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Volumn 260, Issue 5, 1996, Pages 756-766

Cooperativity in F-actin: Binding of gelsolin at the barbed end affects structure and dynamics of the whole filament

Author keywords

Actin; Cooperativity; Dynamics; Gelsolin; Phosphorescence

Indexed keywords

ACTIN BINDING PROTEIN; ERYTHROSINE; F ACTIN; GELSOLIN; GLUTARALDEHYDE; IODOACETAMIDE;

EID: 0030564835     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0435     Document Type: Article
Times cited : (93)

References (63)
  • 1
    • 0028603483 scopus 로고
    • Gelsolin displaces phalloidin from actin filaments. A new fluorescence method shows that both Ca and Mg affect the rate at which gelsolin severs F-actin
    • Allen, P. G. & Janmey, P. A. (1994). Gelsolin displaces phalloidin from actin filaments. A new fluorescence method shows that both Ca and Mg affect the rate at which gelsolin severs F-actin. J. Biol. Chem. 269, 32916-32923.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32916-32923
    • Allen, P.G.1    Janmey, P.A.2
  • 2
    • 0002291771 scopus 로고
    • Torsion dynamics and depolarization of fluorescence of linear macromolecules. I. Theory and application to DNA
    • Allison, S. A. & Schurr, M. (1979). Torsion dynamics and depolarization of fluorescence of linear macromolecules. I. Theory and application to DNA. Chem. Phys. 41, 35-59.
    • (1979) Chem. Phys. , vol.41 , pp. 35-59
    • Allison, S.A.1    Schurr, M.2
  • 3
    • 0028905547 scopus 로고
    • Dynamic and elastic properties of F-actin: A normal-modes analysis
    • ben-Avraham, D. & Tirion, M. M. (1995). Dynamic and elastic properties of F-actin: a normal-modes analysis. Biophys. J. 68, 1231-1245.
    • (1995) Biophys. J. , vol.68 , pp. 1231-1245
    • Ben-Avraham, D.1    Tirion, M.M.2
  • 4
    • 0023474327 scopus 로고
    • Antigenic probes locate a serum-gelsolin-interaction site on the C-terminal part of actin
    • Boyer, M., Feinberg, J., Hue, H. K., Capony, J. P., Benyamin, Y. & Roustan, C. (1987). Antigenic probes locate a serum-gelsolin-interaction site on the C-terminal part of actin. Biochem. J. 248, 359-364.
    • (1987) Biochem. J. , vol.248 , pp. 359-364
    • Boyer, M.1    Feinberg, J.2    Hue, H.K.3    Capony, J.P.4    Benyamin, Y.5    Roustan, C.6
  • 5
    • 0025932529 scopus 로고
    • The structural basis for the intrinsic disorder of the actin filament: The "lateral slipping" model
    • Bremer, A., Millonig, R. C., Sutterlin, R., Engel, A., Pollard, T. D. & Aebi, U. (1991). The structural basis for the intrinsic disorder of the actin filament: the "lateral slipping" model. J. Cell. Biol. 115, 689-703.
    • (1991) J. Cell. Biol. , vol.115 , pp. 689-703
    • Bremer, A.1    Millonig, R.C.2    Sutterlin, R.3    Engel, A.4    Pollard, T.D.5    Aebi, U.6
  • 6
    • 0021770684 scopus 로고
    • Actin-gelsolin interactions. Evidence for two actin-binding sites
    • Bryan, J. & Kurth, M. C. (1984). Actin-gelsolin interactions. Evidence for two actin-binding sites. J. Biol. Chem. 259, 7480-7487.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7480-7487
    • Bryan, J.1    Kurth, M.C.2
  • 7
    • 0027240526 scopus 로고
    • Cooperative interactions between adjacent troponin-tropomyosin complexes may be transmitted through the actin filament
    • Butters, C. A., Willadsen, K. A. & Tobacman, L. S. (1993). Cooperative interactions between adjacent troponin-tropomyosin complexes may be transmitted through the actin filament. J. Biol Chem. 268, 15565-15570.
