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Volumn 260, Issue 3, 1999, Pages 672-683

Differences in the ionic interaction of actin with the motor domains of nonmuscle and muscle myosin II

Author keywords

Actin; Actomyosin interface; Adenosinetriphosphatase; Cross linking; Mutagenesis; Myosin; Proteolysis

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; ALPHA ACTIN; CYANAMIDE; F ACTIN; G ACTIN; MYOSIN;

EID: 0033559611     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00172.x     Document Type: Article
Times cited : (18)

References (67)
  • 1
    • 0011364439 scopus 로고
    • Structural studies of myosin-nucleotide complexes: A revised model for the molecular basis of muscle contraction
    • Fisher, A.J., Smith, C.A., Thoden, J., Smith, R., Sutoh, K., Holden, H.M. & Rayment, I. (1995). Structural studies of myosin-nucleotide complexes: a revised model for the molecular basis of muscle contraction. Biophys. J. 68, 19S-28S.
    • (1995) Biophys. J. , vol.68
    • Fisher, A.J.1    Smith, C.A.2    Thoden, J.3    Smith, R.4    Sutoh, K.5    Holden, H.M.6    Rayment, I.7
  • 2
    • 0019317330 scopus 로고
    • Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles
    • Marston, S.B. & Taylor, E.W. (1980) Comparison of the myosin and actomyosin ATPase mechanisms of the four types of vertebrate muscles. J. Mol. Biol. 139, 573-600.
    • (1980) J. Mol. Biol. , vol.139 , pp. 573-600
    • Marston, S.B.1    Taylor, E.W.2
  • 3
    • 0027267667 scopus 로고
    • Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum
    • Ritchie, M.D., Geeves, M., Woodward, S.K.A. & Manstein, D.J. (1993) Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum. Proc. Natl Acad. Sci. USA 90, 8619-8623.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8619-8623
    • Ritchie, M.D.1    Geeves, M.2    Woodward, S.K.A.3    Manstein, D.J.4
  • 4
    • 0029915892 scopus 로고    scopus 로고
    • Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase
    • Ostap, E.M. & Pollard, T.D. (1996) Biochemical kinetic characterization of the Acanthamoeba myosin-I ATPase. J. Cell Biol. 132, 1053-1060.
    • (1996) J. Cell Biol. , vol.132 , pp. 1053-1060
    • Ostap, E.M.1    Pollard, T.D.2
  • 9
    • 0030832286 scopus 로고    scopus 로고
    • The structure of the acto-myosin subfragment 1 complex: Results of searches using data from electron microscopy and X-ray crystallography
    • Mendelson, R. & Morris, E.P. (1997) The structure of the acto-myosin subfragment 1 complex: results of searches using data from electron microscopy and X-ray crystallography, Proc. Natl Acad. Sci. USA 94, 8533-8538.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 8533-8538
    • Mendelson, R.1    Morris, E.P.2
  • 10
    • 0342293921 scopus 로고
    • Modifying preselected sites on proteins: The stretch of residues 633-642 of the myosin heavy chain is part of the actin-binding site
    • Chaussepied, P. & Morales, F. (1988) Modifying preselected sites on proteins: The stretch of residues 633-642 of the myosin heavy chain is part of the actin-binding site. Proc. Natl Acad. Sci. USA 85, 7471-7475.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 7471-7475
    • Chaussepied, P.1    Morales, F.2
  • 11
    • 0024461342 scopus 로고
    • Interaction between stretch of residues 633-642 (actin binding site) and nucleotide binding site on skeletal myosin subfragment 1 heavy chain
    • Chaussepied, P. (1989) Interaction between stretch of residues 633-642 (actin binding site) and nucleotide binding site on skeletal myosin subfragment 1 heavy chain. Biochemistry 28, 9123-9128.
    • (1989) Biochemistry , vol.28 , pp. 9123-9128
    • Chaussepied, P.1
  • 12
    • 0024377140 scopus 로고
    • ATP-induced structural change in myosin subfragment-1 revealed by the location of protease cleavage sites on the primary structure
    • Yamamoto, K. (1989) ATP-induced structural change in myosin subfragment-1 revealed by the location of protease cleavage sites on the primary structure. J. Mol. Biol. 209, 703-709.
