메뉴 건너뛰기




Volumn 119, Issue 3, 1997, Pages 295-320

Actin: From cell biology to atomic detail

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; F ACTIN; G ACTIN;

EID: 0030745347     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1997.3873     Document Type: Article
Times cited : (103)

References (119)
  • 3
    • 0022924035 scopus 로고
    • The three-dimensional structure of the actin filament revisited
    • Aebi U., Millonig R., Salvo H., Engel A. The three-dimensional structure of the actin filament revisited. Ann. N.Y. Acad. Sci. 483:1986;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
  • 4
    • 0026634166 scopus 로고
    • Characterization of yeast-expressed β-actins, site-specifically mutated at the tumor-related residue Gly245
    • Aspenstrom P., Engkvist H., Lindberg U., Karlsson R. Characterization of yeast-expressed β-actins, site-specifically mutated at the tumor-related residue Gly245. Eur. J. Biochem. 207:1992;315-320.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 315-320
    • Aspenstrom, P.1    Engkvist, H.2    Lindberg, U.3    Karlsson, R.4
  • 5
    • 0025868225 scopus 로고
    • Distribution of actin filament lengths and their orientation measured by gel electrophoresis in capillaries
    • Borejdo J., Burlacu S. Distribution of actin filament lengths and their orientation measured by gel electrophoresis in capillaries. J. Muscle Res. Cell Motil. 12:1991;394-407.
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 394-407
    • Borejdo, J.1    Burlacu, S.2
  • 6
    • 0025932529 scopus 로고
    • The structural basis for the intrinsic disorder of the actin filament: The 'lateral slipping' model
    • Bremer A., Millonig R. C., Sütterlin R., Engel A., Pollard T. D., Aebi U. The structural basis for the intrinsic disorder of the actin filament: The 'lateral slipping' model. J. Cell Biol. 115:1991;689-703.
    • (1991) J. Cell Biol. , vol.115 , pp. 689-703
    • Bremer, A.1    Millonig, R.C.2    Sütterlin, R.3    Engel, A.4    Pollard, T.D.5    Aebi, U.6
  • 7
    • 0026810836 scopus 로고
    • The structure of the F-actin filament and the actin molecule
    • Bremer A., Aebi U. The structure of the F-actin filament and the actin molecule. Curr. Opin. Cell Biol. 4:1992;20-26.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 20-26
    • Bremer, A.1    Aebi, U.2
  • 8
    • 0028046781 scopus 로고
    • Towards atomic interpretation of F-actin filament three-dimensional reconstructions
    • Bremer A., Henn C., Goldie K. N., Engel A., Smith P. R., Aebi U. Towards atomic interpretation of F-actin filament three-dimensional reconstructions. J. Mol. Biol. 242:1994;683-700.
    • (1994) J. Mol. Biol. , vol.242 , pp. 683-700
    • Bremer, A.1    Henn, C.2    Goldie, K.N.3    Engel, A.4    Smith, P.R.5    Aebi, U.6
  • 9
    • 0026603093 scopus 로고
    • Distribution of actin filament length measured by fluorescence microscopy
    • Burlacu S., Janmey P. A., Borejdo J. Distribution of actin filament length measured by fluorescence microscopy. Am. J. Physiol. (Cell Physiol.). 262:1992;C569-C577.
    • (1992) Am. J. Physiol. (Cell Physiol.) , vol.262
    • Burlacu, S.1    Janmey, P.A.2    Borejdo, J.3
  • 10
    • 0028046084 scopus 로고
    • Actobindin binds with high-affinity to a covalently crosslinked actin dimer
    • Bubb M. R., Lewis M. S., Korn E. D. Actobindin binds with high-affinity to a covalently crosslinked actin dimer. J. Biol. Chem. 269:1994a;25587-25591.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25587-25591
    • Bubb, M.R.1    Lewis, M.S.2    Korn, E.D.3
  • 11
    • 0028072754 scopus 로고
    • Actobindin induces the accumulation of actin dimers that neither nucleate polymerization nor self-associate
    • Bubb M. R., Knutson J. R., Porter D. K., Korn E. D. Actobindin induces the accumulation of actin dimers that neither nucleate polymerization nor self-associate. J. Biol. Chem. 269:1994b;25592-25597.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25592-25597
    • Bubb, M.R.1    Knutson, J.R.2    Porter, D.K.3    Korn, E.D.4
  • 12
    • 0028967310 scopus 로고
    • Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments
    • Bubb M. R., Spector I., Bershadsky A. D., Korn E. D. Swinholide A is a microfilament disrupting marine toxin that stabilizes actin dimers and severs actin filaments. J. Biol. Chem. 270:1995;3463-3466.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3463-3466
    • Bubb, M.R.1    Spector, I.2    Bershadsky, A.D.3    Korn, E.D.4
  • 13
    • 0023832666 scopus 로고
    • Binding of phosphate to F-ADP-actin and role of F-ADP-Pi-actin in ATP-actin polymerization
    • Carlier M. F., Pantaloni D. Binding of phosphate to F-ADP-actin and role of F-ADP-Pi-actin in ATP-actin polymerization. J. Biol. Chem. 263:1988;817-825.
