. Natl Acad Sci. USA. 85:1988;1047-1051.
    • (1988) Proc. Natl Acad Sci. USA , vol.85 , pp. 1047-1051
    • Nagai, R.1    Larson, D.M.2    Periasam, M.3
  • 43
    • 0018572714 scopus 로고
    • DNA sequence of the gene for the outer membrane lipoprotein of E. coli: An extremely AT-rich promoter
    • Nakamura K., Inouye M. DNA sequence of the gene for the outer membrane lipoprotein of E. coli: an extremely AT-rich promoter. Cell. 18:1979;1109-1117.
    • (1979) Cell , vol.18 , pp. 1109-1117
    • Nakamura, K.1    Inouye, M.2
  • 44
    • 0020337391 scopus 로고
    • Construction of versatile expression cloning vehicles using the lipoprotein gene of Escherichia coli
    • Nakamura K., Inouye M. Construction of versatile expression cloning vehicles using the lipoprotein gene of Escherichia coli. EMBO J. 1:1982;771-775.
    • (1982) EMBO J. , vol.1 , pp. 771-775
    • Nakamura, K.1    Inouye, M.2
  • 46
    • 0025644199 scopus 로고
    • Nucleotide sequence of full length cDNa for a scallop striated muscle myosin heavy chain
    • Nyitray L., Goodwin E. B., Szent-Gyorgyi A. G. Nucleotide sequence of full length cDNa for a scallop striated muscle myosin heavy chain. Nucl. Acids Res. 18:1990;7158.
    • (1990) Nucl. Acids Res. , vol.18 , pp. 7158
    • Nyitray, L.1    Goodwin, E.B.2    Szent-Gyorgyi, A.G.3
  • 47
    • 0025138386 scopus 로고
    • Expression of Dictyostelium myosin tail segments in Escherichia coli: Domains requred for assembly and phosphorylation
    • O'Halloran T. J., Ravid S., Spudich J. A. Expression of Dictyostelium myosin tail segments in Escherichia coli: domains requred for assembly and phosphorylation. J. Cell. Biol. 110:1990;63-70.
    • (1990) J. Cell. Biol. , vol.110 , pp. 63-70
    • O'Halloran, T.J.1    Ravid, S.2    Spudich, J.A.3
  • 48
    • 0000969298 scopus 로고
    • Localization of two phosphorylation sites adjacent to a region important for polymerization on the tail ofDictyostelium myosin
    • Pagh K., Maruta H., Claviez M., Gerisch G. Localization of two phosphorylation sites adjacent to a region important for polymerization on the tail ofDictyostelium myosin. EMBO J. 3:1984;3271-3278.
    • (1984) EMBO J. , vol.3 , pp. 3271-3278
    • Pagh, K.1    Maruta, H.2    Claviez, M.3    Gerisch, G.4
  • 49
    • 0019873745 scopus 로고
    • Structure of rabbit skeletal myosin. analysis of the amino acid sequences of two fragments from the rod region
    • Parry D. A. Structure of rabbit skeletal myosin. analysis of the amino acid sequences of two fragments from the rod region. J. Mol. Biol. 153:1981;459-464.
    • (1981) J. Mol. Biol. , vol.153 , pp. 459-464
    • Parry, D.A.1
  • 50
    • 0000237236 scopus 로고
    • The structure of light-meromyosin: An electron microscopic study
    • Philpott D. E., Szent-Gyorgyi A. G. The structure of light-meromyosin: an electron microscopic study. Biochim Biophys. Acta. 15:1954;165-173.
    • (1954) Biochim Biophys. Acta , vol.15 , pp. 165-173
    • Philpott, D.E.1    Szent-Gyorgyi, A.G.2
  • 51
    • 0024240399 scopus 로고
    • Unexpected translation initiation within the coding region of eukaryotic genes expressed in Escherichia coli
    • Preibisch G., Hideki I., Tripier D., Leineweber M. Unexpected translation initiation within the coding region of eukaryotic genes expressed in Escherichia coli. Gene. 72:1988;179-186.
