메뉴 건너뛰기




Volumn 69, Issue 11, 2012, Pages 942-956

Comparing contractile apparatus-driven cytokinesis mechanisms across kingdoms

Author keywords

Contractile apparatus; Cytokinesis; Cytoskeleton

Indexed keywords

CONTRACTILE PROTEIN; F ACTIN; FTSZ PROTEIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN II;

EID: 84869509861     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.21082     Document Type: Review
Times cited : (31)

References (182)
  • 1
    • 69249126551 scopus 로고    scopus 로고
    • Bacterial cell division: assembly, maintenance and disassembly of the Z ring
    • Adams DW, Errington J. 2009. Bacterial cell division: assembly, maintenance and disassembly of the Z ring. Nat Rev Microbiol 7( 9): 642-653.
    • (2009) Nat Rev Microbiol , vol.7 , Issue.9 , pp. 642-653
    • Adams, D.W.1    Errington, J.2
  • 2
    • 0030837787 scopus 로고    scopus 로고
    • Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated
    • Addinall SG, Cao C, Lutkenhaus J. 1997. Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated. J Bacteriol 179( 13): 4277-4284.
    • (1997) J Bacteriol , vol.179 , Issue.13 , pp. 4277-4284
    • Addinall, S.G.1    Cao, C.2    Lutkenhaus, J.3
  • 3
    • 4344652693 scopus 로고    scopus 로고
    • Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins
    • Anderson DE, Gueiros-Filho FJ, Erickson HP. 2004. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins. J Bacteriol 186( 17): 5775-5781.
    • (2004) J Bacteriol , vol.186 , Issue.17 , pp. 5775-5781
    • Anderson, D.E.1    Gueiros-Filho, F.J.2    Erickson, H.P.3
  • 4
    • 4544268020 scopus 로고    scopus 로고
    • Comparative analysis of cytokinesis in budding yeast, fission yeast and animal cells
    • Balasubramanian MK, Bi E, Glotzer M. 2004. Comparative analysis of cytokinesis in budding yeast, fission yeast and animal cells. Curr Biol 14( 18): R806-R818.
    • (2004) Curr Biol , vol.14 , Issue.18
    • Balasubramanian, M.K.1    Bi, E.2    Glotzer, M.3
  • 5
    • 33750011475 scopus 로고    scopus 로고
    • Rho GTPase activity zones and transient contractile arrays
    • Bement WM, Miller AL, von Dassow G. 2006. Rho GTPase activity zones and transient contractile arrays. Bioessays 28( 10): 983-993.
    • (2006) Bioessays , vol.28 , Issue.10 , pp. 983-993
    • Bement, W.M.1    Miller, A.L.2    von Dassow, G.3
  • 6
    • 0037133943 scopus 로고    scopus 로고
    • Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ
    • Ben-Yehuda S, Losick R. 2002. Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ. Cell 109( 2): 257-323.
    • (2002) Cell , vol.109 , Issue.2 , pp. 257-323
    • Ben-Yehuda, S.1    Losick, R.2
  • 7
    • 0024829578 scopus 로고
    • Multicopy suppression of the cdc24 budding defect in yeast by CDC42 and three newly identified genes including the ras-related gene RSR1
    • Bender A, Pringle JR. 1989. Multicopy suppression of the cdc24 budding defect in yeast by CDC42 and three newly identified genes including the ras-related gene RSR1. Proc Natl Acad Sci USA 86( 24): 9976-9980.
    • (1989) Proc Natl Acad Sci USA , vol.86 , Issue.24 , pp. 9976-9980
    • Bender, A.1    Pringle, J.R.2
  • 8
    • 19444386428 scopus 로고    scopus 로고
    • SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli
    • Bernhardt TG, de Boer PA. 2005. SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli. Mol Cell 18( 5): 555-564.
    • (2005) Mol Cell , vol.18 , Issue.5 , pp. 555-564
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 9
    • 0035545087 scopus 로고    scopus 로고
    • Cytokinesis in budding yeast: the relationship between actomyosin ring function and septum formation
    • Bi E. 2001. Cytokinesis in budding yeast: the relationship between actomyosin ring function and septum formation. Cell Struct Funct 26( 6): 529-537.