    • (1988) J. Biol. Chem. , vol.263 , pp. 817-825
    • Carlier, M.F.1    Pantaloni, D.2
  • 14
    • 0025970527 scopus 로고
    • Actin: Protein structure and filament dynamics
    • Carlier M. F. Actin: Protein structure and filament dynamics. J. Biol. Chem. 266:1991;1-4.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1-4
    • Carlier, M.F.1
  • 15
    • 0027128656 scopus 로고
    • Nucleotide hydrolysis regulates the dynamics of actin filaments and microtubules
    • Carlier M. F. Nucleotide hydrolysis regulates the dynamics of actin filaments and microtubules. Philos. Trans. R. Soc. London, Ser. B., Biol. Sci. 336:1992;93-97.
    • (1992) Philos. Trans. R. Soc. London, Ser. B., Biol. Sci. , vol.336 , pp. 93-97
    • Carlier, M.F.1
  • 16
    • 0027277010 scopus 로고
    • A rotational offset model for 2-stranded F-actin
    • Censullo R., Cheung H. C. A rotational offset model for 2-stranded F-actin. J. Struct. Biol. 110:1993;75-83.
    • (1993) J. Struct. Biol. , vol.110 , pp. 75-83
    • Censullo, R.1    Cheung, H.C.2
  • 17
    • 0027385362 scopus 로고
    • Yeast actin with a mutation in the 'hydrophobic plug' between subdomains 3 and 4 (L266D) displays a cold-sensitive polymerization defect
    • Chen X., Cook R. K., Rubenstein P. A. Yeast actin with a mutation in the 'hydrophobic plug' between subdomains 3 and 4 (L266D) displays a cold-sensitive polymerization defect. J. Cell Biol. 123:1993;1185-1195.
    • (1993) J. Cell Biol. , vol.123 , pp. 1185-1195
    • Chen, X.1    Cook, R.K.2    Rubenstein, P.A.3
  • 18
    • 0027333420 scopus 로고
    • Life at the leading edge - The formation of cell protrusions
    • Condeelis J. Life at the leading edge - The formation of cell protrusions. Annu. Rev. Cell Biol. 9:1993;411-444.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 411-444
    • Condeelis, J.1
  • 19
    • 0020533805 scopus 로고
    • Pyrene actin: Documentation of the validity of a sensitive assay for actin polymerization
    • Copper J. A., Walker S. B., Pollard T. D. Pyrene actin: Documentation of the validity of a sensitive assay for actin polymerization. J. Muscle Res. Cell Motil. 4:1983;253-262.
    • (1983) J. Muscle Res. Cell Motil. , vol.4 , pp. 253-262
    • Copper, J.A.1    Walker, S.B.2    Pollard, T.D.3
  • 21
    • 0027765526 scopus 로고
    • Actin structure and function - Roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site
    • Drubin D. G., Jones H. D., Wertman K. F. Actin structure and function - Roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site. Mol. Biol. Cell. 4:1993;1277-1294.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1277-1294
    • Drubin, D.G.1    Jones, H.D.2    Wertman, K.F.3
  • 22
    • 0025258860 scopus 로고
    • Alteration in crossbridge kinetics caused by mutations in actin
    • Drummond D. R., Pecklham M., Sparrow J. C., White D. C. S. Alteration in crossbridge kinetics caused by mutations in actin. Nature. 348:1990;440-444.
    • (1990) Nature , vol.348 , pp. 440-444
    • Drummond, D.R.1    Pecklham, M.2    Sparrow, J.C.3    White, D.C.S.4
  • 23
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman E. H., Francis N., DeRosier D. F-actin is a helix with a random variable twist. Nature. 298:1982;131-135.