    • (1989) J. Mol. Biol. , vol.209 , pp. 703-709
    • Yamamoto, K.1
  • 13
    • 0029935220 scopus 로고    scopus 로고
    • The role of surface loops (residues 204-216 and 627-646) in the motor function of the myosin head
    • Bobkov, A.A., Bobkova, E.A., Lin, S.H. & Reisler, E. (1996) The role of surface loops (residues 204-216 and 627-646) in the motor function of the myosin head. Proc. Natl Acad. Sci. USA 93, 2285-2289.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2285-2289
    • Bobkov, A.A.1    Bobkova, E.A.2    Lin, S.H.3    Reisler, E.4
  • 14
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin
    • Uyeda, T.Q.P., Ruppel, K.M. & Spudich, J.A. (1994) Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin. Nature 368, 567-569.
    • (1994) Nature , vol.368 , pp. 567-569
    • Uyeda, T.Q.P.1    Ruppel, K.M.2    Spudich, J.A.3
  • 15
    • 0029561337 scopus 로고
    • Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin
    • Rovner, A.S., Freyzon, Y., & Trybus, K.M. (1995) Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin, J. Biol. Chem. 270, 30260-30263.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30260-30263
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 16
    • 0032485859 scopus 로고    scopus 로고
    • Modulation of actin affinity and actomyosin ATPase by charge changes in the myosin motor domain
    • Furch, M., Geeves, M.A. & Manstein, D.J. (1998) Modulation of actin affinity and actomyosin ATPase by charge changes inthe myosin motor domain. Biochemistry 37, 6317-6326.
    • (1998) Biochemistry , vol.37 , pp. 6317-6326
    • Furch, M.1    Geeves, M.A.2    Manstein, D.J.3
  • 17
    • 0032499649 scopus 로고    scopus 로고
    • Effect of ATP analogues on the actin-myosin interface
    • Van Dijk, J., Fernandez, C. & Chaussepied, P. (1998) Effect of ATP analogues on the actin-myosin interface. Biochemistry 37, 8385-8394.
    • (1998) Biochemistry , vol.37 , pp. 8385-8394
    • Van Dijk, J.1    Fernandez, C.2    Chaussepied, P.3
  • 18
    • 0031028517 scopus 로고    scopus 로고
    • Dictyostelium discoideum myosin II: Characterization of functional myosin motor fragments
    • Kurzawa, S.E., Manstein, D.J. & Geeves, M.A. (1997) Dictyostelium discoideum myosin II: characterization of functional myosin motor fragments. Biochemistry 36, 317-323.
    • (1997) Biochemistry , vol.36 , pp. 317-323
    • Kurzawa, S.E.1    Manstein, D.J.2    Geeves, M.A.3
  • 20
    • 0018419696 scopus 로고
    • Determination of the association of myosin subfragment 1 with actin in the presence of ATE
    • Wagner, P.D. & Weeds, A.G. (1979) Determination of the association of myosin subfragment 1 with actin in the presence of ATE Biochemistry 18, 2260-2266.
    • (1979) Biochemistry , vol.18 , pp. 2260-2266
    • Wagner, P.D.1    Weeds, A.G.2
  • 21
    • 0027305413 scopus 로고
    • Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay
    • Lowey, S., Waller, G.S., Trybus, K. & M. (1993) Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay, J. Biol. Chem. 268, 20414-20418.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20414-20418
    • Lowey, S.1    Waller, G.S.2    Trybus, K.M.3
  • 22
    • 0027426228 scopus 로고
    • Skeletal muscle myosin light chains are essential for physiological speeds of shortening
    • Lowey, S., Waller, G.S. & Trybus, K.M. (1993) Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature 365, 454-456.
