메뉴 건너뛰기




Volumn 138, Issue 4, 1997, Pages 771-781

Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; COFILIN; F ACTIN; PHALLOIDIN;

EID: 0030820734     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.138.4.771     Document Type: Article
Times cited : (609)

References (68)
  • 1
    • 0022924035 scopus 로고
    • The three-dimensional structure of the actin filament revisited
    • Aebi, U., R. Millonig, H. Salvo, and A. Engel. 1986. The three-dimensional structure of the actin filament revisited. Ann. N.Y. Acad. Sci. 483:100-119.
    • (1986) Ann. N.Y. Acad. Sci. , vol.483 , pp. 100-119
    • Aebi, U.1    Millonig, R.2    Salvo, H.3    Engel, A.4
  • 2
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew, B.J., L.S. Minamide, and J.R. Bamburg. 1995. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J. Biol. Chem. 270:17582-17587.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 3
    • 0016816385 scopus 로고
    • Combination of data from helical particles: Correlation and selection
    • Amos, L.A. 1975. Combination of data from helical particles: correlation and selection. J. Mol. Biol. 99:65-73.
    • (1975) J. Mol. Biol. , vol.99 , pp. 65-73
    • Amos, L.A.1
  • 4
    • 0023571668 scopus 로고
    • Distribution and cellular localization of actin depolymerizing factor
    • Bamburg, J.R., and D. Bray. 1987. Distribution and cellular localization of actin depolymerizing factor. J. Cell Biol. 105:2817-2825.
    • (1987) J. Cell Biol. , vol.105 , pp. 2817-2825
    • Bamburg, J.R.1    Bray, D.2
  • 5
    • 0019170917 scopus 로고
    • Partial purification and characterization of an actin depolymerizing factor from brain
    • Bamburg, J.R., H.E. Harris. and A.G. Weeds. 1980. Partial purification and characterization of an actin depolymerizing factor from brain. FEBS (Fed. Eur. Biochem. Soc.) Lett. 121:178-182.
    • (1980) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.121 , pp. 178-182
    • Bamburg, J.R.1    Harris, H.E.2    Weeds, A.G.3
  • 6
    • 0020025754 scopus 로고
    • Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin depolymerizing factor (ADF)
    • Bernstein, B.W., and J.R. Bamburg. 1982. Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin depolymerizing factor (ADF). Cell Motil. 2:1-8.
    • (1982) Cell Motil. , vol.2 , pp. 1-8
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 7
    • 0025932529 scopus 로고
    • The structural basis for the intrinsic disorder of the actin filament: The "lateral slipping" model
    • Bremer, A., R.C. Millonig, R. Sutterlin, A. Engel, and T. Pollard. 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.5
  • 8
    • 0028046781 scopus 로고
    • Towards atomic interpretation of F-actin filament three-dimensional reconstructions
    • Bremer, A., C. Henn, K. Goldie, A. Engel, P.R. Smith, and U. Aebi. 1994. Towards atomic interpretation of F-actin filament three-dimensional reconstructions. J. Mol. Biol. 741:683-700.
    • (1994) J. Mol. Biol. , vol.741 , pp. 683-700
    • Bremer, A.1    Henn, C.2    Goldie, K.3    Engel, A.4    Smith, P.R.5    Aebi, U.6
  • 9
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier, M., J. Santolini, V. Laurent, D. Didry, H. Yan, N. Chua, and D. Pantaloni. 1997. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136:1307-1323.
    • (1997) J. Cell Biol. , vol.136 , pp. 1307-1323
    • Carlier, M.1    Santolini, J.2    Laurent, V.3    Didry, D.4    Yan, H.5    Chua, N.6    Pantaloni, D.7
  • 10
    • 0001037624 scopus 로고
    • Algorithm for ribbon models of proteins
    • Carson, M., and C.E. Bugg. 1986. Algorithm for ribbon models of proteins. J. Mol. Graphics. 4:121-122.
