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Volumn 45, Issue 2, 2006, Pages 195-201

Evaluating spatial constraints in cellular assembly processes using a Monte Carlo approach

Author keywords

Actin; Biochemical polymerization; Cell macromolecular crowding; Computer models; Monte Carlo

Indexed keywords

POLYMER;

EID: 33745712035     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:45:2:195     Document Type: Article
Times cited : (8)

References (37)
  • 1
    • 0020639256 scopus 로고
    • Changes in cell shape and actin distribution induced by constant electric fields
    • Luther, P. W., Peng, H. B., and Lin, J. J. (1983) Changes in cell shape and actin distribution induced by constant electric fields. Nature 303, 61-64.
    • (1983) Nature , vol.303 , pp. 61-64
    • Luther, P.W.1    Peng, H.B.2    Lin, J.J.3
  • 2
    • 0035997133 scopus 로고    scopus 로고
    • Buckling of actin stress fibers: A new wrinkle in the cytoskeletal tapestry
    • Costa, K. D., Hucker, W. J., and Yin, F. C. (2002) Buckling of actin stress fibers: a new wrinkle in the cytoskeletal tapestry. Cell Motil. Cytoskeleton 52, 266-274.
    • (2002) Cell Motil. Cytoskeleton , vol.52 , pp. 266-274
    • Costa, K.D.1    Hucker, W.J.2    Yin, F.C.3
  • 4
    • 0031048791 scopus 로고    scopus 로고
    • Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
    • Amano, M., Chihara, K., Kimura, K., et al. (1997) Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. Science 275, 1308-1311.
    • (1997) Science , vol.275 , pp. 1308-1311
    • Amano, M.1    Chihara, K.2    Kimura, K.3
  • 5
    • 0037026491 scopus 로고    scopus 로고
    • Cell biology: Spinning actin to divide
    • Narumiya, S. and Mabuchi, I. (2002) Cell biology: spinning actin to divide. Nature 419, 27-28.
    • (2002) Nature , vol.419 , pp. 27-28
    • Narumiya, S.1    Mabuchi, I.2
  • 6
    • 0033529620 scopus 로고    scopus 로고
    • Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase
    • Maekawa, M., Ishizaki, T., Boku, S., et al. (1999) Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285, 895-898.
    • (1999) Science , vol.285 , pp. 895-898
    • Maekawa, M.1    Ishizaki, T.2    Boku, S.3
  • 7
    • 0034896467 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of actin filament nucleation
    • Sept, M. and McCammon J. A. (2001) Thermodynamics and kinetics of actin filament nucleation. Biophys. J. 81, 667-674.
    • (2001) Biophys. J. , vol.81 , pp. 667-674
    • Sept, M.1    McCammon, J.A.2
  • 8
    • 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
  • 9
    • 0025970527 scopus 로고
    • Actin protein structure and filament dynamics
    • Carlier, M. F. (1991) Actin protein structure and filament dynamics. J. Biol. Chem. 266, 1-4.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1-4
    • Carlier, M.F.1
  • 10
    • 33745686923 scopus 로고    scopus 로고
    • Cooperative symmetry breaking by actin filament polymerization in a model for cell motility
    • van Oudenaarden, A. and Theriot, J. A. (2000) Cooperative symmetry breaking by actin filament polymerization in a model for cell motility. Biophys. J. 78, 1421 POS Part 2.
    • (2000) Biophys. J. , vol.78 , Issue.2 POS PART , pp. 1421
    • Van Oudenaarden, A.1    Theriot, J.A.2
  • 11
    • 0028921185 scopus 로고
    • Kinetic model for the inhibition of actin polymerization by actobindin
    • Bubb, M. R. and Korn, E. D. (1995) Kinetic model for the inhibition of actin polymerization by actobindin. Biochemistry 34, 3921-3926.
    • (1995) Biochemistry , vol.34 , pp. 3921-3926
    • Bubb, M.R.1    Korn, E.D.2
  • 13
    • 0033579419 scopus 로고    scopus 로고
    • Computer simulations of actin polymerization can explain the barbed-pointed end asymmetry