    • (1993) Nature , vol.365 , pp. 454-456
    • Lowey, S.1    Waller, G.S.2    Trybus, K.M.3
  • 23
    • 0024843553 scopus 로고
    • Isolation and characterization of the G-actin-myosin head complex
    • Chaussepied, P. & Kasprzak, A.A. (1989) Isolation and characterization of the G-actin-myosin head complex. Nature 342, 950-953.
    • (1989) Nature , vol.342 , pp. 950-953
    • Chaussepied, P.1    Kasprzak, A.A.2
  • 24
    • 0027501844 scopus 로고
    • Interaction and polymerization of the G-actin-myosin head complex: Effect of DNase I
    • Lheureux, K., Forné T. & Chaussepied, P. (1993) Interaction and polymerization of the G-actin-myosin head complex: effect of DNase I. Biochemistry 32, 10005-10014.
    • (1993) Biochemistry , vol.32 , pp. 10005-10014
    • Lheureux, K.1    Forné, T.2    Chaussepied, P.3
  • 25
    • 0015924821 scopus 로고
    • A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization
    • Offer, G., Moos, C. & Starr, R. (1973) A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization. J. Mol. Biol. 74, 653-676.
    • (1973) J. Mol. Biol. , vol.74 , pp. 653-676
    • Offer, G.1    Moos, C.2    Starr, R.3
  • 26
    • 0016752124 scopus 로고
    • Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin
    • Weeds, A.G. & Taylor, R.S. (1975) Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin. Nature 257, 54-56.
    • (1975) Nature , vol.257 , pp. 54-56
    • Weeds, A.G.1    Taylor, R.S.2
  • 27
    • 0016168984 scopus 로고
    • Troponin-tropomyosin complex. Column chromatographic separation and activity of the three active troponin components with and without tropomyosin present
    • Eisenberg, E. & Kielley, W.W. (1974) Troponin-tropomyosin complex. Column chromatographic separation and activity of the three active troponin components with and without tropomyosin present. J. Biol. Chem. 249, 4742-4748.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4742-4748
    • Eisenberg, E.1    Kielley, W.W.2
  • 28
    • 0029055358 scopus 로고
    • Overexpression of myosin motor domain in Dictyostelium: Screening of transformants and purification of the affinity tagged protein
    • Manstein, D.J. & Hunt, D.M. (1995) Overexpression of myosin motor domain in Dictyostelium: screening of transformants and purification of the affinity tagged protein. J. Muscle Res. Cell Motil. 16, 325-332.
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 325-332
    • Manstein, D.J.1    Hunt, D.M.2
  • 29
    • 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.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal, Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 0020023988 scopus 로고
    • Myosin active-site trapping with vanadate ion
    • Goodno, C.C. (1982) Myosin active-site trapping with vanadate ion. Methods Enzymol. 85, 116-123.
    • (1982) Methods Enzymol. , vol.85 , pp. 116-123
    • Goodno, C.C.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
  • 32
    • 0027241883 scopus 로고
    • Photochemical cross-linking of the skeletal myosin head heavy chain to actin subdomain-1 at Arg95 and Arg28
    • Bonafé, N., Chaussepied, P., Capony, J.P., Derancourt, J. & Kassab, R. (1993) Photochemical cross-linking of the skeletal myosin head heavy chain to actin subdomain-1 at Arg95 and Arg28. Eur. J. Biochem. 213, 1243-1254.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1243-1254
    • Bonafé, N.1    Chaussepied, P.2    Capony, J.P.3    Derancourt, J.4    Kassab, R.5
  • 33
    • 0015875525 scopus 로고
    • Fluorimetric studies on the influence of metal ions and chelators on the interaction between myosin and ATP
    • Mandelkow, E.M. & Mandelkow, E. (1973) Fluorimetric studies on the influence of metal ions and chelators on the interaction between myosin and ATP. FEBS Lett. 33, 161-166.
    • (1973) FEBS Lett. , vol.33 , pp. 161-166
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 34
    • 0029089026 scopus 로고
    • Comparative studies of the monomeric and filamentous actin-myosin head complexes
    • Lheureux, K. & Chaussepied, P. (1995) Comparative studies of the monomeric and filamentous actin-myosin head complexes. Biochemistry 34, 11435-11444.