    • (1988) Gene , vol.72 , pp. 179-186
    • Preibisch, G.1    Hideki, I.2    Tripier, D.3    Leineweber, M.4
  • 52
    • 0022571043 scopus 로고
    • Characterization of diverse forms of myosin heavy chain expressed in adult human skeletal muscle
    • Saez L., Leinwand L. Characterization of diverse forms of myosin heavy chain expressed in adult human skeletal muscle. Nucl. Acids Res. 14:1986;2951-2969.
    • (1986) Nucl. Acids Res. , vol.14 , pp. 2951-2969
    • Saez, L.1    Leinwand, L.2
  • 53
    • 0025174075 scopus 로고
    • Human non-muscle myosin heavy chain mRNA: Generation of diversity through alternative polyadenylation
    • Saez C. G., Myers J. C., Shows T. B. Jr, Leinwand L. A. Human non-muscle myosin heavy chain mRNA: generation of diversity through alternative polyadenylation. Proc. Natl Acad. Sci. USA. 87:1990;1164-1168.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1164-1168
    • Saez, C.G.1    Myers, J.C.2    Shows T.B. Jr3    Leinwand, L.A.4
  • 55
    • 0024747004 scopus 로고
    • The mechanism of assembly of Acanthamoeba myosin-II minifilaments: Minifilaments assemble by three successive dimerization steps
    • Sinard J. H., Stafford W. F., Pollard T. D. The mechanism of assembly of Acanthamoeba myosin-II minifilaments: minifilaments assemble by three successive dimerization steps. J. Cell. Biol. 107:1989;1537-1547.
    • (1989) J. Cell. Biol. , vol.107 , pp. 1537-1547
    • Sinard, J.H.1    Stafford, W.F.2    Pollard, T.D.3
  • 56
    • 0025642376 scopus 로고
    • Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions
    • Sinard J. H., Rimm D. L., Pollard T. D. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions. J. Cell. Biol. 111:1990;2417-2426.
    • (1990) J. Cell. Biol. , vol.111 , pp. 2417-2426
    • Sinard, J.H.1    Rimm, D.L.2    Pollard, T.D.3
  • 58
    • 0022516684 scopus 로고
    • Complete nucleotide and encoded amino acid sequence of a mammalian myosin heavy chain gene. Evidence against intron-dependent evolution of the rod
    • Strehler E. E., Strehler-Page M. A., Perriard J. C., Periasamy M., Nadal-Ginard B. Complete nucleotide and encoded amino acid sequence of a mammalian myosin heavy chain gene. Evidence against intron-dependent evolution of the rod. J. Mol. Biol. 190:1986;291-317.
    • (1986) J. Mol. Biol. , vol.190 , pp. 291-317
    • Strehler, E.E.1    Strehler-Page, M.A.2    Perriard, J.C.3    Periasamy, M.4    Nadal-Ginard, B.5
  • 60
    • 0018276960 scopus 로고
    • Isolation and physico-chemical properties of a high molecular weight subfragment-2 of myosin
    • Sutoh K., Sutoh K., Karr T., Harrington W. F. Isolation and physico-chemical properties of a high molecular weight subfragment-2 of myosin. J. Mol. Biol. 126:1978;1-22.
    • (1978) J. Mol. Biol. , vol.126 , pp. 1-22
    • Sutoh, K.1    Sutoh, K.2    Karr, T.3    Harrington, W.F.4
  • 61
    • 0000668251 scopus 로고
    • Meromyosins, the subunits of myosin
    • Szent-Gyorgyi A. G. Meromyosins, the subunits of myosin. Arch. Biochem. Biophys. 42:1953;305-320.