    • Sept, M., Elcock, A., and McCammon, J. (1999) Computer simulations of actin polymerization can explain the barbed-pointed end asymmetry. J. Mol. Biol. 294, 1181-1189.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1181-1189
    • Sept, M.1    Elcock, A.2    McCammon, J.3
  • 14
    • 0023190718 scopus 로고
    • The dynamics of free calcium in dendritic spines in response to repetitive synaptic input
    • Gamble, E. and Koch, C. (1987) The dynamics of free calcium in dendritic spines in response to repetitive synaptic input. Science 236, 1311-1315.
    • (1987) Science , vol.236 , pp. 1311-1315
    • Gamble, E.1    Koch, C.2
  • 15
    • 0025014719 scopus 로고
    • Subcellular calcium transients visualized by confocal microscopy in a voltage-clamped vertebrate neuron
    • Hernandez-Cruz, A., Sala, F., and Adams, P. R. (1990) Subcellular calcium transients visualized by confocal microscopy in a voltage-clamped vertebrate neuron. Science 247, 858-862.
    • (1990) Science , vol.247 , pp. 858-862
    • Hernandez-Cruz, A.1    Sala, F.2    Adams, P.R.3
  • 17
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton, A. P. (2001) The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J. Biol. Chem. 276, 10,577-10,580.
    • (2001) J. Biol. Chem. , vol.276
    • Minton, A.P.1
  • 18
    • 0037008414 scopus 로고    scopus 로고
    • On the role of the macromolecular phase transitions in biology in response to change in solution volume or macromolecular composition: Action as an entropy buffer
    • Hall, D. (2002) On the role of the macromolecular phase transitions in biology in response to change in solution volume or macromolecular composition: action as an entropy buffer. Biophys. Chem. 98, 233-248.
    • (2002) Biophys. Chem. , vol.98 , pp. 233-248
    • Hall, D.1
  • 19
    • 0141889980 scopus 로고    scopus 로고
    • Cell biology. How cells step out
    • Marx, J. (2003) Cell biology. How cells step out. Science 302, 214-216.
    • (2003) Science , vol.302 , pp. 214-216
    • Marx, J.1
  • 20
    • 0033587619 scopus 로고    scopus 로고
    • Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: Theory, experiment, and biological significance
    • Rivas, G., Fernandez, J. A., and Minton, A. P. Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: theory, experiment, and biological significance. (1999) Biochemistry 38, 9379-9388.
    • (1999) Biochemistry , vol.38 , pp. 9379-9388
    • Rivas, G.1    Fernandez, J.A.2    Minton, A.P.3
  • 21
    • 0030981013 scopus 로고    scopus 로고
    • Macromolecular crowding: Effects on actin polymerisation
    • Lindner, R. A. and Raison, G. B. (1997) Macromolecular crowding: effects on actin polymerisation. Biophys. Chem. 66, 57-66.
    • (1997) Biophys. Chem. , vol.66 , pp. 57-66
    • Lindner, R.A.1    Raison, G.B.2
  • 22
    • 0029064234 scopus 로고
    • Cytoskeletal filament assembly and the control of cell spreading and function by extracellular matrix
    • Mooney D. J., Langer, R., and Ingber, D. E. (1995) Cytoskeletal filament assembly and the control of cell spreading and function by extracellular matrix. J. Cell Sci. 108, 2311-2320.
    • (1995) J. Cell Sci. , vol.108 , pp. 2311-2320
    • Mooney, D.J.1    Langer, R.2    Ingber, D.E.3
  • 23
    • 0033542474 scopus 로고    scopus 로고
    • Dynamics of individual flexible polymers in a shear flow
    • LeDuc, P., Haber, C., Bao, G., and Wirtz, D. (1999) Dynamics of individual flexible polymers in a shear flow. Nature 399, 564-566.
    • (1999) Nature , vol.399 , pp. 564-566
    • Leduc, P.1    Haber, C.2    Bao, G.3    Wirtz, D.4
  • 24
    • 0020440730 scopus 로고
    • A comparison of K-562 and HL-60 human leukemic cell surface membrane proteins by two-dimensional electrophoresis