    • (1995) Biochemistry , vol.34 , pp. 11435-11444
    • Lheureux, K.1    Chaussepied, P.2
  • 35
    • 0019879677 scopus 로고
    • Proteolytic approach to structure and function of actin recognition site in myosin heads
    • Mornet, D., Bertrand, R., Pantel, P., Audemard, E. & Kassab, R. (1981) Proteolytic approach to structure and function of actin recognition site in myosin heads. Biochemistry 20, 2110-2120.
    • (1981) Biochemistry , vol.20 , pp. 2110-2120
    • Mornet, D.1    Bertrand, R.2    Pantel, P.3    Audemard, E.4    Kassab, R.5
  • 36
    • 0024326914 scopus 로고
    • Change in the actin-myosin subfragment 1 interaction during actin polymerization
    • Chaussepied, P. & Kasprzak, A.A. (1989) Change in the actin-myosin subfragment 1 interaction during actin polymerization. J. Biol. Chem. 264, 20752-20759.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20752-20759
    • Chaussepied, P.1    Kasprzak, A.A.2
  • 37
    • 0027525483 scopus 로고
    • Myosin subfragment 1 inhibits dissociation of nucleotide and calcium from G-actin
    • Kasprzak, A.A. (1993) Myosin subfragment 1 inhibits dissociation of nucleotide and calcium from G-actin. J. Biol. Chem. 268, 13261-13266.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13261-13266
    • Kasprzak, A.A.1
  • 38
    • 0020314178 scopus 로고
    • Effects of tryptic digestion on myosin subfragment 1 and its actin-activated adenosinetriphosphatase
    • Botts, J., Muhlrad, A., Takashi, R. & Morales, M.F. (1982) Effects of tryptic digestion on myosin subfragment 1 and its actin-activated adenosinetriphosphatase. Biochemistry 21, 6903-6905.
    • (1982) Biochemistry , vol.21 , pp. 6903-6905
    • Botts, J.1    Muhlrad, A.2    Takashi, R.3    Morales, M.F.4
  • 40
    • 0020382825 scopus 로고
    • Identification of myosin-binding sites on the actin sequence
    • Sutoh, K. (1982) Identification of myosin-binding sites on the actin sequence. Biochemistry 21, 3654-3661.
    • (1982) Biochemistry , vol.21 , pp. 3654-3661
    • Sutoh, K.1
  • 41
    • 0027718079 scopus 로고
    • Structure of the 265-kilodalton complex formed upon EDC cross-linking of subfragment 1 to F-actin
    • Andreeva, A.L., Andreev, O.A. & Borejdo, J. (1993) Structure of the 265-kilodalton complex formed upon EDC cross-linking of subfragment 1 to F-actin. Biochemistry 32, 13956-13960.
    • (1993) Biochemistry , vol.32 , pp. 13956-13960
    • Andreeva, A.L.1    Andreev, O.A.2    Borejdo, J.3
  • 42
    • 0028921163 scopus 로고
    • A single myosin head can be cross-linked to the N termini of two adjacent actin monomers
    • Bonafé, N. & Chaussepied, P. (1995) A single myosin head can be cross-linked to the N termini of two adjacent actin monomers. Biophys. J. 68, 35-43.
    • (1995) Biophys. J. , vol.68 , pp. 35-43
    • Bonafé, N.1    Chaussepied, P.2
  • 43
    • 0016614461 scopus 로고
    • The fragmentation of actin by thrombin. Isolation and characterization of the split products
    • Muszbek, L., Gladner, J.A. & Laki, K. (1975) The fragmentation of actin by thrombin. Isolation and characterization of the split products. Arch. Biochem. Biophys. 167, 99-103.