    • (1982) Nature , vol.298 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    Derosier, D.3
  • 24
  • 25
    • 0028787131 scopus 로고
    • Allostery, cooperativity, and different structural states in F-actin
    • Egelman E. H., Orlova A. Allostery, cooperativity, and different structural states in F-actin. J. Struct. Biol. 115:1995b;159-162.
    • (1995) J. Struct. Biol. , vol.115 , pp. 159-162
    • Egelman, E.H.1    Orlova, A.2
  • 26
    • 0021682089 scopus 로고
    • F-actin is intermolecularly crosslinked by N,N′-p-phenylenedimaleimide through lysine 191 and cysteine 374
    • Elzinga M., Phelan J. J. F-actin is intermolecularly crosslinked by N,N′-p-phenylenedimaleimide through lysine 191 and cysteine 374. Proc. Natl. Acad. Sci. USA. 81:1984;6599-6602.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6599-6602
    • Elzinga, M.1    Phelan, J.J.2
  • 27
    • 0027219313 scopus 로고
    • Application of scanning transmission electron microscopy to the study of biological structure
    • Engel A., Colliex C. Application of scanning transmission electron microscopy to the study of biological structure. Curr. Opin. Biotech. 4:1993;403-411.
    • (1993) Curr. Opin. Biotech. , vol.4 , pp. 403-411
    • Engel, A.1    Colliex, C.2
  • 28
    • 0024511257 scopus 로고
    • Co-operativity in protein-protein association: The structure and stability of the actin filament
    • Erickson H. P. Co-operativity in protein-protein association: The structure and stability of the actin filament. J. Mol. Biol. 206:1989;465-474.
    • (1989) J. Mol. Biol. , vol.206 , pp. 465-474
    • Erickson, H.P.1
  • 32
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics - Piconewton forces and nanometer steps
    • Finer J. T., Simmons R. M., Spudich J. A. Single myosin molecule mechanics - Piconewton forces and nanometer steps. Nature. 368:1994;113-119.
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 33
    • 0021403304 scopus 로고
    • Tubular arrays of the actin-DNase I complex induced by gadolinium
    • Fowler W. E., Buhle E. L., Aebi U. Tubular arrays of the actin-DNase I complex induced by gadolinium. Proc. Natl. Acad. Sci. USA. 81:1984;1669-1673.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1669-1673
    • Fowler, W.E.1    Buhle, E.L.2    Aebi, U.3
  • 34
    • 0018347884 scopus 로고
    • Actin heterogeneity in primary embryonic culture cells fromDrosophila melanogaster
    • Fyrberg E. A., Donady J. J. Actin heterogeneity in primary embryonic culture cells fromDrosophila melanogaster. Dev. Biol. 68:1979;487-502.
    • (1979) Dev. Biol. , vol.68 , pp. 487-502
    • Fyrberg, E.A.1    Donady, J.J.2
  • 37
    • 0024709992 scopus 로고
    • The condensation of small oligomers. An alternative pathway of actin filament elongation
    • Grazi E. The condensation of small oligomers. An alternative pathway of actin filament elongation. J. Muscle Res. Cell Motil. 10:1989;275-279.
    • (1989) J. Muscle Res. Cell Motil. , vol.10 , pp. 275-279
    • Grazi, E.1
  • 39
    • 0027134875 scopus 로고
    • The actin monomers in the ternary gelsolin:2 actin complex are in an antiparallel orientation
    • Hesterkamp T., Weeds A. G., Mannherz H. G. The actin monomers in the ternary gelsolin:2 actin complex are in an antiparallel orientation. Eur. J. Biochem. 218:1993;507-513.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 507-513
    • Hesterkamp, T.1    Weeds, A.G.2    Mannherz, H.G.3
  • 40
    • 0028036369 scopus 로고
    • Membrane interactions with the actin cytoskeleton
    • Hitt A. L., Luna E. J. Membrane interactions with the actin cytoskeleton. Curr. Opin. Cell Biol. 6:1994;120-130.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 120-130
    • Hitt, A.L.1    Luna, E.J.2
  • 41
    • 0030249624 scopus 로고    scopus 로고
    • 3-D reconstructions from ice-embedded and negatively stained biomolecular assemblies: A critical comparison
    • Hoenger A., Aebi U. 3-D reconstructions from ice-embedded and negatively stained biomolecular assemblies: A critical comparison. J. Struct. Biol. 117:1996;99-116.