    • Felsted, R. L. and Gupta, S. K. (1982) A comparison of K-562 and HL-60 human leukemic cell surface membrane proteins by two-dimensional electrophoresis. J. Biol. Chem. 257, 13,211-13,117.
    • (1982) J. Biol. Chem. , vol.257
    • Felsted, R.L.1    Gupta, S.K.2
  • 25
    • 0035228621 scopus 로고    scopus 로고
    • Three-dimensional extracellular matrix substrates for cell culture
    • Voytik-Harbin, S. L. (2001) Three-dimensional extracellular matrix substrates for cell culture. Methods Cell. Biol. 63, 561-581.
    • (2001) Methods Cell. Biol. , vol.63 , pp. 561-581
    • Voytik-Harbin, S.L.1
  • 26
    • 0033952145 scopus 로고    scopus 로고
    • The biology of cell locomotion within three-dimensional extracellular matrix
    • Friedl, P. and Brocker, E. B. (2000) The biology of cell locomotion within three-dimensional extracellular matrix. Cell. Mol. Life Sci. 57, 41-64.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 41-64
    • Friedl, P.1    Brocker, E.B.2
  • 30
    • 0027216184 scopus 로고
    • Cellular automaton model of the actin cytoskeleton
    • Dufort, P. and Lumsden, C. (1993) Cellular automaton model of the actin cytoskeleton. Cell. Motil. Cytoskeleton 25, 87-104.
    • (1993) Cell. Motil. Cytoskeleton , vol.25 , pp. 87-104
    • Dufort, P.1    Lumsden, C.2
  • 31
    • 0036789480 scopus 로고    scopus 로고
    • Monte carlo simulations of enzyme reactions in two dimensions: Fractal kinetics and spatial segregation
    • Berry, H. (2002) Monte carlo simulations of enzyme reactions in two dimensions: fractal kinetics and spatial segregation. Biophys. J. 83, 1891-1901.
    • (2002) Biophys. J. , vol.83 , pp. 1891-1901
    • Berry, H.1
  • 33
    • 0026322417 scopus 로고
    • Stabilization of actin by phalloidin: A differential scanning calorimetric study
    • Le Bihan, T. and Gicquaud, C. (1991) Stabilization of actin by phalloidin: a differential scanning calorimetric study. Biochem. Biophys. Res. Commun. 181, 542-547.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 542-547
    • Le Bihan, T.1    Gicquaud, C.2
  • 34
    • 0032077675 scopus 로고    scopus 로고
    • Models for the length distributions of actin filaments: I. Simple polymerization and fragmentation
    • Edelstein-Keshet, L. and Ermentrout, G. B. (1998) Models for the length distributions of actin filaments: I. Simple polymerization and fragmentation. Bull. Math. Biol. 60, 449-475.
    • (1998) Bull. Math. Biol. , vol.60 , pp. 449-475
    • Edelstein-Keshet, L.1    Ermentrout, G.B.2
  • 35
    • 0032030413 scopus 로고    scopus 로고
    • Testing a model for the dynamics of actin structures with biological parameter values
    • Spiros, A., and Edelstein-Keshet, L. (1998) Testing a model for the dynamics of actin structures with biological parameter values. Bull. Math. Biol. 60, 275-305.
    • (1998) Bull. Math. Biol. , vol.60 , pp. 275-305
    • Spiros, A.1    Edelstein-Keshet, L.2
  • 36
    • 0020184671 scopus 로고
    • How crowded is the cytoplasm?
    • Fulton, A. B. (1982) How crowded is the cytoplasm? Cell 30, 345-347.
    • (1982) Cell , vol.30 , pp. 345-347
    • Fulton, A.B.1
  • 37
    • 33645151225 scopus 로고    scopus 로고
    • Understanding actin organization in cell structure through lattice based Monte Carlo simulation
    • Puskar, K., Apeltsin, L., Ta'asan, S., Schwartz, R., and LeDuc, P. R. (2004) Understanding actin organization in cell structure through lattice based Monte Carlo simulation. Mech. Chem. Biosys. 1, 123-131.
    • (2004) Mech. Chem. Biosys. , vol.1 , pp. 123-131
    • Puskar, K.1    Apeltsin, L.2    Ta'asan, S.3    Schwartz, R.4    Leduc, P.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.