    • (1975) Arch. Biochem. Biophys. , vol.167 , pp. 99-103
    • Muszbek, L.1    Gladner, J.A.2    Laki, K.3
  • 44
    • 0024344637 scopus 로고
    • Functional characterization of skeletal F-actin labeled on the NH2-terminal segment of residues 1-28
    • Bertrand, R., Chaussepied, P., Audemard, E. & Kassab, R. (1989) Functional characterization of skeletal F-actin labeled on the NH2-terminal segment of residues 1-28. Eur. J. Biochem. 181, 747-754.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 747-754
    • Bertrand, R.1    Chaussepied, P.2    Audemard, E.3    Kassab, R.4
  • 45
    • 0023729137 scopus 로고
    • Cross-linking of the skeletal myosin subfragment 1 heavy chain to the N-terminal actin segment of residues 40-113
    • Bertrand, R., Chaussepied, P., Kassab, R., Boyer, M., Roustan, C. & Benyamin, Y. (1988) Cross-linking of the skeletal myosin subfragment 1 heavy chain to the N-terminal actin segment of residues 40-113. Biochemistry 27, 5728-5736.
    • (1988) Biochemistry , vol.27 , pp. 5728-5736
    • Bertrand, R.1    Chaussepied, P.2    Kassab, R.3    Boyer, M.4    Roustan, C.5    Benyamin, Y.6
  • 46
    • 84890979204 scopus 로고
    • Carboxyl group reactivity in action
    • (Walsh, J.E., ed.) The Human Press, Totowa, NJ, USA
    • Elzinga, M. (1987) Carboxyl group reactivity in action. In Methods in Protein Science Analysis. (Walsh, J.E., ed.), pp. 615-623. The Human Press, Totowa, NJ, USA.
    • (1987) Methods in Protein Science Analysis , pp. 615-623
    • Elzinga, M.1
  • 47
    • 0025774077 scopus 로고
    • Interactions of myosin subfragment 1 isozymes with G-actin
    • Chen, T. & Reisler, E. (1991) Interactions of myosin subfragment 1 isozymes with G-actin. Biochemistry 30, 4546-4552.
    • (1991) Biochemistry , vol.30 , pp. 4546-4552
    • Chen, T.1    Reisler, E.2
  • 48
    • 0023875598 scopus 로고
    • Polymerization of G-actin by myosin subfragment 1
    • Miller, L., Phillips, M. & Reisler, E. (1988) Polymerization of G-actin by myosin subfragment 1. J. Biol. Chem. 263, 1996-2002.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1996-2002
    • Miller, L.1    Phillips, M.2    Reisler, E.3
  • 50
    • 0021097746 scopus 로고
    • Structural and actin-binding properties of the trypsin-produced HMM and S1 from gizzard smooth muscle myosin
    • Marianne-Pépin, T., Mornet, D., Audemard, E. & Kassab, R. (1983) Structural and actin-binding properties of the trypsin-produced HMM and S1 from gizzard smooth muscle myosin. FEBS Lett. 159, 211-216.
    • (1983) FEBS Lett. , vol.159 , pp. 211-216
    • Marianne-Pépin, T.1    Mornet, D.2    Audemard, E.3    Kassab, R.4
  • 51
    • 0023645957 scopus 로고
    • Comparative structure of the protease-sensitive regions of the subfragment-1 heavy chain from smooth and skeletal myosins
    • Bonet, A., Mornet, D., Audemard, E., Derancourt, J., Bertrand, R. & Kassab, R. (1987) Comparative structure of the protease-sensitive regions of the subfragment-1 heavy chain from smooth and skeletal myosins. J. Biol. Chem. 262, 16524-16530.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16524-16530
    • Bonet, A.1    Mornet, D.2    Audemard, E.3    Derancourt, J.4    Bertrand, R.5    Kassab, R.6
  • 52
    • 0021763149 scopus 로고
    • Comparison of the tryptic digestion pattern of subfragments 1 from V1 and V3 rat cardiac isomyosins
    • Lompré, A.M., Han, K.K., Bouveret, P., Richard, C. & Schwartz, K. (1984) Comparison of the tryptic digestion pattern of subfragments 1 from V1 and V3 rat cardiac isomyosins. Eur. J. Biochem. 139, 459-465.