    • (1993) J. Biol Chem. , vol.268 , pp. 15565-15570
    • Butters, C.A.1    Willadsen, K.A.2    Tobacman, L.S.3
  • 8
    • 0027967683 scopus 로고
    • Structural connectivity in actin: Effect of C-terminal modifications on the properties of actin
    • Crosbie, R. H., Miller, C., Cheung, P., Goodnight, T., Muhlrad, A. & Reisler, E. (1994). Structural connectivity in actin: effect 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
  • 9
    • 0026593988 scopus 로고
    • Actomyosin interactions in the presence of ATP and the N-terminal segment of actin
    • DasGupta, G. & Reisler, E. (1992). Actomyosin interactions in the presence of ATP and the N-terminal segment of actin. Biochemistry, 31, 1836-1841.
    • (1992) Biochemistry , vol.31 , pp. 1836-1841
    • DasGupta, G.1    Reisler, E.2
  • 10
    • 0028067048 scopus 로고
    • Nucleation of actin polymerization by gelsolin
    • Ditsch, A. & Wegner, A. (1994). Nucleation of actin polymerization by gelsolin. Eur. J. Biochem. 224, 223-227.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 223-227
    • Ditsch, A.1    Wegner, A.2
  • 11
    • 0026795843 scopus 로고
    • Interaction of gelsolin with covalently cross-linked actin dimer
    • Doi, Y. (1992). Interaction of gelsolin with covalently cross-linked actin dimer. Biochemistry, 31, 10061-10069.
    • (1992) Biochemistry , vol.31 , pp. 10061-10069
    • Doi, Y.1
  • 12
    • 0027497704 scopus 로고
    • Cooperative effect on filament stability in actin modified at the C-terminus by substitution or truncation
    • Drewes, G. & Faulstich, H. (1993). Cooperative effect on filament stability in actin modified at the C-terminus by substitution or truncation. Eur. J. Biochem. 212, 247-253.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 247-253
    • Drewes, G.1    Faulstich, H.2
  • 13
    • 0021659708 scopus 로고
    • Microsecond rotational motions of eosin-labeled myosin measured by time-resolved anisotropy of absorption and phosphorescence
    • Eads, T. & Thomas, D. D. (1984). Microsecond rotational motions of eosin-labeled myosin measured by time-resolved anisotropy of absorption and phosphorescence. J. Mol, Biol. 179, 55-81.
    • (1984) J. Mol, Biol. , vol.179 , pp. 55-81
    • Eads, T.1    Thomas, D.D.2
  • 14
    • 0028988935 scopus 로고
    • New insight into actin filament dynamics
    • Egelman, E. H. & Orlova, A. (1995). New insight into actin filament dynamics. Curr. Opin. Cell Biol. 5, 172-180.
    • (1995) Curr. Opin. Cell Biol. , vol.5 , pp. 172-180
    • Egelman, E.H.1    Orlova, A.2
  • 15
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman, E. H., Francis, N. & DeRosier, D. J. (1982). F-actin is a helix with a random variable twist. Nature, 298, 131-135.
    • (1982) Nature , vol.298 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.J.3
  • 16
    • 0024511257 scopus 로고
    • Co-operativity in protein-protein association. The structure and stability of the actin filament
    • Erickson, H. P. (1989). Co-operativity in protein-protein association. The structure and stability of the actin filament. J. Mol. Biol. 206, 465-474.
    • (1989) J. Mol. Biol. , vol.206 , pp. 465-474
    • Erickson, H.P.1
  • 17
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: The size of cooperative unit
    • Geeves, M. A. & Lehrer, S. S. (1994). Dynamics of the muscle thin filament regulatory switch: the size of cooperative unit. Biophys. J. 67, 273-282.
    • (1994) Biophys. J. , vol.67 , pp. 273-282
    • Geeves, M.A.1    Lehrer, S.S.2
  • 18
    • 0022214653 scopus 로고
    • Lack of nucleotide cleavage on the binding of G-actin-ATP to plasma gelsolin
    • Harris, H. E. (1985). Lack of nucleotide cleavage on the binding of G-actin-ATP to plasma gelsolin. FEBS Letters, 90, 81-83.
    • (1985) FEBS Letters , vol.90 , pp. 81-83
    • Harris, H.E.1
  • 19
    • 0023950903 scopus 로고
    • 2+-G-actin in ATP and ADP
    • 2+-G-actin in ATP and ADP. FEBS Letters, 233, 359-362.