    • (1986) J. Mol. Graphics. , vol.4 , pp. 121-122
    • Carson, M.1    Bugg, C.E.2
  • 11
    • 0021050753 scopus 로고
    • Under physiological conditions actin disassembles slowly from the nonpreferred end of an actin filament
    • Coluccio, L., and L. Tilney. 1983. Under physiological conditions actin disassembles slowly from the nonpreferred end of an actin filament. J. Cell Biol. 97:1629-1634.
    • (1983) J. Cell Biol. , vol.97 , pp. 1629-1634
    • Coluccio, L.1    Tilney, L.2
  • 12
    • 0022619258 scopus 로고
    • Purification and characterization of actophorin, a new 15,000-Dalton actin-binding protein from Acanthamoeba castellanii
    • Cooper, J.A., J.D. Blum, R.C.J. Williams, and T.D. Pollard. 1986. Purification and characterization of actophorin, a new 15,000-Dalton actin-binding protein from Acanthamoeba castellanii. J. Biol. Chem. 261:477-485.
    • (1986) J. Biol. Chem. , vol.261 , pp. 477-485
    • Cooper, J.A.1    Blum, J.D.2    Williams, R.C.J.3    Pollard, T.D.4
  • 13
    • 0014945329 scopus 로고
    • Reconstruction of three-dimensional images from electron micrograph of structures with helical symmetry
    • DeRosier, D.J., and P.B. Moore. 1970. Reconstruction of three-dimensional images from electron micrograph of structures with helical symmetry. J. Mol. Biol. 52:355-369.
    • (1970) J. Mol. Biol. , vol.52 , pp. 355-369
    • DeRosier, D.J.1    Moore, P.B.2
  • 14
    • 0022993466 scopus 로고
    • Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules
    • Drenckhahn, D., and T. Pollard. 1986. Elongation of actin filaments is a diffusion-limited reaction at the barbed end and is accelerated by inert macromolecules. J. Biol. Chem. 261:12754-12758.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12754-12758
    • Drenckhahn, D.1    Pollard, T.2
  • 15
    • 0026619126 scopus 로고
    • Image analysis shows that variations in actin crossover spacings are random, not compensatory
    • Egelman, E.H., and D.J. DeRosier. 1992. Image analysis shows that variations in actin crossover spacings are random, not compensatory. Biophys. J. 63: 1299-1305.
    • (1992) Biophys. J. , vol.63 , pp. 1299-1305
    • Egelman, E.H.1    DeRosier, D.J.2
  • 16
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman, E.H., N. Francis, and D.J. DeRosier. 1982. F-actin is a helix with a random variable twist. Nature (Lond.). 298:131-135.
    • (1982) Nature (Lond.) , vol.298 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.J.3
  • 19
    • 0028799957 scopus 로고
    • Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis
    • Gunsalus, K.C., S. Bonaccorsi, E. Williams, F. Verni, M. Gatti, and M.L. Goldberg. 1995. Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis. J. Cell Biol. 131:1243-1259.
    • (1995) J. Cell Biol. , vol.131 , pp. 1243-1259
    • Gunsalus, K.C.1    Bonaccorsi, S.2    Williams, E.3    Verni, F.4    Gatti, M.5    Goldberg, M.L.6
  • 20
    • 0008711922 scopus 로고
    • Axial period of actin filaments
    • Hanson, J. 1967. Axial period of actin filaments. Nature (Lond.). 213:353-356.
    • (1967) Nature (Lond.) , vol.213 , pp. 353-356
    • Hanson, J.1
  • 21
    • 0020568199 scopus 로고
    • Plasma actin depolymerizing factor has both calcium-dependent and calcium-independent effects on actin
    • Harris, H.E., and A.G. Weeds. 1983. Plasma actin depolymerizing factor has both calcium-dependent and calcium-independent effects on actin. Biochemistry. 22:2728-2741.