    • (1984) Eur. J. Biochem. , vol.139 , pp. 459-465
    • Lompré, A.M.1    Han, K.K.2    Bouveret, P.3    Richard, C.4    Schwartz, K.5
  • 53
    • 0021339136 scopus 로고
    • Proteolysis and the domain organization of myosin subfragment 1
    • Mornet, D., Ue, K. & Morales, M.F. (1984) Proteolysis and the domain organization of myosin subfragment 1. Proc. Natl Acad. Sci. USA 81, 736-739.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 736-739
    • Mornet, D.1    Ue, K.2    Morales, M.F.3
  • 54
    • 0021154996 scopus 로고
    • Effects of limited tryptic cleavage on the physical and enzymatic properties of myosin II from Acanthamoeba castellanii
    • Kuznicki, J., Atkinson, M.A. & Korn, E.D. (1984) Effects of limited tryptic cleavage on the physical and enzymatic properties of myosin II from Acanthamoeba castellanii. J. Biol. Chem. 259, 9308-9313.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9308-9313
    • Kuznicki, J.1    Atkinson, M.A.2    Korn, E.D.3
  • 55
    • 0022544577 scopus 로고
    • Proteolytic fragmentation of brain myosin and localisation of the heavy-chain phosphorylation site
    • Barylko, B., Tooth, P. & Kendrick-Jones, J. (1986) Proteolytic fragmentation of brain myosin and localisation of the heavy-chain phosphorylation site. Eur. J. Biochem. 158, 271-282.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 271-282
    • Barylko, B.1    Tooth, P.2    Kendrick-Jones, J.3
  • 56
    • 0032510769 scopus 로고    scopus 로고
    • Dictyostelium myosin 25-50K loop substitutions specifically affect ADP release rates
    • Murphy, C.T. & Spudich, J.A. (1998) Dictyostelium myosin 25-50K loop substitutions specifically affect ADP release rates. Biochemistry 37, 6738-6744.
    • (1998) Biochemistry , vol.37 , pp. 6738-6744
    • Murphy, C.T.1    Spudich, J.A.2
  • 57
    • 0021095627 scopus 로고
    • Selective cleavage of the connector segments within the myosin-S1 heavy chain by staphylococcal protease
    • Chaussepied, P., Bertrand, R., Audemard, E., Pantel, P., Derancourt, J. & Kassab, R. (1983) Selective cleavage of the connector segments within the myosin-S1 heavy chain by staphylococcal protease. FEBS Lett 161, 84-88.
    • (1983) FEBS Lett , vol.161 , pp. 84-88
    • Chaussepied, P.1    Bertrand, R.2    Audemard, E.3    Pantel, P.4    Derancourt, J.5    Kassab, R.6
  • 58
    • 0024970683 scopus 로고
    • The effect of actin and phosphorylation on the tryptic cleavage pattern of Acanthamoeba myosin IA
    • Brzeska, H., Lynch, T.J. & Korn, E.D. (1989) The effect of actin and phosphorylation on the tryptic cleavage pattern of Acanthamoeba myosin IA. J. Biol. Chem. 264, 10243-10250.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10243-10250
    • Brzeska, H.1    Lynch, T.J.2    Korn, E.D.3
  • 59
    • 0021181995 scopus 로고
    • Nucleotide-induced changes in the proteolytically sensitive regions of myosin subfragment 1
    • Applegate, D. & Reisler, E. (1984) Nucleotide-induced changes in the proteolytically sensitive regions of myosin subfragment 1. Biochemistry 23, 4779-4784.
    • (1984) Biochemistry , vol.23 , pp. 4779-4784
    • Applegate, D.1    Reisler, E.2
  • 60
    • 0021873380 scopus 로고
    • Molecular movements promoted by metal nucleotides in the heavy-chain regions of myosin heads from skeletal muscle
    • Mornet, D., Pantel, P., Audemard, E., Derancourt, J. & Kassab, R. (1985) Molecular movements promoted by metal nucleotides in the heavy-chain regions of myosin heads from skeletal muscle. J. Mol. Biol. 183, 479-489.