    • (1988) FEBS Letters , vol.233 , pp. 359-362
    • Harris, H.E.1
  • 20
    • 0027134875 scopus 로고
    • The actin monomers in the ternary gelsolin: 2 actin complex are in an antiparallel orientation
    • Hesterkamp, T., Weeds, A. G. & Mannhertz, H. G. (1993). The actin monomers in the ternary gelsolin: 2 actin complex are in an antiparallel orientation. Eur. J. Biochem. 218, 507-513.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 507-513
    • Hesterkamp, T.1    Weeds, A.G.2    Mannhertz, H.G.3
  • 21
    • 0025075839 scopus 로고
    • Atomic model of the actin filament
    • Holmes, K. C., Popp, D., Gebhard, W. & 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
  • 22
    • 0023035551 scopus 로고
    • Kinetics of actin monomer exchange at the slow growing ends of actin filaments and their relation to the elongation of filaments shortened by gelsolin
    • Janmey, P. A. & Stossel, T. P. (1986). Kinetics of actin monomer exchange at the slow growing ends of actin filaments and their relation to the elongation of filaments shortened by gelsolin. J. Muscle Res. Cell Motil. 7, 446-454.
    • (1986) J. Muscle Res. Cell Motil. , vol.7 , pp. 446-454
    • Janmey, P.A.1    Stossel, T.P.2
  • 23
    • 0022969835 scopus 로고
    • Structure and mobility of actin filaments as measured by quasielastic light scattering, viscometry and electron microscopy
    • Janmey, P. A., Peetermans, J., Zaner, K. S., Stossel, T. P. & Tanaka, T. (1986). Structure and mobility of actin filaments as measured by quasielastic light scattering, viscometry and electron microscopy. J. Biol. Chem. 261, 8357-8362.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8357-8362
    • Janmey, P.A.1    Peetermans, J.2    Zaner, K.S.3    Stossel, T.P.4    Tanaka, T.5
  • 24
    • 0027134594 scopus 로고
    • The actin/actin interactions involving the N-terminus of the DNase-I-binding loop are crucial for stabilization of the actin filament
    • Khaitlina, S. Y., Moraczewska, J. & Strzelecka-Golaszewska, H. (1993). The actin/actin interactions involving the N-terminus of the DNase-I-binding loop are crucial for stabilization of the actin filament. Eur. J. Biochem. 218, 911-920.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 911-920
    • Khaitlina, S.Y.1    Moraczewska, J.2    Strzelecka-Golaszewska, H.3
  • 25
    • 0017729574 scopus 로고
    • A theory of fluorescence polarization decay in membranes
    • Kinosita, K., Kawato, S. & Ikegami, A. (1977). A theory of fluorescence polarization decay in membranes. Biophys. J. 20, 289-305.
    • (1977) Biophys. J. , vol.20 , pp. 289-305
    • Kinosita, K.1    Kawato, S.2    Ikegami, A.3
  • 27
    • 0015518610 scopus 로고
    • The crosslinking of actin and of tropomyosin by glutaraldehyde
    • Lehrer, S. (1972). The crosslinking of actin and of tropomyosin by glutaraldehyde. Biochem. Biophys. Res. Commun. 48, 967-975.
    • (1972) Biochem. Biophys. Res. Commun. , vol.48 , pp. 967-975
    • Lehrer, S.1
  • 28
    • 0000488695 scopus 로고
    • Interactions of tensin with actin and identification of its three distinct actin-binding domains
    • Lo, S. H., Janmey, P. A., Hartwig, J. H. & Chen, L. B. (1994). Interactions of tensin with actin and identification of its three distinct actin-binding domains. J. Cell Biol. 125, 1067-1075.
    • (1994) J. Cell Biol. , vol.125 , pp. 1067-1075
    • Lo, S.H.1    Janmey, P.A.2    Hartwig, J.H.3    Chen, L.B.4
  • 29
    • 0027131941 scopus 로고
    • Refinement of the F-actin structure against X-ray fiber diffraction data by the use of a direct mutation algorithm
    • Lorenz, M., Popp, D. & Holmes, K. C. (1993). Refinement of the F-actin structure against X-ray fiber diffraction data by the use of a direct 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
  • 30
    • 0024276822 scopus 로고
    • Microsecond rotational dynamics of phosphorescent-labeled muscle crossbridges
    • Ludescher, R. D. & Thomas, D. D. (1988). Microsecond rotational dynamics of phosphorescent-labeled muscle crossbridges. Biochemistry, 27, 3343-3351.