    • (1953) Arch. Biochem. Biophys. , vol.42 , pp. 305-320
    • Szent-Gyorgyi, A.G.1
  • 62
    • 84986424120 scopus 로고
    • Light meromyosin fraction I: A helical molecule from myosin
    • Szent-Gyorgyi A. G., Cohen C., Philpott D. E. Light meromyosin fraction I: a helical molecule from myosin. J. Mol. Biol. 2:1960;133-142.
    • (1960) J. Mol. Biol. , vol.2 , pp. 133-142
    • Szent-Gyorgyi, A.G.1    Cohen, C.2    Philpott, D.E.3
  • 63
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 64
    • 0023604845 scopus 로고
    • Assembly of smooth muscle myosin minifilaments: Effects of phosphorylation and nucleotide binding
    • Trybus K. M., Lowey S. Assembly of smooth muscle myosin minifilaments: effects of phosphorylation and nucleotide binding. J. Cell Biol. 105:1987;3007-3019.
    • (1987) J. Cell Biol. , vol.105 , pp. 3007-3019
    • Trybus, K.M.1    Lowey, S.2
  • 65
    • 0018852410 scopus 로고
    • Rotary shadowing of extended molecules dried from glycerol
    • Tyler J. M., Branton D. Rotary shadowing of extended molecules dried from glycerol. J. Ultrastruc. Res. 71:1980;95-102.
    • (1980) J. Ultrastruc. Res. , vol.71 , pp. 95-102
    • Tyler, J.M.1    Branton, D.2
  • 66
    • 0027436343 scopus 로고
    • Sarcomeric myosin heavy chain expressed in non-muscle cells forms thick filaments in the presence of substoichiometric amounts of light chains
    • Vikstrom K. L., Rovner A. S., Saez C. G., Bravo-Zehnder M., Straceski A. J., Leinwand L. Sarcomeric myosin heavy chain expressed in non-muscle cells forms thick filaments in the presence of substoichiometric amounts of light chains. Cell Motil. Cytoskel. 26:1993;192-204.
    • (1993) Cell Motil. Cytoskel , vol.26 , pp. 192-204
    • Vikstrom, K.L.1    Rovner, A.S.2    Saez, C.G.3    Bravo-Zehnder, M.4    Straceski, A.J.5    Leinwand, L.6
  • 67
    • 0025093899 scopus 로고
    • Identification of a region in segment 1 of gelsolin critical for actin binding
    • Way M., Pope B., Gooch J., Hawkins M., Weeds A. G. Identification of a region in segment 1 of gelsolin critical for actin binding. EMBO J. 9:1990;4103-4109.
    • (1990) EMBO J. , vol.9 , pp. 4103-4109
    • Way, M.1    Pope, B.2    Gooch, J.3    Hawkins, M.4    Weeds, A.G.5
  • 68
    • 0020774275 scopus 로고
    • The genes sup-7 X and sup-5 III of C. elegans suppress amber nonsense mutations via altered transfer RNA
    • Wills N., Gesteland R. F., Karn J., Barnett L. D., Bolten S. L., Waterston R. The genes sup-7 X and sup-5 III of C. elegans suppress amber nonsense mutations via altered transfer RNA. Cell. 33:1983;575-583.
    • (1983) Cell , vol.33 , pp. 575-583
    • Wills, N.1    Gesteland, R.F.2    Karn, J.3    Barnett, L.D.4    Bolten, S.L.5    Waterston, R.6
  • 69
    • 0023661175 scopus 로고
    • Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence. Implications on topography and function of myosin
    • Yanagisawa M., Hamada Y., Katsuragawa Y., Imamura M., Mikawa T., Masaki T. Complete primary structure of vertebrate smooth muscle myosin heavy chain deduced from its complementary DNA sequence. Implications on topography and function of myosin. J. Mol. Biol. 198:1987;143-157.
    • (1987) J. Mol. Biol. , vol.198 , pp. 143-157
    • Yanagisawa, M.1    Hamada, Y.2    Katsuragawa, Y.3    Imamura, M.4    Mikawa, T.5    Masaki, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.