메뉴 건너뛰기




Volumn 69, Issue 2, 2012, Pages 71-87

Supramolecular cellular filament systems: How and why do they form?

Author keywords

Cation counterion fluctuations; Cellular filament systems; Liquid crystals; Molecular crowding; Supramolecular structures

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; COUNTERION; DIETHYLAMINOETHYL CELLULOSE; DNA; F ACTIN; FTSZ PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MICROTUBULE ASSOCIATED PROTEIN; MREB PROTEIN; PARM PROTEIN; POLYELECTROLYTE; POTASSIUM CHLORIDE; TUBULIN; UNCLASSIFIED DRUG;

EID: 84857140482     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.21006     Document Type: Review
Times cited : (14)

References (106)
  • 1
    • 0030740939 scopus 로고    scopus 로고
    • AFM analysis of DNA-protamine complexes bound to mica
    • Allen MJ, Bradbury EM, Balhorn R. 1997. AFM analysis of DNA-protamine complexes bound to mica. Nucleic Acids Res 25: 2221-2226.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2221-2226
    • Allen, M.J.1    Bradbury, E.M.2    Balhorn, R.3
  • 2
    • 58549106648 scopus 로고    scopus 로고
    • Force generation by a dynamic Z-ring in Escherichia coli cell division
    • Allard JF, Cytrynbaum EN. 2009. Force generation by a dynamic Z-ring in Escherichia coli cell division. Proc Natl Acad Sci USA 106: 145-150.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 145-150
    • Allard, J.F.1    Cytrynbaum, E.N.2
  • 3
    • 0014889416 scopus 로고
    • Polymerization of flagellin and polymorphism of flagella
    • Asakura S. 1970. Polymerization of flagellin and polymorphism of flagella. Adv Biophys 1: 99-155.
    • (1970) Adv Biophys , vol.1 , pp. 99-155
    • Asakura, S.1
  • 6
    • 0026253815 scopus 로고
    • Condensation of DNA by multivalent cations: considerations on mechanism
    • Bloomfield VA. 1991. Condensation of DNA by multivalent cations: considerations on mechanism. Biopolymers 31: 1471-1481.
    • (1991) Biopolymers , vol.31 , pp. 1471-1481
    • Bloomfield, V.A.1
  • 7
    • 14844363958 scopus 로고    scopus 로고
    • Structural polymorphism of the cytoskeleton: a model of linker-assisted filament aggregation
    • Borukhov I, Bruinsma RF, Gelbart WM, Liu AJ. 2005. Structural polymorphism of the cytoskeleton: a model of linker-assisted filament aggregation. Proc Natl Acad Sci USA 102: 3673-3678.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3673-3678
    • Borukhov, I.1    Bruinsma, R.F.2    Gelbart, W.M.3    Liu, A.J.4
  • 8
    • 0004058896 scopus 로고    scopus 로고
    • Taylor & Francis: New York
    • Bray D. 2001. Cell Movements. Taylor & Francis: New York, 392 p.
    • (2001) Cell Movements , pp. 392
    • Bray, D.1
  • 9
    • 0033565651 scopus 로고    scopus 로고
    • Mechanism of DNA segregation in prokaryotes: ParM partitioning protein of plasmid R1 colocalizes with its replicon during the cell cycle
    • Bugge-Jensen R, Gerdes K. 1999. Mechanism of DNA segregation in prokaryotes: ParM partitioning protein of plasmid R1 colocalizes with its replicon during the cell cycle. EMBO J 18: 4076-4084.
    • (1999) EMBO J , vol.18 , pp. 4076-4084
    • Bugge-Jensen, R.1    Gerdes, K.2
  • 10
    • 0017841508 scopus 로고
    • Change of waveform in bacterial flagella: the role of mechanics at the molecular level
    • Calldine CR. 1978. Change of waveform in bacterial flagella: the role of mechanics at the molecular level. J Mol Biol 4: 457-479.
    • (1978) J Mol Biol , vol.4 , pp. 457-479
    • Calldine, C.R.1
  • 11
    • 0025809627 scopus 로고
    • Osmotically induced electrical signals from actin filaments
    • Cantiello HF, Patenaude C, Zaner K. 1991. Osmotically induced electrical signals from actin filaments. Biophys J 59: 1284-1289.