    • (2001) Cell Struct Funct , vol.26 , Issue.6 , pp. 529-537
    • Bi, E.1
  • 10
    • 0032494183 scopus 로고    scopus 로고
    • Involvement of an actomyosin contractile ring in Saccharomyces cerevisiae cytokinesis
    • Bi E, Maddox P, Lew DJ, Salmon ED, McMillan JN, Yeh E, Pringle JR. 1998. Involvement of an actomyosin contractile ring in Saccharomyces cerevisiae cytokinesis. J Cell Biol 142( 5): 1301-1312.
    • (1998) J Cell Biol , vol.142 , Issue.5 , pp. 1301-1312
    • Bi, E.1    Maddox, P.2    Lew, D.J.3    Salmon, E.D.4    McMillan, J.N.5    Yeh, E.6    Pringle, J.R.7
  • 11
    • 84859055009 scopus 로고    scopus 로고
    • Three-dimensional super-resolution imaging of the midplane protein FtsZ in live Caulobacter crescentus cells using astigmatism
    • Biteen JS, Goley ED, Shapiro L, Moerner WE. 2012. Three-dimensional super-resolution imaging of the midplane protein FtsZ in live Caulobacter crescentus cells using astigmatism. Chemphyschem 13( 4): 1007-1012.
    • (2012) Chemphyschem , vol.13 , Issue.4 , pp. 1007-1012
    • Biteen, J.S.1    Goley, E.D.2    Shapiro, L.3    Moerner, W.E.4
  • 12
    • 0031857307 scopus 로고    scopus 로고
    • Spindle self-organization and cytokinesis during male meiosis in asterless mutants of Drosophila melanogaster
    • Bonaccorsi S, Giansanti MG, Gatti M. 1998. Spindle self-organization and cytokinesis during male meiosis in asterless mutants of Drosophila melanogaster. J Cell Biol 142( 3): 751-761.
    • (1998) J Cell Biol , vol.142 , Issue.3 , pp. 751-761
    • Bonaccorsi, S.1    Giansanti, M.G.2    Gatti, M.3
  • 13
    • 0034266786 scopus 로고    scopus 로고
    • CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast
    • Brunner D, Nurse P. 2000. CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast. Cell 102( 5): 695-704.
    • (2000) Cell , vol.102 , Issue.5 , pp. 695-704
    • Brunner, D.1    Nurse, P.2
  • 14
    • 0025259496 scopus 로고
    • Mechanism of the formation of contractile ring in dividing cultured animal cells. I. Recruitment of preexisting actin filaments into the cleavage furrow
    • Cao LG, Wang YL. 1990a. Mechanism of the formation of contractile ring in dividing cultured animal cells. I. Recruitment of preexisting actin filaments into the cleavage furrow. J Cell Biol 110( 4): 1089-1095.
    • (1990) J Cell Biol , vol.110 , Issue.4 , pp. 1089-1095
    • Cao, L.G.1    Wang, Y.L.2
  • 15
    • 0025059359 scopus 로고
    • Mechanism of the formation of contractile ring in dividing cultured animal cells. II. Cortical movement of microinjected actin filaments
    • Cao LG, Wang YL. 1990b. Mechanism of the formation of contractile ring in dividing cultured animal cells. II. Cortical movement of microinjected actin filaments. J Cell Biol 111( 5 Pt 1): 1905-1911.
    • (1990) J Cell Biol , vol.111 , Issue.5 PART 1 , pp. 1905-1911
    • Cao, L.G.1    Wang, Y.L.2
  • 16
    • 0030022357 scopus 로고    scopus 로고
    • Signals from the spindle midzone are required for the stimulation of cytokinesis in cultured epithelial cells
    • Cao LG, Wang YL. 1996. Signals from the spindle midzone are required for the stimulation of cytokinesis in cultured epithelial cells. Mol Biol Cell 7( 2): 225-232.
    • (1996) Mol Biol Cell , vol.7 , Issue.2 , pp. 225-232
    • Cao, L.G.1    Wang, Y.L.2
  • 17
    • 33749172400 scopus 로고    scopus 로고
    • Self-organization of interphase microtubule arrays in fission yeast
    • Carazo-Salas RE, Nurse P. 2006. Self-organization of interphase microtubule arrays in fission yeast. Nat Cell Biol 8( 10): 1102-1107.