    • (1996) J. Struct. Biol. , vol.117 , pp. 99-116
    • Hoenger, A.1    Aebi, U.2
  • 44
    • 0028882389 scopus 로고
    • Solving the structure of macromolecular complexes with the help of X-ray fiber diffraction diagrams
    • Holmes K. C. Solving the structure of macromolecular complexes with the help of X-ray fiber diffraction diagrams. J. Struct. Biol. 115:1995;151-158.
    • (1995) J. Struct. Biol. , vol.115 , pp. 151-158
    • Holmes, K.C.1
  • 46
    • 0019256032 scopus 로고
    • A novel actin binding protein fromAcanthamoeba
    • Isenberg G., Aebi U., Pollard T. D. A novel actin binding protein fromAcanthamoeba. Nature. 288:1980;455-459.
    • (1980) Nature , vol.288 , pp. 455-459
    • Isenberg, G.1    Aebi, U.2    Pollard, T.D.3
  • 48
    • 0028884013 scopus 로고    scopus 로고
    • Theories of muscle contraction
    • Jontes J. D. Theories of muscle contraction. J. Struct. Biol. 115:1996;119-143.
    • (1996) J. Struct. Biol. , vol.115 , pp. 119-143
    • Jontes, J.D.1
  • 50
    • 0013954606 scopus 로고
    • Optical filtering of electron micrographs: Reconstruction of one-sided images
    • Klug A., DeRosier D. J. Optical filtering of electron micrographs: reconstruction of one-sided images. Nature. 212:1966;29-32.
    • (1966) Nature , vol.212 , pp. 29-32
    • Klug, A.1    Derosier, D.J.2
  • 51
    • 0018162170 scopus 로고
    • P-N,N′-phenylenebismaleimide, a specific crosslinking agent for F-actin
    • Knight P., Offer G. p-N,N′-phenylenebismaleimide, a specific crosslinking agent for F-actin. Biochem. J. 175:1978;1023-1032.
    • (1978) Biochem. J. , vol.175 , pp. 1023-1032
    • Knight, P.1    Offer, G.2
  • 52
    • 0023637721 scopus 로고
    • Actin polymerization and ATP hydrolysis
    • Korn E. D., Carlier M. F., Pantaloni D. Actin polymerization and ATP hydrolysis. Science. 238:1987;638-641.
    • (1987) Science , vol.238 , pp. 638-641
    • Korn, E.D.1    Carlier, M.F.2    Pantaloni, D.3
  • 54
  • 56
    • 0018854688 scopus 로고
    • Expression of a variant form of actin and additional polypeptide changes following chemical-inducedin vitro
    • Leavitt J., Kakunaga T. Expression of a variant form of actin and additional polypeptide changes following chemical-inducedin vitro. J. Biol. Chem. 255:1980;1650-1661.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1650-1661
    • Leavitt, J.1    Kakunaga, T.2
  • 57
    • 0020056174 scopus 로고
    • Variations in expression of mutant β-actin accompanying incremental increases in human fibroblasts tumorigeneicity
    • Leavitt J., Bushar G., Kakunaga T., Hamada H., Hirakawa T., Goldman D., Merril C. Variations in expression of mutant β-actin accompanying incremental increases in human fibroblasts tumorigeneicity. Cell. 28:1982;259-268.
    • (1982) Cell , vol.28 , pp. 259-268
    • Leavitt, J.1    Bushar, G.2    Kakunaga, T.3    Hamada, H.4    Hirakawa, T.5    Goldman, D.6    Merril, C.7
  • 58
    • 0023374630 scopus 로고
    • Expression of transfected mutant β-actin genes: I. Alterations of cell morphology and evidence for autoregulation and aberrant partitioning in actin pools
    • Leavitt J., Ng S.-Y., Aebi U., Varma M., Latter G., Burbeck S., Kedes L., Gunning P. Expression of transfected mutant β-actin genes: I. Alterations of cell morphology and evidence for autoregulation and aberrant partitioning in actin pools. Mol. Cell Biol. 7:1987;2457-2466.
    • (1987) Mol. Cell Biol. , vol.7 , pp. 2457-2466
    • Leavitt, J.1    Ng, S.-Y.2    Aebi, U.3    Varma, M.4    Latter, G.5    Burbeck, S.6    Kedes, L.7    Gunning, P.8
  • 59
    • 0028024049 scopus 로고
    • Small angle X-ray scattering and electron cryomicroscopy study of actin filaments: Role of the bound nucleotide in the structure of F-actin
    • Lepault J., Ranck J. L., Erk I., Carlier M. F. Small angle X-ray scattering and electron cryomicroscopy study of actin filaments: Role of the bound nucleotide in the structure of F-actin. J. Struct. Biol. 112:1994;79-91.