    • (1991) Biophys J , vol.59 , pp. 1284-1289
    • Cantiello, H.F.1    Patenaude, C.2    Zaner, K.3
  • 13
    • 0026409841 scopus 로고
    • Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo
    • Cayley S, Lewis BA, Guttman HJ, Record MT. 1991. Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo. J Mol Biol 222: 281-300.
    • (1991) J Mol Biol , vol.222 , pp. 281-300
    • Cayley, S.1    Lewis, B.A.2    Guttman, H.J.3    Record, M.T.4
  • 15
    • 11244348910 scopus 로고    scopus 로고
    • A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus
    • Chen Y, Bjornson K, Redick SD, Erickson HP. 2005. A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus. Biophys J 88: 505-514.
    • (2005) Biophys J , vol.88 , pp. 505-514
    • Chen, Y.1    Bjornson, K.2    Redick, S.D.3    Erickson, H.P.4
  • 17
    • 0035072953 scopus 로고    scopus 로고
    • Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I
    • Coleman ML, Sahai EA, Yeo M, Bosch M, Dewar A, Olson MF. 2001. Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I. Nature Cell Biol 3: 339-345.
    • (2001) Nature Cell Biol , vol.3 , pp. 339-345
    • Coleman, M.L.1    Sahai, E.A.2    Yeo, M.3    Bosch, M.4    Dewar, A.5    Olson, M.F.6
  • 18
    • 0015232094 scopus 로고
    • Tumor detection by nuclear magnetic resonance
    • Damadian R. 1971. Tumor detection by nuclear magnetic resonance. Science 171: 1151-1153.
    • (1971) Science , vol.171 , pp. 1151-1153
    • Damadian, R.1
  • 19
    • 64449085394 scopus 로고    scopus 로고
    • Analysis of mechanisms for force generation during cell septation in Escherichia coli
    • Drew DA, Koch GA, Vellante H, Talati R, Sanchez O. 2009. Analysis of mechanisms for force generation during cell septation in Escherichia coli. Bull Math Biol 71: 980-1005.
    • (2009) Bull Math Biol , vol.71 , pp. 980-1005
    • Drew, D.A.1    Koch, G.A.2    Vellante, H.3    Talati, R.4    Sanchez, O.5
  • 20
    • 67249097621 scopus 로고    scopus 로고
    • Modeling the physics of FtsZ assembly and force generation
    • Erickson HP. 2009. Modeling the physics of FtsZ assembly and force generation. Proc Natl Acad Sci USA 106: 9238-9243.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9238-9243
    • Erickson, H.P.1
  • 21
    • 0030068218 scopus 로고    scopus 로고
    • Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
    • Erickson HP, Taylor DW, Taylor KA, Bramhill D. 1996. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers. Proc Natl Acad Sci USA 93: 519-523.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 519-523
    • Erickson, H.P.1    Taylor, D.W.2    Taylor, K.A.3    Bramhill, D.4
  • 22
    • 31344480941 scopus 로고    scopus 로고
    • GTPase activity, structure and mechanical properties of filaments assembled from bacterial cytoskeleton protein MeB
    • Esue O, Tseng Y, Wirtz D. 2006. GTPase activity, structure and mechanical properties of filaments assembled from bacterial cytoskeleton protein MeB. J Bacteriol 188: 968-976.
    • (2006) J Bacteriol , vol.188 , pp. 968-976
    • Esue, O.1    Tseng, Y.2    Wirtz, D.3
  • 23
    • 0018881934 scopus 로고
    • Dynamics of nuclear actin bundle induction by dimethyl sulfoxide and factors affecting its development
    • Fukui Y, Katsumaru H. 1980. Dynamics of nuclear actin bundle induction by dimethyl sulfoxide and factors affecting its development. J Cell Biol 84: 131-140.
    • (1980) J Cell Biol , vol.84 , pp. 131-140
    • Fukui, Y.1    Katsumaru, H.2
  • 24
    • 8344247018 scopus 로고    scopus 로고
    • Dynamic instability in a DNA-segregating prokaryotic actin homolog
    • Garner EC, Cambell CS, Mullins RD. 2004. Dynamic instability in a DNA-segregating prokaryotic actin homolog. Science 306: 1021-1025.
    • (2004) Science , vol.306 , pp. 1021-1025
    • Garner, E.C.1    Cambell, C.S.2    Mullins, R.D.3
  • 25
    • 55049117823 scopus 로고    scopus 로고
    • Origin of contractile force during cell division of bacteria
    • Ghosh B, Sain A. 2008. Origin of contractile force during cell division of bacteria. Phys Rev Lett 101: 178101.