    • (2006) Nat Cell Biol , vol.8 , Issue.10 , pp. 1102-1107
    • Carazo-Salas, R.E.1    Nurse, P.2
  • 18
    • 0036220079 scopus 로고    scopus 로고
    • Bud-site selection and cell polarity in budding yeast
    • Casamayor A, Snyder M. 2002. Bud-site selection and cell polarity in budding yeast. Curr Opin Microbiol 5( 2): 179-186.
    • (2002) Curr Opin Microbiol , vol.5 , Issue.2 , pp. 179-186
    • Casamayor, A.1    Snyder, M.2
  • 19
    • 10044250115 scopus 로고    scopus 로고
    • C-terminal anchoring of mid1p to membranes stabilizes cytokinetic ring position in early mitosis in fission yeast
    • Celton-Morizur S, Bordes N, Fraisier V, Tran PT, Paoletti A. 2004. C-terminal anchoring of mid1p to membranes stabilizes cytokinetic ring position in early mitosis in fission yeast. Mol Cell Biol 24( 24): 10621-10635.
    • (2004) Mol Cell Biol , vol.24 , Issue.24 , pp. 10621-10635
    • Celton-Morizur, S.1    Bordes, N.2    Fraisier, V.3    Tran, P.T.4    Paoletti, A.5
  • 20
    • 33845691069 scopus 로고    scopus 로고
    • Pom1 kinase links division plane position to cell polarity by regulating Mid1p cortical distribution
    • Celton-Morizur S, Racine V, Sibarita JB, Paoletti A. 2006. Pom1 kinase links division plane position to cell polarity by regulating Mid1p cortical distribution. J Cell Sci 119( Pt 22): 4710-4718.
    • (2006) J Cell Sci , vol.119 , Issue.PART 22 , pp. 4710-4718
    • Celton-Morizur, S.1    Racine, V.2    Sibarita, J.B.3    Paoletti, A.4
  • 21
    • 0030040263 scopus 로고    scopus 로고
    • Isolation and characterization of fission yeast mutants defective in the assembly and placement of the contractile actin ring
    • Chang F, Woollard A, Nurse P. 1996. Isolation and characterization of fission yeast mutants defective in the assembly and placement of the contractile actin ring. J Cell Sci 109( Pt 1): 131-142.
    • (1996) J Cell Sci , vol.109 , Issue.PART 1 , pp. 131-142
    • Chang, F.1    Woollard, A.2    Nurse, P.3
  • 22
    • 0030958087 scopus 로고    scopus 로고
    • cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin
    • Chang F, Drubin D, Nurse P. 1997. cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J Cell Biol 137( 1): 169-182.
    • (1997) J Cell Biol , vol.137 , Issue.1 , pp. 169-182
    • Chang, F.1    Drubin, D.2    Nurse, P.3
  • 23
    • 0034740520 scopus 로고    scopus 로고
    • FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division
    • Chen JC, Beckwith J. 2001. FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. Mol Microbiol 42( 2): 395-413.
    • (2001) Mol Microbiol , vol.42 , Issue.2 , pp. 395-413
    • Chen, J.C.1    Beckwith, J.2
  • 24
    • 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( 1): 505-514.
    • (2005) Biophys J , vol.88 , Issue.1 , pp. 505-514
    • Chen, Y.1    Bjornson, K.2    Redick, S.D.3    Erickson, H.P.4
  • 25
    • 54749131947 scopus 로고    scopus 로고
    • Redundant mechanisms recruit actin into the contractile ring in silkworm spermatocytes
    • Chen W, Foss M, Tseng KF, Zhang D. 2008. Redundant mechanisms recruit actin into the contractile ring in silkworm spermatocytes. PLoS Biol 6( 9): e209.
    • (2008) PLoS Biol , vol.6 , Issue.9
    • Chen, W.1    Foss, M.2    Tseng, K.F.3    Zhang, D.4
  • 26
    • 79952741894 scopus 로고    scopus 로고
    • Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist
    • Cho H, McManus HR, Dove SL, Bernhardt TG. 2011. Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. Proc Natl Acad Sci USA 108( 9): 3773-3778.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.9 , pp. 3773-3778
    • Cho, H.1    McManus, H.R.2    Dove, S.L.3    Bernhardt, T.G.4
  • 27
    • 7744230898 scopus 로고    scopus 로고
    • Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay
    • Corbin BD, Geissler B, Sadasivam M, Margolin W. 2004. Z-ring-independent interaction between a subdomain of FtsA and late septation proteins as revealed by a polar recruitment assay. J Bacteriol 186( 22): 7736-7744.