    • (1994) J. Struct. Biol. , vol.112 , pp. 79-91
    • Lepault, J.1    Ranck, J.L.2    Erk, I.3    Carlier, M.F.4
  • 60
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz M., Popp D., Holmes K. C. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234:1993;826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 61
    • 0028940312 scopus 로고
    • An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosin gels
    • Lorenz M., Poole K. J. V., Popp D., Rosenbaum G., Holmes K. C. An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosin gels. J. Mol. Biol. 246:1995;108-119.
    • (1995) J. Mol. Biol. , vol.246 , pp. 108-119
    • Lorenz, M.1    Poole, K.J.V.2    Popp, D.3    Rosenbaum, G.4    Holmes, K.C.5
  • 62
    • 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. Function of skeletal muscle myosin heavy and light chain isoforms by an in vitro motility assay. J. Biol. Chem. 268:1993a;20414-20418.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20414-20418
    • Lowey, S.1    Waller, G.S.2    Trybus, K.M.3
  • 63
    • 0027426228 scopus 로고
    • Skeletal muscle myosin light chains are essential for physiological speeds of shortening
    • Lowey S., Waller G. S., Trybus K. M. Skeletal muscle myosin light chains are essential for physiological speeds of shortening. Nature. 365:1993b;454-456.
    • (1993) Nature , vol.365 , pp. 454-456
    • Lowey, S.1    Waller, G.S.2    Trybus, K.M.3
  • 64
    • 0026340941 scopus 로고
    • Characterization of actin filament severing by actophorin fromAcanthamoeba castellanii
    • Maciver S. K., Zot H. G., Pollard T. Characterization of actin filament severing by actophorin fromAcanthamoeba castellanii. J. Cell Biol. 115:1991;1611-1620.
    • (1991) J. Cell Biol. , vol.115 , pp. 1611-1620
    • MacIver, S.K.1    Zot, H.G.2    Pollard, T.3
  • 65
    • 0017330116 scopus 로고
    • Crystals of skeletal muscle actin:pancreatic DNase I complex
    • Mannherz H. G., Kabsch W., Leverman R. Crystals of skeletal muscle actin:pancreatic DNase I complex. FEBS Lett. 73:1977;141-143.
    • (1977) FEBS Lett. , vol.73 , pp. 141-143
    • Mannherz, H.G.1    Kabsch, W.2    Leverman, R.3
  • 67
    • 0023198601 scopus 로고
    • Synchroton X-ray diffraction studies of actin structure during polymerization
    • Matsudaira P., Bordas J., Koch M. H. J. Synchroton X-ray diffraction studies of actin structure during polymerization. Proc. Natl. Acad. Sci. USA. 84:1987;3151-3155.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3151-3155
    • Matsudaira, P.1    Bordas, J.2    Koch, M.H.J.3
  • 68
    • 0026034515 scopus 로고
    • Modular organization of actin crosslinking proteins
    • Matsudaira P. Modular organization of actin crosslinking proteins. Trends Biochem. Sci. 16:1991;87-92.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 87-92
    • Matsudaira, P.1
  • 69
    • 0028176006 scopus 로고
    • Determination of the α-actinin-binding site on actin filaments by cryo-electron microscopy and image analysis
    • McGough A., Way M., DeRosier D. Determination of the α-actinin-binding site on actin filaments by cryo-electron microscopy and image analysis. J. Cell Biol. 126:1994;433-443.
    • (1994) J. Cell Biol. , vol.126 , pp. 433-443
    • McGough, A.1    Way, M.2    Derosier, D.3
  • 70
    • 0028863184 scopus 로고
    • Molecular model of an actin filament capped by a severing protein
    • McGough A., Way M. Molecular model of an actin filament capped by a severing protein. J. Struct. Biol. 115:1995;144-150.
    • (1995) J. Struct. Biol. , vol.115 , pp. 144-150
    • McGough, A.1    Way, M.2
  • 71
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin P. J., Gooch J. T., Mannherz H. G., Weeds A. G. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature. 364:1993;685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.G.3    Weeds, A.G.4
  • 72
    • 0025339009 scopus 로고
    • Bundling of actin filaments by α-actinin depends on its molecular length
    • Meyer R. K., Aebi U. Bundling of actin filaments by α-actinin depends on its molecular length. J. Cell Biol. 110:1990;2013-2024.