    • (2008) Phys Rev Lett , vol.101 , pp. 178101
    • Ghosh, B.1    Sain, A.2
  • 26
    • 48849105558 scopus 로고    scopus 로고
    • Packing defects and the width of polymer bundles
    • Gov N. 2008. Packing defects and the width of polymer bundles. Phys Rev E Stat Nonlin Soft Matter Phys 78: 011916.
    • (2008) Phys Rev E Stat Nonlin Soft Matter Phys , vol.78 , pp. 011916
    • Gov, N.1
  • 27
    • 34548238660 scopus 로고    scopus 로고
    • Chirality and equilibrium biopolymer bundles
    • Grason GM, Bruinsma RF. 2007. Chirality and equilibrium biopolymer bundles. Phys Rev Lett 99: 098101.
    • (2007) Phys Rev Lett , vol.99 , pp. 098101
    • Grason, G.M.1    Bruinsma, R.F.2
  • 28
    • 0022691668 scopus 로고
    • On the compact form of linear duplex DNA: globular states of the uniform elastic (persistent) macromolecule
    • Grosberg AYu, Zhestkov AV. 1986. On the compact form of linear duplex DNA: globular states of the uniform elastic (persistent) macromolecule. J Biomol Struct Dyn 5: 859-872.
    • (1986) J Biomol Struct Dyn , vol.5 , pp. 859-872
    • Grosberg, A.Y.1    Zhestkov, A.V.2
  • 29
    • 33744791437 scopus 로고    scopus 로고
    • The effect of salt on self-assembled actin-lysozyme complexes
    • Guáqueta C, Sanders LK, Wong GC, Luijten E. 2006. The effect of salt on self-assembled actin-lysozyme complexes. Biophys J 90: 4630-4638.
    • (2006) Biophys J , vol.90 , pp. 4630-4638
    • Guáqueta, C.1    Sanders, L.K.2    Wong, G.C.3    Luijten, E.4
  • 30
    • 0033137413 scopus 로고    scopus 로고
    • Kinetics of bundle growth in DNA condensation
    • Ha BY, Liu AJ. 1999. Kinetics of bundle growth in DNA condensation. Europhys Lett 46: 624-630.
    • (1999) Europhys Lett , vol.46 , pp. 624-630
    • Ha, B.Y.1    Liu, A.J.2
  • 32
    • 23244456804 scopus 로고    scopus 로고
    • The interplay between viscoelastic and thermodynamic properties determines the birefringence of f-actin gels
    • Helfer E, Panine P, Carlier M-F, Davidson P. 2005. The interplay between viscoelastic and thermodynamic properties determines the birefringence of f-actin gels. Biophys J 89: 543-553.
    • (2005) Biophys J , vol.89 , pp. 543-553
    • Helfer, E.1    Panine, P.2    Carlier, M.-F.3    Davidson, P.4
  • 33
    • 27944447667 scopus 로고    scopus 로고
    • Equilibrium bundle size of rodlike polyelectrolytes with counterion-induced attractive interactions
    • Henle M, Pincus PA. 2005. Equilibrium bundle size of rodlike polyelectrolytes with counterion-induced attractive interactions. Phys Rev E Stat Nonlin Soft Matter Phys 71: 060801.
    • (2005) Phys Rev E Stat Nonlin Soft Matter Phys , vol.71 , pp. 060801
    • Henle, M.1    Pincus, P.A.2
  • 34
    • 0025138656 scopus 로고
    • Microtubule solutions display nematic liquid crystalline structure
    • Hitt AL, Cross AR, Williams RC. 1990. Microtubule solutions display nematic liquid crystalline structure. J Biol Chem 265: 1639-1647.
    • (1990) J Biol Chem , vol.265 , pp. 1639-1647
    • Hitt, A.L.1    Cross, A.R.2    Williams, R.C.3
  • 36
    • 33646386142 scopus 로고    scopus 로고
    • Stress fibers are generated by two distinct actin assembly mechanisms in motile cells
    • Hotulainen P, Lappalainen P. 2006. Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J Cell Biol 173: 383-394.