    • (2004) J Bacteriol , vol.186 , Issue.22 , pp. 7736-7744
    • Corbin, B.D.1    Geissler, B.2    Sadasivam, M.3    Margolin, W.4
  • 28
    • 33749159663 scopus 로고    scopus 로고
    • Self-organization of microtubule bundles in anucleate fission yeast cells
    • Daga RR, Lee KG, Bratman S, Salas-Pino S, Chang F. 2006. Self-organization of microtubule bundles in anucleate fission yeast cells. Nat Cell Biol 8( 10): 1108-1113.
    • (2006) Nat Cell Biol , vol.8 , Issue.10 , pp. 1108-1113
    • Daga, R.R.1    Lee, K.G.2    Bratman, S.3    Salas-Pino, S.4    Chang, F.5
  • 29
    • 39249085850 scopus 로고    scopus 로고
    • MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ
    • Dajkovic A, Lan G, Sun SX, Wirtz D, Lutkenhaus J. 2008. MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ. Curr Biol 18( 4): 235-244.
    • (2008) Curr Biol , vol.18 , Issue.4 , pp. 235-244
    • Dajkovic, A.1    Lan, G.2    Sun, S.X.3    Wirtz, D.4    Lutkenhaus, J.5
  • 30
    • 0036558591 scopus 로고    scopus 로고
    • Molecular evolution before the origin of species
    • Davis BK. 2002. Molecular evolution before the origin of species. Prog Biophys Mol Biol 79( 1-3): 77-133.
    • (2002) Prog Biophys Mol Biol , vol.79 , Issue.1-3 , pp. 77-133
    • Davis, B.K.1
  • 31
    • 70350141267 scopus 로고    scopus 로고
    • Phylogenetic analysis identifies many uncharacterized actin-like proteins (Alps) in bacteria: regulated polymerization, dynamic instability and treadmilling in Alp7A
    • Derman AI, Becker EC, Truong BD, Fujioka A, Tucey TM, Erb ML, Patterson PC, Pogliano J. 2009. Phylogenetic analysis identifies many uncharacterized actin-like proteins (Alps) in bacteria: regulated polymerization, dynamic instability and treadmilling in Alp7A. Mol Microbiol 73( 4): 534-552.
    • (2009) Mol Microbiol , vol.73 , Issue.4 , pp. 534-552
    • Derman, A.I.1    Becker, E.C.2    Truong, B.D.3    Fujioka, A.4    Tucey, T.M.5    Erb, M.L.6    Patterson, P.C.7    Pogliano, J.8
  • 32
    • 0346252349 scopus 로고    scopus 로고
    • Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation
    • Di Lallo G, Fagioli M, Barionovi D, Ghelardini P, Paolozzi L. 2003. Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation. Microbiology 149( Pt 12): 3353-3359.
    • (2003) Microbiology , vol.149 , Issue.PART 12 , pp. 3353-3359
    • Di Lallo, G.1    Fagioli, M.2    Barionovi, D.3    Ghelardini, P.4    Paolozzi, L.5
  • 33
    • 84860708902 scopus 로고    scopus 로고
    • MipZ: one for the pole, two for the DNA
    • Du S, Lutkenhaus J. 2012. MipZ: one for the pole, two for the DNA. Mol Cell 46( 3): 239-240.
    • (2012) Mol Cell , vol.46 , Issue.3 , pp. 239-240
    • Du, S.1    Lutkenhaus, J.2
  • 34
    • 34447318642 scopus 로고    scopus 로고
    • Evolution of the cytoskeleton
    • Erickson HP. 2007. Evolution of the cytoskeleton. Bioessays 29( 7): 668-677.
    • (2007) Bioessays , vol.29 , Issue.7 , pp. 668-677
    • Erickson, H.P.1
  • 35
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one
    • Erickson HP, Anderson DE, Osawa M. 2010. FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol Mol Biol Rev 74( 4): 504-528.
    • (2010) Microbiol Mol Biol Rev , vol.74 , Issue.4 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 37
    • 79955706693 scopus 로고    scopus 로고
    • An actin-based cytoskeleton in archaea
    • Ettema TJ, Lindas AC, Bernander R. 2011. An actin-based cytoskeleton in archaea. Mol Microbiol 80( 4): 1052-1061.