    • (1990) J. Cell Biol. , vol.110 , pp. 2013-2024
    • Meyer, R.K.1    Aebi, U.2
  • 73
    • 0025052483 scopus 로고
    • Molecular structure of F-actin and location of surface binding sites
    • Milligan R. A., Whittaker M., Safer D. Molecular structure of F-actin and location of surface binding sites. Nature. 348:1990;217-221.
    • (1990) Nature , vol.348 , pp. 217-221
    • Milligan, R.A.1    Whittaker, M.2    Safer, D.3
  • 74
    • 0023840623 scopus 로고
    • Probing actin polymerization by intermolecular cross-linking
    • Millonig R., Salvo H., Aebi U. Probing actin polymerization by intermolecular cross-linking. J. Cell Biol. 106:1988;785-796.
    • (1988) J. Cell Biol. , vol.106 , pp. 785-796
    • Millonig, R.1    Salvo, H.2    Aebi, U.3
  • 75
    • 0014945041 scopus 로고
    • Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments
    • Moore P. B., Huxley H. E., DeRosier D. J. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J. Mol. Biol. 50:1970;279-295.
    • (1970) J. Mol. Biol. , vol.50 , pp. 279-295
    • Moore, P.B.1    Huxley, H.E.2    Derosier, D.J.3
  • 76
    • 0028228518 scopus 로고
    • Dynamic properties of actin - Structural changes induced by beryllium fluoride
    • Muhlrad A., Cheung P., Phan B. C., Miller C., Reisler E. Dynamic properties of actin - structural changes induced by beryllium fluoride. J. Biol. Chem. 269:1994;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
  • 77
    • 0021985484 scopus 로고
    • Presence of oligomers at subcritical actin concentrations
    • Newman J., Estes J. E., Selden L. A., Gershman L. C. Presence of oligomers at subcritical actin concentrations. Biochemistry. 24:1985;1538-1544.
    • (1985) Biochemistry , vol.24 , pp. 1538-1544
    • Newman, J.1    Estes, J.E.2    Selden, L.A.3    Gershman, L.C.4
  • 78
    • 0027258216 scopus 로고
    • Physical chemistry of actin - Past, present and future
    • Oosawa F. Physical chemistry of actin - Past, present and future. Biophys. Chem. 47:1993;101-111.
    • (1993) Biophys. Chem. , vol.47 , pp. 101-111
    • Oosawa, F.1
  • 79
    • 0026437417 scopus 로고
    • Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis
    • Orlova A., Egelman E. H. Structural basis for the destabilization of F-actin by phosphate release following ATP hydrolysis. J. Mol. Biol. 227:1992;1043-1053.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1043-1053
    • Orlova, A.1    Egelman, E.H.2
  • 80
    • 0027328612 scopus 로고
    • A conformational change in the actin subunit can change the flexibility of the actin filament
    • Orlova A., Egelman E. H. A conformational change in the actin subunit can change the flexibility of the actin filament. J. Mol. Biol. 232:1993;334-341.
    • (1993) J. Mol. Biol. , vol.232 , pp. 334-341
    • Orlova, A.1    Egelman, E.H.2
  • 81
    • 0028907435 scopus 로고
    • Structural dynamics of F-actin: I. Changes in the C terminus
    • Orlova A., Egelman E. H. Structural dynamics of F-actin: I. Changes in the C terminus. J. Mol. Biol. 245:1995;582-597.
    • (1995) J. Mol. Biol. , vol.245 , pp. 582-597
    • Orlova, A.1    Egelman, E.H.2
  • 82
    • 0028920157 scopus 로고
    • Structural dynamics of F-actin: II. cooperativity in structural transitions
    • Orlova A., Prochniewicz E., Egelman E. H. Structural dynamics of F-actin: II. cooperativity in structural transitions. J. Mol. Biol. 245:1995;598-607.
    • (1995) J. Mol. Biol. , vol.245 , pp. 598-607
    • Orlova, A.1    Prochniewicz, E.2    Egelman, E.H.3
  • 83
    • 0027340549 scopus 로고
    • A 13-Å map of the actin-scruin filament from theLimulus
    • Owen C., DeRosier D. A 13-Å map of the actin-scruin filament from theLimulus. J. Cell Biol. 123:1993;337-344.