    • (2006) J Cell Biol , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 37
    • 0028906570 scopus 로고
    • A constant radius of curvature model for the organization of DNA in toroidal condensates
    • Hud NV, Downing KH, Balhorn R. 1995 A constant radius of curvature model for the organization of DNA in toroidal condensates. Proc Natl Acad Sci USA 92: 3581-3585.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3581-3585
    • Hud, N.V.1    Downing, K.H.2    Balhorn, R.3
  • 38
    • 14044271924 scopus 로고    scopus 로고
    • Toroidal DNA condensates: unraveling the fine structure and the role of nucleation in determining size
    • Hud NV, Vilfan ID. 2005. Toroidal DNA condensates: unraveling the fine structure and the role of nucleation in determining size. Annu Rev Biophys Biomol Struct 34: 295-318.
    • (2005) Annu Rev Biophys Biomol Struct , vol.34 , pp. 295-318
    • Hud, N.V.1    Vilfan, I.D.2
  • 39
  • 40
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • Isambert H, Venier P, Maggs AC, Fattoum A, Kassab R, Pantaloni D, Carlier MF. 1995. Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J Biol Chem 270: 11437-11444.
    • (1995) J Biol Chem , vol.270 , pp. 11437-11444
    • Isambert, H.1    Venier, P.2    Maggs, A.C.3    Fattoum, A.4    Kassab, R.5    Pantaloni, D.6    Carlier, M.F.7
  • 41
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis
    • Jones LJ, Carballido-López, Errington J. 2001. Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104: 913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-López, E.J.2
  • 42
    • 0017138443 scopus 로고
    • Helical transformations of Salmonella flagella in vitro
    • Kamiya R, Asakura S. 1976. Helical transformations of Salmonella flagella in vitro. J Mol Biol 106: 167-186.
    • (1976) J Mol Biol , vol.106 , pp. 167-186
    • Kamiya, R.1    Asakura, S.2
  • 43
    • 0017166951 scopus 로고
    • Flagellar transformations at alkaline pH
    • Kamiya R, Asakura S. 1977. Flagellar transformations at alkaline pH. J Mol Biol 108: 513-518.
    • (1977) J Mol Biol , vol.108 , pp. 513-518
    • Kamiya, R.1    Asakura, S.2
  • 44
    • 49049148028 scopus 로고
    • Liquid-crystalline ordering in the solution of long persistent chains
    • Khokhlov AR, Semenov AN. 1981. Liquid-crystalline ordering in the solution of long persistent chains. Physics 108A: 546-556.
    • (1981) Physics , vol.108 A , pp. 546-556
    • Khokhlov, A.R.1    Semenov, A.N.2
  • 46
    • 0032506008 scopus 로고    scopus 로고
    • Electrostatic interaction between helical macromolecules in dense aggregates: an impetus for DNA poly- and mesomorphism
    • Kornyshev AA, Leikin S. 1998. Electrostatic interaction between helical macromolecules in dense aggregates: an impetus for DNA poly- and mesomorphism. Proc Natl Acad Sci USA 95: 13579-13584.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13579-13584
    • Kornyshev, A.A.1    Leikin, S.2
  • 47
    • 69249088090 scopus 로고    scopus 로고
    • Structural plasticity in actin and tubulin polymer dynamics
    • Kueh HY, Mitchison TJ. 2009. Structural plasticity in actin and tubulin polymer dynamics. Science 325: 960-963.
    • (2009) Science , vol.325 , pp. 960-963
    • Kueh, H.Y.1    Mitchison, T.J.2
  • 49
    • 36048937705 scopus 로고    scopus 로고
    • Z-ring force and cell shape during division in rod-like bacteria
    • Lan G, Wolgemuth CW, Sun SX. 2007. Z-ring force and cell shape during division in rod-like bacteria. Proc Natl Acad Sci USA 104: 16110-16115.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16110-16115
    • Lan, G.1    Wolgemuth, C.W.2    Sun, S.X.3
  • 50
    • 56949093012 scopus 로고    scopus 로고
    • Evolution of cytomotive filaments: the cytoskeleton from prokaryotes to eukaryotes
    • Löwe, J, Amos, LA. 2009. Evolution of cytomotive filaments: the cytoskeleton from prokaryotes to eukaryotes. Int J Biochem Cell Biol 41: 323-329.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 323-329
    • Löwe, J.1    Amos, L.A.2
  • 51
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Löwe J, Amos LA. 1998. Crystal structure of the bacterial cell-division protein FtsZ. Nature 391: 203-206.