    • (1983) Biochemistry. , vol.22 , pp. 2728-2741
    • Harris, H.E.1    Weeds, A.G.2
  • 22
    • 0030604703 scopus 로고    scopus 로고
    • Tertiary structure of destrin and structural similarity between two actin-regulating protein families
    • Hatanaka, H., K. Ogura, M. Moriyama, S. Ichikawa, I. Yahara, and F. Inagaki. 1996. Tertiary structure of destrin and structural similarity between two actin-regulating protein families. Cell. 85:1047-1055.
    • (1996) Cell , vol.85 , pp. 1047-1055
    • Hatanaka, H.1    Ogura, K.2    Moriyama, M.3    Ichikawa, S.4    Yahara, I.5    Inagaki, F.6
  • 23
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins, M., B. Pope, S. Maciver, and A.G. Weeds. 1993. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry. 32:9985-9993.
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.3    Weeds, A.G.4
  • 24
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor (ADF) with G- and F-actin
    • Hayden, S.M., P.S. Miller, A. Brauweiler, and J.R. Bamburg. 1993. Analysis of the interactions of actin depolymerizing factor (ADF) with G-and F-actin. Biochemistry. 32:9994-10004.
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 25
    • 0030927201 scopus 로고    scopus 로고
    • 3D reconstruction of smooth muscle thin filaments: Contribution of caldesmon and calponin to filament structure
    • Hodgkinson, J.L., M. El-Mezgueldi, S. Marston, R. Craig, P. Vibert, and W. Lehman. 1997. 3D reconstruction of smooth muscle thin filaments: contribution of caldesmon and calponin to filament structure. Biophys. J. 72:2398-2404.
    • (1997) Biophys. J. , vol.72 , pp. 2398-2404
    • Hodgkinson, J.L.1    El-Mezgueldi, M.2    Marston, S.3    Craig, R.4    Vibert, P.5    Lehman, W.6
  • 27
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones, T.A., J.Y. Zou, C. Cowan, and M. Kjeldgaard. 1991. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47:110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, C.3    Kjeldgaard, M.4
  • 28
    • 0028179144 scopus 로고
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature (Lond.). 368:65-67.
    • (1994) Nature (Lond.) , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vibert, P.3
  • 29
    • 0029131118 scopus 로고
    • Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments
    • Lehman, W., P. Vibert, P. Uman, and R. Craig. 1995. Steric-blocking by tropomyosin visualized in relaxed vertebrate muscle thin filaments. J. Mol. Biol. 251:191-196.
    • (1995) J. Mol. Biol. , vol.251 , pp. 191-196
    • Lehman, W.1    Vibert, P.2    Uman, P.3    Craig, R.4
  • 30
    • 0031134225 scopus 로고    scopus 로고
    • Crystal structure of the actin-binding protein actophorin from Acanthamoeba
    • Leonard, S., A. Gittis, E. Petrulla, T. Pollard, and E. Lattman. 1997. Crystal structure of the actin-binding protein actophorin from Acanthamoeba. Nat. Struct. Biol. 4:369-373.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 369-373
    • Leonard, S.1    Gittis, A.2    Petrulla, E.3    Pollard, T.4    Lattman, E.5
  • 32
    • 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., D. Popp, and K.C. Holmes. 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
  • 33
    • 0028357931 scopus 로고
    • Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: Consequences for cell locomotion
    • Maciver, S.K., and A.G. Weeds. 1994. Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: consequences for cell locomotion. FEBS (Fed. Eur. Biochem. Soc.) Lett. 347:251-256.
    • (1994) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.347 , pp. 251-256
    • Maciver, S.K.1    Weeds, A.G.2
  • 34
    • 0026340941 scopus 로고
    • Characterization of actin filament severing by actophorin from Acanthamoeba castellanii
    • Maciver, S.K., H.G. Zot, and T.D. Pollard. 1991. Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J. Cell Biol. 115:1611-1620.