    • (1993) J. Cell Biol. , vol.123 , pp. 337-344
    • Owen, C.1    Derosier, D.2
  • 85
    • 0021105144 scopus 로고
    • Measurement of rate constants of actin filament elongation in solution
    • Pollard T. D. Measurement of rate constants of actin filament elongation in solution. Anal. Biochem. 134:1983;406-412.
    • (1983) Anal. Biochem. , vol.134 , pp. 406-412
    • Pollard, T.D.1
  • 86
    • 0021200245 scopus 로고
    • Polymerization of ADP-actin
    • Pollard T. D. Polymerization of ADP-actin. J. Cell Biol. 99:1984;769-777.
    • (1984) J. Cell Biol. , vol.99 , pp. 769-777
    • Pollard, T.D.1
  • 87
    • 0021259215 scopus 로고
    • The rate constant for ATP hydrolysis by polymerized actin
    • Pollard T. D., Weeds A. G. The rate constant for ATP hydrolysis by polymerized actin. FEBS Lett. 170:1984;94-98.
    • (1984) FEBS Lett. , vol.170 , pp. 94-98
    • Pollard, T.D.1    Weeds, A.G.2
  • 88
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins. A critical evaluation of mechanisms and functions
    • Pollard T. D., Cooper J. A. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu. Rev. Biochem. 55:1986;987-1035.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 89
    • 0022437077 scopus 로고
    • Assembly and dynamics of the actin filament system in non-muscle cells
    • Pollard T. D. Assembly and dynamics of the actin filament system in non-muscle cells. J. Cell Biochem. 31:1986;87-95.
    • (1986) J. Cell Biochem. , vol.31 , pp. 87-95
    • Pollard, T.D.1
  • 91
    • 0025685506 scopus 로고
    • Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility
    • Prochniewicz E., Yanagida T. Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility. J. Mol. Biol. 216:1990;761-772.
    • (1990) J. Mol. Biol. , vol.216 , pp. 761-772
    • Prochniewicz, E.1    Yanagida, T.2
  • 92
    • 0030564835 scopus 로고    scopus 로고
    • Cooperativity in F-actin: Binding of gelsolin at the barbed end affects structure and dynamics of the whole filament
    • Prochniewicz E., Zhang Q., Janmey P. A., Thomas D. D. Cooperativity in F-actin: Binding of gelsolin at the barbed end affects structure and dynamics of the whole filament. J. Mol. Biol. 260:1996;756-766.
    • (1996) J. Mol. Biol. , vol.260 , pp. 756-766
    • Prochniewicz, E.1    Zhang, Q.2    Janmey, P.A.3    Thomas, D.D.4
  • 96
    • 0025735407 scopus 로고
    • Heat shock gene activation by mutant actin is independent of myofibril degeneration inDrosophila
    • Sakai Y., Okamoto H., Mogami K., Matsuo H., Hotta Y. Heat shock gene activation by mutant actin is independent of myofibril degeneration inDrosophila. J. Biochem. Tokyo. 109:1991;670-673.
    • (1991) J. Biochem. Tokyo , vol.109 , pp. 670-673
    • Sakai, Y.1    Okamoto, H.2    Mogami, K.3    Matsuo, H.4    Hotta, Y.5
  • 100
    • 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. Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin. J. Cell Biol. 111:1990;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
  • 102
    • 0024185459 scopus 로고
    • The actin cytoskeleton
    • Small J. V. The actin cytoskeleton. Electron Microsc. Rev. 1:1988;155-174.
    • (1988) Electron Microsc. Rev. , vol.1 , pp. 155-174
    • Small, J.V.1
  • 104
    • 0029000811 scopus 로고
    • Actin filament organization in the fish keratocyte lamellipodium
    • Small J. V., Herzog M., Anderson K. Actin filament organization in the fish keratocyte lamellipodium. J. Cell Biol. 129:1995;1275-1286.
    • (1995) J. Cell Biol. , vol.129 , pp. 1275-1286
    • Small, J.V.1    Herzog, M.2    Anderson, K.3
  • 105
    • 0001521247 scopus 로고
    • Computer-generated Fourier transforms of helical particles
    • Smith P. R., Aebi U. Computer-generated Fourier transforms of helical particles. J. Phys. A: Math Gen. 7:1974;1627-1633.