    • (1998) Nature , vol.391 , pp. 203-206
    • Löwe, J.1    Amos, L.A.2
  • 52
    • 0031968795 scopus 로고    scopus 로고
    • FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermatoga maritime-quantitaion, GTP hydrolysis and assembly
    • Lu C, Stricker J, Erickson HP. 1998. FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermatoga maritime-quantitaion, GTP hydrolysis and assembly. Cell Motil Cytoskel 40: 71-86.
    • (1998) Cell Motil Cytoskel , vol.40 , pp. 71-86
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 53
    • 0033991590 scopus 로고    scopus 로고
    • Cytoarchitecture and physical properties of cytoplasm: volume, viscosity, diffusion, intracellular surface area
    • Luby-Phelps K. 2000. Cytoarchitecture and physical properties of cytoplasm: volume, viscosity, diffusion, intracellular surface area. Int Rev Cytol 192: 189-221.
    • (2000) Int Rev Cytol , vol.192 , pp. 189-221
    • Luby-Phelps, K.1
  • 54
    • 0030956145 scopus 로고    scopus 로고
    • Bacterial cell division and the Z ring
    • Lutkenhaus J, Addinall SG. 1997. Bacterial cell division and the Z ring. Annu Rev Biochem 66: 93-116.
    • (1997) Annu Rev Biochem , vol.66 , pp. 93-116
    • Lutkenhaus, J.1    Addinall, S.G.2
  • 55
    • 0020639256 scopus 로고
    • Changes in cell shape and actin distribution induced by constant electric fields
    • Luther PW, Peng HB, Lin JJC. 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.C.3
  • 56
    • 0028224273 scopus 로고
    • The internal pH of the forespore compartment of Bacillis magaterium decreases by about 1 pH unit during sporulation
    • MacGill NG, Cowan AE, Koppel DE, Setlow P. 1994. The internal pH of the forespore compartment of Bacillis magaterium decreases by about 1 pH unit during sporulation. J Bacteriol 176: 2252-2258.
    • (1994) J Bacteriol , vol.176 , pp. 2252-2258
    • MacGill, N.G.1    Cowan, A.E.2    Koppel, D.E.3    Setlow, P.4
  • 58
    • 0006826044 scopus 로고
    • Processing of X-ray diffraction data from partially oriented specimen
    • Makowski L. 1978. Processing of X-ray diffraction data from partially oriented specimen. J Appl Cryst 11: 273-283.
    • (1978) J Appl Cryst , vol.11 , pp. 273-283
    • Makowski, L.1
  • 59
    • 0018141095 scopus 로고
    • Limiting laws and counterion condensation in polyelectric solutions. V. Further development of the chemical model
    • Manning GS. 1978. Limiting laws and counterion condensation in polyelectric solutions. V. Further development of the chemical model. Biophys Chem 9: 65-70.
    • (1978) Biophys Chem , vol.9 , pp. 65-70
    • Manning, G.S.1
  • 60
    • 0031787749 scopus 로고    scopus 로고
    • Counterion condensation revisted
    • Manning GS, Ray J. 1998. Counterion condensation revisted. J Biomol Struct Dyn 16: 461-476.
    • (1998) J Biomol Struct Dyn , vol.16 , pp. 461-476
    • Manning, G.S.1    Ray, J.2
  • 61
    • 0021111713 scopus 로고
    • Evidence for hydrated spermidine-calf thymus DNA toruses organized by circumferential DNA wrapping
    • Marx KA, Ruben GC. 1983. Evidence for hydrated spermidine-calf thymus DNA toruses organized by circumferential DNA wrapping. Nucleic Acids Res 11: 1839-1854.
    • (1983) Nucleic Acids Res , vol.11 , pp. 1839-1854
    • Marx, K.A.1    Ruben, G.C.2
  • 62
    • 20144383298 scopus 로고    scopus 로고
    • Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy
    • Mingorance J, Tadros M, Vicente M, González JM, Rivas G, Vélez M. 2005. Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy. J Biol Chem 280: 20909-20914.
    • (2005) J Biol Chem , vol.280 , pp. 20909-20914
    • Mingorance, J.1    Tadros, M.2    Vicente, M.3    González, J.M.4    Rivas, G.5    Vélez, M.6
  • 63
    • 0032311227 scopus 로고    scopus 로고
    • Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion
    • Minton AP. 1998. Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion. Methods Enzymol 295: 127-149.
    • (1998) Methods Enzymol , vol.295 , pp. 127-149
    • Minton, A.P.1
  • 64
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton AP. 2000. Implications of macromolecular crowding for protein assembly. Curr Opin Struct Biol 10: 34-39.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 65
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton AP. 2001. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J Biol Chem 276: 10577-10580.