    • (1991) J. Cell Biol. , vol.115 , pp. 1611-1620
    • Maciver, S.K.1    Zot, H.G.2    Pollard, T.D.3
  • 35
    • 0028176006 scopus 로고
    • Determination of the α-actinin binding site on actin filaments by cryoelectron microscopy and image analysis
    • McGough, A., M. Way, and D. DeRosier. 1994. Determination of the α-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
  • 36
    • 0028069286 scopus 로고
    • The Caneorhabditis elegans unc-60 gene encodes proteins homologous to a family of actin-binding proteins
    • McKim, K., C. Matheson, M. Marra, M. Wakarchuk, and D. Baillie. 1994. The Caneorhabditis elegans unc-60 gene encodes proteins homologous to a family of actin-binding proteins. Mol. Gen. Genet. 242:346-357.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 346-357
    • McKim, K.1    Matheson, C.2    Marra, M.3    Wakarchuk, M.4    Baillie, D.5
  • 37
    • 0023374114 scopus 로고
    • Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy
    • Milligan, R.A., and P.F. Flicker. 1987. Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy. J. Cell Biol. 105:29-39.
    • (1987) J. Cell Biol. , vol.105 , pp. 29-39
    • Milligan, R.A.1    Flicker, P.F.2
  • 38
    • 0028839660 scopus 로고
    • The ADF/cofilin proteins: Stimulus-responsive modulators of actin dynamics
    • Moon, A., and D. Drubin. 1995. The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics. Mol. Biol. Cell. 6:1423-1431.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1423-1431
    • Moon, A.1    Drubin, D.2
  • 39
    • 0027446345 scopus 로고
    • Cofilin is an essential component of the yeast cortical cytoskeleton
    • Moon, A.L., P.A. Janmey, K.A. Louie, and D. Drubin. 1993. Cofilin is an essential component of the yeast cortical cytoskeleton. J. Cell Biol. 120:421-435.
    • (1993) J. Cell Biol. , vol.120 , pp. 421-435
    • Moon, A.L.1    Janmey, P.A.2    Louie, K.A.3    Drubin, D.4
  • 41
    • 0026726153 scopus 로고
    • Mutational analysis of chimeric proteins between cofilin and destrin
    • Moriyama, K., N. Yonezawa, H. Sakai, I. Yahara, and E. Nishida. 1992. Mutational analysis of chimeric proteins between cofilin and destrin. J. Biol. Chem. 267:7240-7244.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7240-7244
    • Moriyama, K.1    Yonezawa, N.2    Sakai, H.3    Yahara, I.4    Nishida, E.5
  • 42
    • 0021749110 scopus 로고
    • Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
    • Nishida, E., S. Maekawa, and H. Sakai. 1984. Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry. 23:5307-5313.
    • (1984) Biochemistry , vol.23 , pp. 5307-5313
    • Nishida, E.1    Maekawa, S.2    Sakai, H.3
  • 43
    • 0026437417 scopus 로고
    • Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis
    • Orlova, A., and E.H. Egelman. 1992. Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis. J. Mol. Biol. 227: 1043-1053.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1043-1053
    • Orlova, A.1    Egelman, E.H.2
  • 44
    • 0027328612 scopus 로고
    • A conformational change in the actin subunit can change the flexibility of the actin filament
    • Orlova, A., and E.H. Egelman. 1993. A conformational change in the actin subunit can change the flexibility of the actin filament. J. Mol. Biol. 232:334-341.
    • (1993) J. Mol. Biol. , vol.232 , pp. 334-341
    • Orlova, A.1    Egelman, E.H.2
  • 45
    • 0028049263 scopus 로고
    • Three-dimensional reconstruction of a complex of F-actin with antibody Fab fragments to actin's amino terminus
    • Orlova, A., X. Yu, and E.H. Egelman. 1994. Three-dimensional reconstruction of a complex of F-actin with antibody Fab fragments to actin's amino terminus. Biophys. J. 66:276-285.
    • (1994) Biophys. J. , vol.66 , pp. 276-285
    • Orlova, A.1    Yu, X.2    Egelman, E.H.3
  • 46
    • 0027340549 scopus 로고
    • A 13 Å map of the actin-scruin filament from the Limulus acrosomal process
    • Owen, C., and D.J. DeRosier. 1993. A 13 Å map of the actin-scruin filament from the Limulus acrosomal process. J. Cell Biol. 123:337-344.
