메뉴 건너뛰기




Volumn 2, Issue 2, 2006, Pages 83-86

Dynamic polymorphism of single actin molecules in the actin filament

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; MOLECULAR MOTOR; MYOSIN; MYOSIN V;

EID: 33644897629     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio763     Document Type: Article
Times cited : (81)

References (28)
  • 1
    • 3943052117 scopus 로고    scopus 로고
    • Crawling toward a unified model of cell mobility: Spatial and temporal regulation of actin dynamics
    • Rafelski, S.M. & Theriot, J.A. Crawling toward a unified model of cell mobility: spatial and temporal regulation of actin dynamics. Annu. Rev. Biochem. 73, 209-239 (2004).
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 209-239
    • Rafelski, S.M.1    Theriot, J.A.2
  • 2
  • 3
    • 0021261156 scopus 로고
    • Direct observation of motion of single F-actin filaments in the presence of myosin
    • Yanagida, T., Nakase, M., Nishiyama, K. & Oosawa, F. Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 307, 58-60 (1984).
    • (1984) Nature , vol.307 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4
  • 4
    • 85047699197 scopus 로고    scopus 로고
    • Active fluidization of polymer networks through molecular motors
    • Humphrey, D., Duggan, C., Saha, D., Smith, D. & Kas, J. Active fluidization of polymer networks through molecular motors. Nature 416, 413-416 (2002).
    • (2002) Nature , vol.416 , pp. 413-416
    • Humphrey, D.1    Duggan, C.2    Saha, D.3    Smith, D.4    Kas, J.5
  • 5
    • 0033548686 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of single biomolecules
    • Weiss, S. Fluorescence spectroscopy of single biomolecules. Science 283, 1676-1683 (1999).
    • (1999) Science , vol.283 , pp. 1676-1683
    • Weiss, S.1
  • 6
    • 0033413080 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution
    • Ishii, Y., Yoshida, T., Funatsu, T., Wazawa, T. & Yanagida, T. Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution. Chem. Phys. 247, 163-173 (1999).
    • (1999) Chem. Phys. , vol.247 , pp. 163-173
    • Ishii, Y.1    Yoshida, T.2    Funatsu, T.3    Wazawa, T.4    Yanagida, T.5
  • 7
    • 0037057630 scopus 로고    scopus 로고
    • Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase
    • Ha, T. et al. Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase. Nature 419, 638-641 (2002).
    • (2002) Nature , vol.419 , pp. 638-641
    • Ha, T.1
  • 8
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
    • Funatsu, T., Harada, Y., Tokunaga, M., Saito, K. & Yanagida, T. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374, 555-559 (1995).
    • (1995) Nature , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 9
    • 0025685506 scopus 로고
    • Inhibition of sliding movement of F-actin by cross-linking emphasizes the role of actin structure in the mechanism of motility
    • Prochniewicz, E. & Yanagida, T. Inhibition of sliding movement of F-actin by cross-linking emphasizes the role of actin structure in the mechanism of motility. J. Mol. Biol. 216, 761-772 (1990).
    • (1990) J. Mol. Biol. , vol.216 , pp. 761-772
    • Prochniewicz, E.1    Yanagida, T.2
  • 10
    • 0028077728 scopus 로고
    • Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: Effect of phalloidin on polymer assembly
    • Moens, P.D., Yee, D.J. & dos Remedios, C.G. Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: effect of phalloidin on polymer assembly. Biochemistry 33, 13102-13108 (1994).
    • (1994) Biochemistry , vol.33 , pp. 13102-13108
    • Moens, P.D.1    Yee, D.J.2    Dos Remedios, C.G.3
  • 11
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall, V., Post, P.L. & Mooseker, M.S. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science 279, 527-533 (1998).
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 12
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein, L.R., Graceffa, P. & Dominguez, R. The crystal structure of uncomplexed actin in the ADP state. Science 293, 708-711 (2001).
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 13
    • 0037006805 scopus 로고    scopus 로고
    • A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure
    • Galkin, V.E., VanLoock, M.S., Orlova, A. & Egelman, E.H. A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure. Curr. Biol. 12, 570-575 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 570-575
    • Galkin, V.E.1    VanLoock, M.S.2    Orlova, A.3    Egelman, E.H.4
  • 14
    • 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, 582-597 (1995).
    • (1995) J. Mol. Biol. , vol.245 , pp. 582-597
    • Orlova, A.1    Egelman, E.H.2
  • 15
    • 0030988670 scopus 로고    scopus 로고
    • A conformational change in F-actin when myosin binds: Fluorescence resonance energy transfer detects an increase in the radial coordinate of Cys-374
    • Moens, P.D. & dos Remedios, C.G. A conformational change in F-actin when myosin binds: fluorescence resonance energy transfer detects an increase in the radial coordinate of Cys-374. Biochemistry 36, 7353-7360 (1997).
    • (1997) Biochemistry , vol.36 , pp. 7353-7360
    • Moens, P.D.1    Dos Remedios, C.G.2
  • 16
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough, A., Pope, B., Chiu, W. & Weeds, A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138, 771-781 (1997).
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 17
    • 0020477574 scopus 로고
    • F-actin is a helix with a random variable twist
    • Egelman, E.H., Francis, N. & DeRosier, D.J. F-actin is a helix with a random variable twist. Nature 298, 131-135 (1982).
    • (1982) Nature , vol.298 , pp. 131-135
    • Egelman, E.H.1    Francis, N.2    DeRosier, D.J.3
  • 19
    • 0028093176 scopus 로고
    • Microsecond rotational dynamics of F-actin in ActoS1 filaments during ATP hydrolysis
    • Ng, C.M. & Ludescher, R.D. Microsecond rotational dynamics of F-actin in ActoS1 filaments during ATP hydrolysis. Biochemistry 33, 9098-9104 (1994).
    • (1994) Biochemistry , vol.33 , pp. 9098-9104
    • Ng, C.M.1    Ludescher, R.D.2
  • 20
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
    • Harada, Y., Sakurada, K., Aoki, T., Thomas, D.D. & Yanagida, T. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 216, 49-68 (1990).
    • (1990) J. Mol. Biol. , vol.216 , pp. 49-68
    • Harada, Y.1    Sakurada, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 21
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution-a 60-year-old hypothesis revisited
    • James, L.C. & Tawfik, D.S. Conformational diversity and protein evolution-a 60-year-old hypothesis revisited. Trends. Biochem. Sci. 28, 361-368 (2003).
    • (2003) Trends. Biochem. Sci. , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 22
    • 0030818825 scopus 로고    scopus 로고
    • Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein
    • Ito, Y. et al. Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein. Biochemistry 36, 9109-9119 (1997).
    • (1997) Biochemistry , vol.36 , pp. 9109-9119
    • Ito, Y.1
  • 23
    • 27744499156 scopus 로고    scopus 로고
    • Intrinsic dynamics of an enzyme underlies catalysis
    • Eisenmesser, E.Z. et al. Intrinsic dynamics of an enzyme underlies catalysis. Nature 438, 117-121 (2005).
    • (2005) Nature , vol.438 , pp. 117-121
    • Eisenmesser, E.Z.1
  • 25
    • 0023834388 scopus 로고
    • A novel actin label: A fluorescent probe at glutamine-41 and its consequences
    • Takashi, R. A novel actin label: a fluorescent probe at glutamine-41 and its consequences. Biochemistry 27, 938-943 (1988).
    • (1988) Biochemistry , vol.27 , pp. 938-943
    • Takashi, R.1
  • 26
    • 0035939958 scopus 로고    scopus 로고
    • The core of the motor domain determines the direction of myosin movement
    • Homma, K., Yoshimura, M., Saito, J., Ikebe, R. & Ikebe, M. The core of the motor domain determines the direction of myosin movement. Nature 412, 831-834 (2001).
    • (2001) Nature , vol.412 , pp. 831-834
    • Homma, K.1    Yoshimura, M.2    Saito, J.3    Ikebe, R.4    Ikebe, M.5
  • 28
    • 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. The structure of the acto-myosin subfragment 1 complex: results of searches using data from electron microscopy and x-ray crystallography. PNAS 94, 8533-8538 (1997).
    • (1997) PNAS , vol.94 , pp. 8533-8538
    • Mendelson, R.1    Morris, E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.