    • (1988) Biochemistry , vol.27 , pp. 3343-3351
    • Ludescher, R.D.1    Thomas, D.D.2
  • 31
    • 84910690843 scopus 로고
    • Triplet anisotropy studies of restricted rotational motion in myosin monomers and filaments
    • (Baskin, R. J. & Yeh, Y., eds), CRC Press Inc., Boca Raton, Florida
    • Ludescher, R. D., Eads, T. M. & Thomas, D. D. (1987). Triplet anisotropy studies of restricted rotational motion in myosin monomers and filaments. In Optical Studies of Muscle Crossbridges (Baskin, R. J. & Yeh, Y., eds), pp. 3-65, CRC Press Inc., Boca Raton, Florida.
    • (1987) Optical Studies of Muscle Crossbridges , pp. 3-65
    • Ludescher, R.D.1    Eads, T.M.2    Thomas, D.D.3
  • 32
    • 0021188285 scopus 로고
    • Capping of one end of an actin filament affects elongation at the other end
    • Maruyama, K., Yamada, N. & Mabuchi, I. (1984). Capping of one end of an actin filament affects elongation at the other end. J. Biochem. 96, 613-620.
    • (1984) J. Biochem. , vol.96 , pp. 613-620
    • Maruyama, K.1    Yamada, N.2    Mabuchi, I.3
  • 33
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin, P. J., Gooch, J. T., Mannhertz, H. G. & Weeds, A. G. (1993). Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature, 364, 685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannhertz, H.G.3    Weeds, A.G.4
  • 34
    • 0028024932 scopus 로고
    • Domain motion in actin observed by fluorescence energy transfer
    • Miki, M. & Kouyama, T. (1994). Domain motion in actin observed by fluorescence energy transfer. Biochemistry, 33, 10171-10177.
    • (1994) Biochemistry , vol.33 , pp. 10171-10177
    • Miki, M.1    Kouyama, T.2
  • 35
    • 0020364082 scopus 로고
    • Fluorescence anisotropy of labeled F-actin: Influence of divalent cations on the interaction between F-actin and myosin heads
    • Miki, M., Wahl, P. & Auchet, J. C. (1982). Fluorescence anisotropy of labeled F-actin: influence of divalent cations on the interaction between F-actin and myosin heads. Biochemistry, 20, 3661-3665.
    • (1982) Biochemistry , vol.20 , pp. 3661-3665
    • Miki, M.1    Wahl, P.2    Auchet, J.C.3
  • 36
    • 0025052483 scopus 로고
    • Molecular structure of F-actin and location of surface binding sites
    • Milligan, R. A., Whittaker, M. & 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
  • 37
    • 0023811623 scopus 로고
    • An EPR study of the rotational dynamics of actins from skeletal and smooth muscle and their complexes with heavy meromyosin
    • Mossakowska, M., Belagyi, J. & Strzelecka-Golaszewska, H. (1988). An EPR study of the rotational dynamics of actins from skeletal and smooth muscle and their complexes with heavy meromyosin. Eur. J. Biochem. 175, 557-564.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 557-564
    • Mossakowska, M.1    Belagyi, J.2    Strzelecka-Golaszewska, H.3
  • 38
    • 0027452835 scopus 로고
    • Proteolytic removal of three C-terminal residues of actin alters the monomer-monomer interactions
    • Mossakowska, M., Moraczewska, J., Khaitlina, S. & Strzelecka-Golaszewska, H. (1993). Proteolytic 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
  • 39
    • 0028228518 scopus 로고
    • Dynamic properties of actin. Structural changes induced by beryllium fluoride
    • Muhlrad, A., Cheung, P., Phan, B. C., Miller, C. & Reisler, E. (1994). Dynamic properties of actin. Structural changes induced by beryllium fluoride. J. Biol. Chem. 269, 11852-11858.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11852-11858
    • Muhlrad, A.1    Cheung, P.2    Phan, B.C.3    Miller, C.4    Reisler, E.5
  • 40
    • 0026558989 scopus 로고
    • Removing of the two C-terminal residues of actin affects the filament structure
    • O'Donoghue, S. L., Miki, M. & dosRemedios, C. G. (1992). Removing of 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.L.1    Miki, M.2    DosRemedios, C.G.3
  • 41
    • 0002232354 scopus 로고
    • Actin
    • (Timasheff, M., ed.), Dekker, New York
    • Oosawa, F. & Kasai, M. (1971). Actin. In Subunits in Biological Systems (Timasheff, M., ed.), part A, pp. 261-322. Dekker, New York.