    • (1993) J. Cell Biol. , vol.123 , pp. 337-344
    • Owen, C.1    DeRosier, D.J.2
  • 47
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard, T.D. 1986. Rate constants for the reactions of ATP-and ADP-actin with the ends of actin filaments. J. Cell Biol. 103:2747-2754.
    • (1986) J. Cell Biol. , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 49
    • 0030821155 scopus 로고    scopus 로고
    • Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails
    • Rosenblatt, J., B.J. Agnew, H. Abe, J.R. Bamburg, and T.J. Mitchison. 1997. Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails. J. Cell Biol. 136: 1323-1332.
    • (1997) J. Cell Biol. , vol.136 , pp. 1323-1332
    • Rosenblatt, J.1    Agnew, B.J.2    Abe, H.3    Bamburg, J.R.4    Mitchison, T.J.5
  • 51
    • 0029928871 scopus 로고    scopus 로고
    • SUPRIM: Easily modified image processing software
    • Schroeter, J.P., and J.-P. Bretaudiere. 1996. SUPRIM: easily modified image processing software. V. Struct. Biol. 116:131-137.
    • (1996) V. Struct. Biol. , vol.116 , pp. 131-137
    • Schroeter, J.P.1    Bretaudiere, J.-P.2
  • 52
    • 0028797231 scopus 로고
    • Getting the actin filaments straight: Nucleation-release or treadmilling
    • Small, J.V. 1995. Getting the actin filaments straight: nucleation-release or treadmilling. Trends Cell Biol. 5:52-55.
    • (1995) Trends Cell Biol. , vol.5 , pp. 52-55
    • Small, J.V.1
  • 53
    • 0001420610 scopus 로고
    • Computer image processing of electron micrographs of biological structures with helical symmetry
    • Stewart, M. 1988. Computer image processing of electron micrographs of biological structures with helical symmetry. J. Electron Micros. Tech. 9:325-358.
    • (1988) J. Electron Micros. Tech. , vol.9 , pp. 325-358
    • Stewart, M.1
  • 54
    • 0023252082 scopus 로고
    • The variable twist of actin and its modulation by actin-binding proteins
    • Stokes, D.L., and D.J. DeRosier. 1987. The variable twist of actin and its modulation by actin-binding proteins. J. Cell Biol. 109:1005-1017.
    • (1987) J. Cell Biol. , vol.109 , pp. 1005-1017
    • Stokes, D.L.1    DeRosier, D.J.2
  • 55
    • 0030798735 scopus 로고    scopus 로고
    • Accelerating on a treadmill: ADF/cofilin promotes rapid actin filament turnover in the dynamic cytoskeleton
    • Theriot, J.A. 1997. Accelerating on a treadmill: ADF/cofilin promotes rapid actin filament turnover in the dynamic cytoskeleton. J. Cell Biol. 136:1165-1168.
    • (1997) J. Cell Biol. , vol.136 , pp. 1165-1168
    • Theriot, J.A.1
  • 56
    • 0028861589 scopus 로고
    • Normal modes as refinement parameters for the F-actin model
    • Tirion, M.M., D. ben-Avraham, M. Lorenz, and K.C. Holmes. 1995. Normal modes as refinement parameters for the F-actin model. Biophys. J. 68:5-12.
    • (1995) Biophys. J. , vol.68 , pp. 5-12
    • Tirion, M.M.1    Ben-Avraham, D.2    Lorenz, M.3    Holmes, K.C.4
  • 57
    • 0022924072 scopus 로고
    • Actin and flagellar filaments: Two helical structures with variable twist
    • Trachtenberg, S., D. Stokes, E. Bullitt, and D. DeRosier. 1986. Actin and flagellar filaments: two helical structures with variable twist. Ann. N.Y. Acad. Sci. 483:89-99.