    • (2001) J Biol Chem , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 66
    • 77953996215 scopus 로고    scopus 로고
    • DipM, a new factor required for peptidoglycan remodeling during cell division in Caulobacter crescentus
    • Möll A, Schlimpert S, Briegel A, Jensen GJ, Thanbichler M. 2010. DipM, a new factor required for peptidoglycan remodeling during cell division in Caulobacter crescentus. Mol Microbiol 77: 90-107.
    • (2010) Mol Microbiol , vol.77 , pp. 90-107
    • Möll, A.1    Schlimpert, S.2    Briegel, A.3    Jensen, G.J.4    Thanbichler, M.5
  • 69
    • 19744379853 scopus 로고    scopus 로고
    • Synchrotron X-ray diffraction study of microtubule buckling and bundling under osmotic stress: a probe of inter-protofilament interactions
    • Needleman DJ, Ojeda-Lopez MA, Raviv U, Ewert K, Jones JB, Miller HP, Wilson L, Safinya CR. 2004. Synchrotron X-ray diffraction study of microtubule buckling and bundling under osmotic stress: a probe of inter-protofilament interactions. Phys Rev Lett 93: 198104.
    • (2004) Phys Rev Lett , vol.93 , pp. 198104
    • Needleman, D.J.1    Ojeda-Lopez, M.A.2    Raviv, U.3    Ewert, K.4    Jones, J.B.5    Miller, H.P.6    Wilson, L.7    Safinya, C.R.8
  • 70
    • 35148840132 scopus 로고    scopus 로고
    • Structural insights into the conformational variability of FtsZ
    • Oliva MA, Trambaiolo D, Löwe J. 2007. Structural insights into the conformational variability of FtsZ. J Mol Biol 373: 1229-1242.
    • (2007) J Mol Biol , vol.373 , pp. 1229-1242
    • Oliva, M.A.1    Trambaiolo, D.2    Löwe, J.3
  • 71
    • 84971301149 scopus 로고
    • The effect of shape on the interaction of colloidal particles
    • Onsager L. 1949. The effect of shape on the interaction of colloidal particles. Ann NY Acad Sci 51: 627-659.
    • (1949) Ann NY Acad Sci , vol.51 , pp. 627-659
    • Onsager, L.1
  • 72
    • 0004254691 scopus 로고
    • Marcel Dekker: New York
    • Oosawa F. 1971. Polyelectrolytes. Marcel Dekker: New York, 160 p.
    • (1971) Polyelectrolytes , pp. 160
    • Oosawa, F.1
  • 73
    • 44049091371 scopus 로고    scopus 로고
    • Reconstitution of contractile FtsZ rings in liposomes
    • Osawa M, Anderson DE, Erickson, HP. 2008. Reconstitution of contractile FtsZ rings in liposomes. Science 320: 792-794.
    • (2008) Science , vol.320 , pp. 792-794
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 74
    • 0022388275 scopus 로고
    • Toward molecular electronics. Self-screening of molecular wires
    • Parodi M, Bianco B, Chiabrera 1985. Toward molecular electronics. Self-screening of molecular wires. Cell Biophys 7: 215-235.
    • (1985) Cell Biophys , vol.7 , pp. 215-235
    • Parodi, M.1    Bianco, B.2    Chiabrera3
  • 75
    • 34247349124 scopus 로고    scopus 로고
    • A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis
    • Peters PC, Migocki MD, Thoni C, Harry EJ. 2007. A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis. Mol Microbiol 64: 487-499.
    • (2007) Mol Microbiol , vol.64 , pp. 487-499
    • Peters, P.C.1    Migocki, M.D.2    Thoni, C.3    Harry, E.J.4
  • 76
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard TD, Cooper JA. 2009. Actin, a central player in cell shape and movement. Science 325: 1208-1212.