    • (1985) J. Mol. Biol. , vol.183 , pp. 479-489
    • Mornet, D.1    Pantel, P.2    Audemard, E.3    Derancourt, J.4    Kassab, R.5
  • 61
    • 0023217207 scopus 로고
    • Conformational transitions in the myosin head induced by temperature, nucleotide and actin. Studies on subfragment-1 of myosins from rabbit and frog fast skeletal muscle with a limited proteolysis method
    • Redowicz, M.J., Szilagyi, L. & Strzelecka-Golaszewska, H. (1987) Conformational transitions in the myosin head induced by temperature, nucleotide and actin. Studies on subfragment-1 of myosins from rabbit and frog fast skeletal muscle with a limited proteolysis method. Eur. J. Biochem. 165, 353-362.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 353-362
    • Redowicz, M.J.1    Szilagyi, L.2    Strzelecka-Golaszewska, H.3
  • 62
    • 0021865362 scopus 로고
    • Interaction of the heavy chain of gizzard myosin heads with skeletal F-actin
    • Marianne-Pépin, T., Mornet, D., Bertrand, R., Labbé, J.P. & Kassab, R. (1985) Interaction of the heavy chain of gizzard myosin heads with skeletal F-actin. Biochemistry 24, 3024-3029.
    • (1985) Biochemistry , vol.24 , pp. 3024-3029
    • Marianne-Pépin, T.1    Mornet, D.2    Bertrand, R.3    Labbé, J.P.4    Kassab, R.5
  • 63
    • 0023758682 scopus 로고
    • Interaction of the heavy chain of scallop myosin heads with skeletal F-actin
    • Labbé, J.P., Chaussepied, P., Derancourt, J. & Kassab, R. (1988) Interaction of the heavy chain of scallop myosin heads with skeletal F-actin. Biochemistry 27, 5914-5922.
    • (1988) Biochemistry , vol.27 , pp. 5914-5922
    • Labbé, J.P.1    Chaussepied, P.2    Derancourt, J.3    Kassab, R.4
  • 64
    • 0020314826 scopus 로고
    • Cross-linking of F-actin to skeletal muscle myosin subfragment 1 with Bis (imido esters): Further evidence for the interaction of myosin head heavy chain with an actin dimer
    • Labbé, J.P., Mornet, D., Roseau, G. & Kassab, R. (1982) Cross-linking of F-actin to skeletal muscle myosin subfragment 1 with Bis (imido esters): further evidence for the interaction of myosin head heavy chain with an actin dimer. Biochemistry 21, 6897-6902.
    • (1982) Biochemistry , vol.21 , pp. 6897-6902
    • Labbé, J.P.1    Mornet, D.2    Roseau, G.3    Kassab, R.4
  • 65
    • 0028351888 scopus 로고
    • Tropomyosin inhibits the glutaraldehyde-induced cross-link between the central 48-kDa fragment of myosin head and segment 48-67 in actin subdomain 2
    • Bonafé, N., Mathieu, M., Kassab, R. & Chaussepied, P. (1994) Tropomyosin inhibits the glutaraldehyde-induced cross-link between the central 48-kDa fragment of myosin head and segment 48-67 in actin subdomain 2. Biochemistry 33, 2594-2603.
    • (1994) Biochemistry , vol.33 , pp. 2594-2603
    • Bonafé, N.1    Mathieu, M.2    Kassab, R.3    Chaussepied, P.4
  • 66
    • 0028849487 scopus 로고
    • Binding of heavy-chain and essential light-chain 1 of S1 to actin depends on the degree of saturation of F-actin filaments with S1
    • Andreev, O.A. & Borejdo, J. (1995) Binding of heavy-chain and essential light-chain 1 of S1 to actin depends on the degree of saturation of F-actin filaments with S1. Biochemistry 34, 14829-14833.
    • (1995) Biochemistry , vol.34 , pp. 14829-14833
    • Andreev, O.A.1    Borejdo, J.2


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