    • (1971) Subunits in Biological Systems , Issue.PART A , pp. 261-322
    • Oosawa, F.1    Kasai, M.2
  • 42
    • 0028907435 scopus 로고
    • Structural dynamics of F-actin: I. Changes in the C terminus
    • Orlova, A. & Egelman, E. H. (1995). Structural dynamics of F-actin: I. Changes in the C terminus. J. Mol. Biol. 245, 582-597.
    • (1995) J. Mol. Biol. , vol.245 , pp. 582-597
    • Orlova, A.1    Egelman, E.H.2
  • 43
    • 0028920157 scopus 로고
    • Structural dynamics of F-actin: II. Cooperativity in structural transitions
    • Orlova, A., Prochniewicz, E. & Egelman, E. H. (1995). Structural dynamics of F-actin: II. Cooperativity in structural transitions. J. Mol. Biol. 245, 598-607.
    • (1995) J. Mol. Biol. , vol.245 , pp. 598-607
    • Orlova, A.1    Prochniewicz, E.2    Egelman, E.H.3
  • 44
    • 0025685506 scopus 로고
    • Inhibition of sliding movement of F-actin by cross-linking emphasize the role of F-actin structure in the mechanism of motility
    • Prochniewicz, E. & Yanagida, T. (1990). Inhibition of sliding movement of F-actin by cross-linking emphasize the role of F-actin structure in the mechanism of motility. J. Mol. Biol. 216, 761-772.
    • (1990) J. Mol. Biol. , vol.216 , pp. 761-772
    • Prochniewicz, E.1    Yanagida, T.2
  • 45
    • 0027254998 scopus 로고
    • Cooperativity in F-actin: Chemical modifications of actin monomers affect the functional interactions of myosin with unmodified monomers in the same actin filament
    • Prochniewicz, E., Katayama, E., Yanagida, T. & Thomas, D. D. (1993). Cooperativity in F-actin: chemical modifications of actin monomers affect the functional interactions of myosin with unmodified monomers in the same actin filament. Biophys. J. 65, 113-123.
    • (1993) Biophys. J. , vol.65 , pp. 113-123
    • Prochniewicz, E.1    Katayama, E.2    Yanagida, T.3    Thomas, D.D.4
  • 46
    • 0029966678 scopus 로고    scopus 로고
    • Microsecond rotational dynamics of actin: Spectroscopic detection and theoretical simulation
    • Prochniewicz, E, Zhang, Q., Howard, E. & Thomas, D. D. (1996). Microsecond rotational dynamics of actin: spectroscopic detection and theoretical simulation. J. Mol. Biol. 255, 446-457.
    • (1996) J. Mol. Biol. , vol.255 , pp. 446-457
    • Prochniewicz, E.1    Zhang, Q.2    Howard, E.3    Thomas, D.D.4
  • 48
    • 0002851534 scopus 로고
    • Rotational diffusion of deformable macromolecules with mean cylindrical symmetry
    • Schurr, J. M. (1984). Rotational diffusion of deformable macromolecules with mean cylindrical symmetry. Chem. Phys. 84, 71-96.
    • (1984) Chem. Phys. , vol.84 , pp. 71-96
    • Schurr, J.M.1
  • 49
    • 0025359118 scopus 로고
    • Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
    • Schwyter, D. H., Kron, S. J., Toyoshima, Y. Y., Spudich, J. A. & Reisler, E. (1990). Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin. J. Cell Biol. 111, 465-470.