    • (2009) Science , vol.325 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 77
    • 75749110614 scopus 로고    scopus 로고
    • Mechanics of cytokinesis in eukaryotes
    • Pollard TD. 2010. Mechanics of cytokinesis in eukaryotes. Curr Opin Cell Biol 22: 50-56.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 50-56
    • Pollard, T.D.1
  • 78
    • 33751051765 scopus 로고    scopus 로고
    • Direct visualization of actin nematic network formation and dynamics
    • Popp D, Yamamoto A, Iwasa M, Maeda, Y. 2006. Direct visualization of actin nematic network formation and dynamics. Biochem Biophys Res Commun 351: 348-353.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 348-353
    • Popp, D.1    Yamamoto, A.2    Iwasa, M.3    Maeda, Y.4
  • 80
    • 49649092897 scopus 로고    scopus 로고
    • Effect of short-range forces on the length distribution of fibrous cytoskeletal proteins
    • Popp D, Gov NS, Iwasa M, Maeda Y. 2008. Effect of short-range forces on the length distribution of fibrous cytoskeletal proteins. Biopolymers 89: 711-721.
    • (2008) Biopolymers , vol.89 , pp. 711-721
    • Popp, D.1    Gov, N.S.2    Iwasa, M.3    Maeda, Y.4
  • 86
  • 88
    • 0028926169 scopus 로고
    • In vivo quantitative characterization of intermolecular interactions
    • Reich Z, Wachtel EJ, Minsky A. 1995. In vivo quantitative characterization of intermolecular interactions. J Biol Chem 270: 7045-7046.
    • (1995) J Biol Chem , vol.270 , pp. 7045-7046
    • Reich, Z.1    Wachtel, E.J.2    Minsky, A.3
  • 89
    • 0021760689 scopus 로고
    • Structure of the nucleosome core particle at 7 Å resolution
    • Richmond TJ, Finch JT, Rushton B, Rhodes D, Klug A. 1984. Structure of the nucleosome core particle at 7 Å resolution. Nature 311: 532-537.
    • (1984) Nature , vol.311 , pp. 532-537
    • Richmond, T.J.1    Finch, J.T.2    Rushton, B.3    Rhodes, D.4    Klug, A.5
  • 90
    • 0017715432 scopus 로고
    • Heat-induced reversible hexagonal packing of spindle microtubules
    • Rieder C, Bajer AS. 1977. Heat-induced reversible hexagonal packing of spindle microtubules. J Cell Biol 74: 717-725.
    • (1977) J Cell Biol , vol.74 , pp. 717-725
    • Rieder, C.1    Bajer, A.S.2
  • 91
    • 0030596081 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA deposited into mica: equilibration versus kinetic trapping studied by statistical polymer chain analysis
    • Rivetti C, Guthold M, Bustamante C. 1996. Scanning force microscopy of DNA deposited into mica: equilibration versus kinetic trapping studied by statistical polymer chain analysis. J Mol Biol 264: 919-932.
    • (1996) J Mol Biol , vol.264 , pp. 919-932
    • Rivetti, C.1    Guthold, M.2    Bustamante, C.3
  • 92
    • 0022345898 scopus 로고
    • The responses of cells to electrical fields: a review
    • Robinson KR. 1985. The responses of cells to electrical fields: a review. J Cell Biol 101: 2023-2027.
    • (1985) J Cell Biol , vol.101 , pp. 2023-2027
    • Robinson, K.R.1
  • 93
    • 0347988122 scopus 로고    scopus 로고
    • Rate-limiting guanosine 5'-triphosphate hydrolysis during nucleotide turnover by FtsZ, a prokaryotic tubulin homolog involved in bacterial cell division
    • Romberg L, Mitchison TJ. 2004. Rate-limiting guanosine 5'-triphosphate hydrolysis during nucleotide turnover by FtsZ, a prokaryotic tubulin homolog involved in bacterial cell division. Biochemistry 43: 282-288.
    • (2004) Biochemistry , vol.43 , pp. 282-288
    • Romberg, L.1    Mitchison, T.J.2
  • 94
    • 58849121358 scopus 로고    scopus 로고
    • Electron microscopy of E. coli reveals filament bundles involved in plasmid DNA segregation
    • Salje J, Zuber B, Löwe J. 2009. Electron microscopy of E. coli reveals filament bundles involved in plasmid DNA segregation. Science 323: 509-512.
    • (2009) Science , vol.323 , pp. 509-512
    • Salje, J.1    Zuber, B.2    Löwe, J.3
  • 95
    • 0019209780 scopus 로고
    • Reversible translocation of cytoplasmatic actin into the nucleus caused by dimethyl sulfoxide
    • Sanger JW, Sanger JM, Jockush BM. 1980. Reversible translocation of cytoplasmatic actin into the nucleus caused by dimethyl sulfoxide. Proc Natl Acad Sci USA 77: 5268-5272.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 5268-5272
    • Sanger, J.W.1    Sanger, J.M.2    Jockush, B.M.3
  • 97
    • 75649148825 scopus 로고    scopus 로고
    • Membrane-mediated interactions drive the condensation and coalescence of FtsZ rings
    • Shlomovitz R, Gov NS. 2009. Membrane-mediated interactions drive the condensation and coalescence of FtsZ rings. Phys Biol 6: 1-9.