    • (1986) Ann. N.Y. Acad. Sci. , vol.483 , pp. 89-99
    • Trachtenberg, S.1    Stokes, D.2    Bullitt, E.3    DeRosier, D.4
  • 58
    • 0029822651 scopus 로고    scopus 로고
    • Torsional rigidity of single actin filaments and actin-actin bond breaking force under torsion measured directly by in vitro micromanipulation
    • Tsuda, Y., H. Yasutake, A. Ishijima, and T. Yanagida. 1996. Torsional rigidity of single actin filaments and actin-actin bond breaking force under torsion measured directly by in vitro micromanipulation. Proc Natl. Acad. Sci. USA. 93:12937-12942.
    • (1996) Proc Natl. Acad. Sci. USA , vol.93 , pp. 12937-12942
    • Tsuda, Y.1    Yasutake, H.2    Ishijima, A.3    Yanagida, T.4
  • 59
    • 0027514929 scopus 로고
    • Three-dimensional reconstruction of caldesmon-containing smooth muscle filaments
    • Vibert, P., R. Craig, and W. Lehman. 1993. Three-dimensional reconstruction of caldesmon-containing smooth muscle filaments. J. Cell Biol. 123:313-321.
    • (1993) J. Cell Biol. , vol.123 , pp. 313-321
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 62
    • 0029311258 scopus 로고
    • PHOELIX: A package for automated helical reconstruction
    • Whittaker, M., B.O. Carragher, and R.A. Milligan. 1995b. PHOELIX: a package for automated helical reconstruction. Ultramicroscopy. 58:245-250.
    • (1995) Ultramicroscopy , vol.58 , pp. 245-250
    • Whittaker, M.1    Carragher, B.O.2    Milligan, R.A.3
  • 63
    • 0022403777 scopus 로고
    • pH control of actin polymerization by cofilin
    • Yonezawa, N., E. Nishida, and H. Sakai. 1985. pH control of actin polymerization by cofilin. J. Biol. Chem. 260:14410-14412.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14410-14412
    • Yonezawa, N.1    Nishida, E.2    Sakai, H.3
  • 64
    • 0025277362 scopus 로고
    • Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease-i with actin by phosphoinositides
    • Yonezawa, N., E. Nishida, K. Iida, I. Yahara, and H. Sakai. 1990. Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease-i with actin by phosphoinositides. J. Biol. Chem. 265:8382-8386.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8382-8386
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Yahara, I.4    Sakai, H.5
  • 65
    • 0023989532 scopus 로고
    • Studies on the interaction between actin and cofilin purified by a new method
    • Yonezawa, N., E. Nishida, S. Maekawa, and H. Sakai. 1988. Studies on the interaction between actin and cofilin purified by a new method. Biochem. J. 251:121-127.
    • (1988) Biochem. J. , vol.251 , pp. 121-127
    • Yonezawa, N.1    Nishida, E.2    Maekawa, S.3    Sakai, H.4
  • 66
    • 0025744897 scopus 로고
    • Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin
    • Yonezawa, N., E. Nishida, K. Iida, H. Kumagai, I. Yahara, and H. Sakai. 1991. Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin. J. Biol. Chem. 266: 10485-10489.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10485-10489
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Kumagai, H.4    Yahara, I.5    Sakai, H.6
  • 67
    • 0029928874 scopus 로고    scopus 로고
    • CTF determination of images of ice-embedded single particles using a graphics interface
    • Zhou, Z.H., S. Hardt, B. Wang, M.B. Sherman, J. Jakana, and W. Chiu. 1996. CTF determination of images of ice-embedded single particles using a graphics interface. J. Struct. Biol. 116:216-223.
    • (1996) J. Struct. Biol. , vol.116 , pp. 216-223
    • Zhou, Z.H.1    Hardt, S.2    Wang, B.3    Sherman, M.B.4    Jakana, J.5    Chiu, W.6
  • 68
    • 0027293382 scopus 로고
    • Recent quantitative studies of actin filament turnover during cell locomotion
    • Zigmond, S.H. 1993. Recent quantitative studies of actin filament turnover during cell locomotion. Cell Motil. Cytoskeleton. 25:309-316.
    • (1993) Cell Motil. Cytoskeleton. , vol.25 , pp. 309-316
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.