    • (1990) J. Cell Biol. , vol.111 , pp. 465-470
    • Schwyter, D.H.1    Kron, S.J.2    Toyoshima, Y.Y.3    Spudich, J.A.4    Reisler, E.5
  • 50
    • 0028235759 scopus 로고
    • The actin-binding domain of gelsolin also caps actin filaments
    • Sun, H.-Q., Wooten, D. C., Janmey, P. A. & Yin, H. L. (1994). The actin-binding domain of gelsolin also caps actin filaments. J. Biol. Chem. 269, 9473-9479.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9473-9479
    • Sun, H.-Q.1    Wooten, D.C.2    Janmey, P.A.3    Yin, H.L.4
  • 51
    • 0022980864 scopus 로고
    • Gelsolin inhibits nucleotide exchange from actin
    • Tellam, R. L. (1986). Gelsolin inhibits nucleotide exchange from actin. Biochemistry, 25, 5799-5804.
    • (1986) Biochemistry , vol.25 , pp. 5799-5804
    • Tellam, R.L.1
  • 52
    • 0018791940 scopus 로고
    • Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range
    • Thomas, D. D., Seidel, J. C. & Gergely, J. (1979). Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range. J. Mol. Biol. 132, 257-273.
    • (1979) J. Mol. Biol. , vol.132 , pp. 257-273
    • Thomas, D.D.1    Seidel, J.C.2    Gergely, J.3
  • 53
    • 0027511431 scopus 로고
    • Normal mode analysis of G-actin
    • Tirion, M. M. & ben-Avraham, D. (1993). Normal mode analysis of G-actin. J. Mol. Biol. 230, 186-195.
    • (1993) J. Mol. Biol. , vol.230 , pp. 186-195
    • Tirion, M.M.1    Ben-Avraham, D.2
  • 54
  • 55
    • 0027134766 scopus 로고
    • The secrets of severings?
    • Way, M. & Matsudaira, P. (1993). The secrets of severings? Curr. Biol. 3, 887-890.
    • (1993) Curr. Biol. , vol.3 , pp. 887-890
    • Way, M.1    Matsudaira, P.2
  • 56
    • 0024318706 scopus 로고
    • Expression of human plasma gelsolin in escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis
    • Way, M., Gooch, J., Pope, B. & Weeds, A. G. (1989). Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis. J. Cell Biol. 109, 593-605.
    • (1989) J. Cell Biol. , vol.109 , pp. 593-605
    • Way, M.1    Gooch, J.2    Pope, B.3    Weeds, A.G.4
  • 57
    • 0025949804 scopus 로고
    • Role of the N-and C-terminal actin binding domains of gelsolin in barbed filament end capping
    • Weber, A., Pring, M., Lin, S. L. & Bryan, J. (1991). Role of the N-and C-terminal actin binding domains of gelsolin in barbed filament end capping. Biochemistry, 30, 9327-9334.
    • (1991) Biochemistry , vol.30 , pp. 9327-9334
    • Weber, A.1    Pring, M.2    Lin, S.L.3    Bryan, J.4
  • 59
    • 0016698509 scopus 로고
    • Kinetics of cooperative association of actin to actin filaments
    • Wegner, A. & Engel, J. (1975). Kinetics of cooperative association of actin to actin filaments. Biophys. Chem. 3, 215-225.
    • (1975) Biophys. Chem. , vol.3 , pp. 215-225
    • Wegner, A.1    Engel, J.2
  • 60
    • 0019321663 scopus 로고
    • 2+-activated regulatory protein of macrophages
    • 2+-activated regulatory protein of macrophages. J. Biol. Chem. 255, 9490-9493.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9490-9493
    • Yin, H.L.1    Stossel, T.P.2
  • 63
    • 0021692991 scopus 로고
    • Torsional motion of eosin-labeled F-actin as detected in the time-resolved anisotropy decay of the probe on the sub-millisecond time range
    • Yoshimura, H., Nishio, T. & Mihashi, K. (1984). Torsional motion of eosin-labeled F-actin as detected in the time-resolved anisotropy decay of the probe on the sub-millisecond time range. J. Mol. Biol. 179, 453-467.
    • (1984) J. Mol. Biol. , vol.179 , pp. 453-467
    • Yoshimura, H.1    Nishio, T.2    Mihashi, K.3


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