    • (2009) Phys Biol , vol.6 , pp. 1-9
    • Shlomovitz, R.1    Gov, N.S.2
  • 98
    • 46249087769 scopus 로고    scopus 로고
    • The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast
    • Srinivasan R, Mishra M, Wu L, Yin Z, Balasubramanian M. 2008. The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast. Genes Dev 22: 1741-1746.
    • (2008) Genes Dev , vol.22 , pp. 1741-1746
    • Srinivasan, R.1    Mishra, M.2    Wu, L.3    Yin, Z.4    Balasubramanian, M.5
  • 99
    • 0022001625 scopus 로고
    • Polyamines in microorganisms
    • Tabor CW, Tabor H. 1985. Polyamines in microorganisms. Microbiol Rev 49: 81-89.
    • (1985) Microbiol Rev , vol.49 , pp. 81-89
    • Tabor, C.W.1    Tabor, H.2
  • 100
    • 0030012323 scopus 로고    scopus 로고
    • The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation
    • Tang JX, Janmey PA. 1996. The polyelectrolyte nature of F-actin and the mechanism of actin bundle formation. J Biol Chem 15: 8556-8563.
    • (1996) J Biol Chem , vol.15 , pp. 8556-8563
    • Tang, J.X.1    Janmey, P.A.2
  • 101
    • 0030845631 scopus 로고    scopus 로고
    • Opposite effects of electrostatic and steric exclusion on bundle formation by F-actin and other filamentous polyelectrolytes
    • Tang JX, Ito T, Tao T, Traub P, Janmey PA. 1997. Opposite effects of electrostatic and steric exclusion on bundle formation by F-actin and other filamentous polyelectrolytes. Biochemistry 36: 12600-12607.
    • (1997) Biochemistry , vol.36 , pp. 12600-12607
    • Tang, J.X.1    Ito, T.2    Tao, T.3    Traub, P.4    Janmey, P.A.5
  • 102
    • 0033746785 scopus 로고    scopus 로고
    • Excluded volume in solvation: sensitivity of scaled-particle theory to solvent size and density
    • Tang KES, Bloomfield VA. 2000. Excluded volume in solvation: sensitivity of scaled-particle theory to solvent size and density. Biophys J 79: 2222-2234.
    • (2000) Biophys J , vol.79 , pp. 2222-2234
    • Tang, K.E.S.1    Bloomfield, V.A.2
  • 103
    • 0034015656 scopus 로고    scopus 로고
    • Real-time imaging of fluorescent flagellar filaments
    • Turner L, Ryu WS, Berg HC. 2000. Real-time imaging of fluorescent flagellar filaments. J Bacteriol 182: 2793-2801.
    • (2000) J Bacteriol , vol.182 , pp. 2793-2801
    • Turner, L.1    Ryu, W.S.2    Berg, H.C.3
  • 104
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • Van den Ent F, Amos LA, Löwe J. 2001. Prokaryotic origin of the actin cytoskeleton. Nature 413: 39-44.
    • (2001) Nature , vol.413 , pp. 39-44
    • Van den Ent, F.1    Amos, L.A.2    Löwe, J.3
  • 105
    • 0034674445 scopus 로고    scopus 로고
    • Hierarchical self-assembly of F-actin and cationic lipid complexes: stacked three-layer tubule networks
    • Wong GC, Tang JX, Lin A, Li Y, Janmey PA, Safinya CR. 2000. Hierarchical self-assembly of F-actin and cationic lipid complexes: stacked three-layer tubule networks. Science 288: 2035-2039.
    • (2000) Science , vol.288 , pp. 2035-2039
    • Wong, G.C.1    Tang, J.X.2    Lin, A.3    Li, Y.4    Janmey, P.A.5    Safinya, C.R.6
  • 106
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
    • Zimmermann SB, Trach SO. 1991. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J Mol Biol 222: 599-620.
    • (1991) J Mol Biol , vol.222 , pp. 599-620
    • Zimmermann, S.B.1    Trach, S.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.