    • (1974) J. Phys. A: Math Gen. , vol.7 , pp. 1627-1633
    • Smith, P.R.1    Aebi, U.2
  • 106
    • 0021095473 scopus 로고
    • Structure of the actin molecule determined from electron micrographs of crystalline actin sheets with a tentative alignment of the molecule in the actin filament
    • Smith P. R., Fowler W. E., Pollard T. D., Aebi U. Structure of the actin molecule determined from electron micrographs of crystalline actin sheets with a tentative alignment of the molecule in the actin filament. J. Mol. Biol. 167:1983;641-660.
    • (1983) J. Mol. Biol. , vol.167 , pp. 641-660
    • Smith, P.R.1    Fowler, W.E.2    Pollard, T.D.3    Aebi, U.4
  • 107
    • 0028674872 scopus 로고
    • Dynamic remodeling of the actin cytoskeleton: Lessons fromListeria
    • Southwick F. S., Purich D. L. Dynamic remodeling of the actin cytoskeleton: Lessons fromListeria. Bioassays. 16:1994;885-891.
    • (1994) Bioassays , vol.16 , pp. 885-891
    • Southwick, F.S.1    Purich, D.L.2
  • 109
    • 0028907624 scopus 로고
    • Muscle - Flight and phosphorylation
    • Sparrow J. C. Muscle - Flight and phosphorylation. Nature. 374:1995;592-593.
    • (1995) Nature , vol.374 , pp. 592-593
    • Sparrow, J.C.1
  • 110
    • 0030804033 scopus 로고    scopus 로고
    • A correlative analysis of actin filament assembly, structure and dynamics
    • Steinmetz M., Goldie K. N., Aebi U. A correlative analysis of actin filament assembly, structure and dynamics. J. Cell Biol. 1997.
    • (1997) J. Cell Biol.
    • Steinmetz, M.1    Goldie, K.N.2    Aebi, U.3
  • 111
    • 0023252082 scopus 로고
    • The variable twist of actin and its modulation by actin-binding proteins
    • Stokes D. L., DeRosier D. The variable twist of actin and its modulation by actin-binding proteins. J. Cell Biol. 104:1987;1005-1017.
    • (1987) J. Cell Biol. , vol.104 , pp. 1005-1017
    • Stokes, D.L.1    Derosier, D.2
  • 112
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel T. P. On the crawling of animal cells. Science. 260:1993;1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 113
    • 0023947166 scopus 로고
    • Deficient polymerization in vitro of a point-mutated β-actin expressed in a human fibroblast cell line
    • Taniguchi S., Sagara J., Kakunaga T. Deficient polymerization in vitro of a point-mutated β-actin expressed in a human fibroblast cell line. J. Biochem. 103:1988;707-713.
    • (1988) J. Biochem. , vol.103 , pp. 707-713
    • Taniguchi, S.1    Sagara, J.2    Kakunaga, T.3
  • 114
    • 0021176612 scopus 로고
    • 3-D reconstruction of rigor insect flight muscle from tilted thin sections
    • Taylor K. A., Reedy M. C., Cordova L., Reedy M. K. 3-D reconstruction of rigor insect flight muscle from tilted thin sections. Nature. 310:1984;285-291.
    • (1984) Nature , vol.310 , pp. 285-291
    • Taylor, K.A.1    Reedy, M.C.2    Cordova, L.3    Reedy, M.K.4
  • 115
    • 0018885271 scopus 로고
    • Vegetativedictyostelium
    • Vanderkerckhove J., Weber K. Vegetativedictyostelium. Nature. 284:1980;475-479.
    • (1980) Nature , vol.284 , pp. 475-479
    • Vanderkerckhove, J.1    Weber, K.2
  • 117
    • 0025643464 scopus 로고
    • Ultramicrotomy of biological objects: From the beginning to the present
    • Villiger W., Bremer A. Ultramicrotomy of biological objects: from the beginning to the present. J. Struct. Biol. 104:1990;178-188.
    • (1990) J. Struct. Biol. , vol.104 , pp. 178-188
    • Villiger, W.1    Bremer, A.2
  • 118
    • 0025366382 scopus 로고
    • Actin-binding proteins. Cytoskeletal ups and downs
    • Way M., Weeds A. Actin-binding proteins. Cytoskeletal ups and downs. Nature. 344:1990;292-294.
    • (1990) Nature , vol.344 , pp. 292-294
    • Way, M.1    Weeds, A.2
  • 119
    • 0017176529 scopus 로고
    • Head to tail polymerization of actin
    • Wegner A. Head to tail polymerization of actin. J. Mol. Biol. 108:1976;139-150.
    • (1976) J. Mol. Biol. , vol.108 , pp. 139-150
    • Wegner, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.