    • (2011) Mol Microbiol , vol.80 , Issue.4 , pp. 1052-1061
    • Ettema, T.J.1    Lindas, A.C.2    Bernander, R.3
  • 39
    • 84860514120 scopus 로고    scopus 로고
    • Molecular control of animal cell cytokinesis
    • Fededa JP, Gerlich DW. 2012. Molecular control of animal cell cytokinesis. Nat Cell Biol 14( 5): 440-447.
    • (2012) Nat Cell Biol , vol.14 , Issue.5 , pp. 440-447
    • Fededa, J.P.1    Gerlich, D.W.2
  • 40
    • 0027360835 scopus 로고
    • Orientation and three-dimensional organization of actin filaments in dividing cultured cells
    • Fishkind DJ, Wang YL. 1993. Orientation and three-dimensional organization of actin filaments in dividing cultured cells. J Cell Biol 123( 4): 837-848.
    • (1993) J Cell Biol , vol.123 , Issue.4 , pp. 837-848
    • Fishkind, D.J.1    Wang, Y.L.2
  • 41
    • 77958525927 scopus 로고    scopus 로고
    • In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM)
    • Fu G, Huang T, Buss J, Coltharp C, Hensel Z, Xiao J. 2010. In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM). PLoS One 5( 9): e12682.
    • (2010) PLoS One , vol.5 , Issue.9
    • Fu, G.1    Huang, T.2    Buss, J.3    Coltharp, C.4    Hensel, Z.5    Xiao, J.6
  • 42
    • 0017109215 scopus 로고
    • Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells
    • Fujiwara K, Pollard TD. 1976. Fluorescent antibody localization of myosin in the cytoplasm, cleavage furrow, and mitotic spindle of human cells. J Cell Biol 71( 3): 848-875.
    • (1976) J Cell Biol , vol.71 , Issue.3 , pp. 848-875
    • Fujiwara, K.1    Pollard, T.D.2
  • 43
    • 8344247018 scopus 로고    scopus 로고
    • Dynamic instability in a DNA-segregating prokaryotic actin homolog
    • Garner EC, Campbell CS, Mullins RD. 2004. Dynamic instability in a DNA-segregating prokaryotic actin homolog. Science 306( 5698): 1021-1025.
    • (2004) Science , vol.306 , Issue.5698 , pp. 1021-1025
    • Garner, E.C.1    Campbell, C.S.2    Mullins, R.D.3
  • 44
    • 24344499517 scopus 로고    scopus 로고
    • The novel fission yeast protein Pal1p interacts with Hip1-related Sla2p/End4p and is involved in cellular morphogenesis
    • Ge W, Chew TG, Wachtler V, Naqvi SN, Balasubramanian MK. 2005. The novel fission yeast protein Pal1p interacts with Hip1-related Sla2p/End4p and is involved in cellular morphogenesis. Mol Biol Cell 16( 9): 4124-4138.
    • (2005) Mol Biol Cell , vol.16 , Issue.9 , pp. 4124-4138
    • Ge, W.1    Chew, T.G.2    Wachtler, V.3    Naqvi, S.N.4    Balasubramanian, M.K.5
  • 45
    • 0037386678 scopus 로고    scopus 로고
    • A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli
    • Geissler B, Elraheb D, Margolin W. 2003. A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli. Proc Natl Acad Sci USA 100( 7): 4197-4202.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.7 , pp. 4197-4202
    • Geissler, B.1    Elraheb, D.2    Margolin, W.3
  • 46
    • 0035032565 scopus 로고    scopus 로고
    • The role of centrosomes and astral microtubules during asymmetric division of Drosophila neuroblasts
    • Giansanti MG, Gatti M, Bonaccorsi S. 2001. The role of centrosomes and astral microtubules during asymmetric division of Drosophila neuroblasts. Development 128( 7): 1137-1145.
    • (2001) Development , vol.128 , Issue.7 , pp. 1137-1145
    • Giansanti, M.G.1    Gatti, M.2    Bonaccorsi, S.3
  • 48
    • 0842331360 scopus 로고    scopus 로고
    • Cleavage furrow positioning
    • Glotzer M. 2004. Cleavage furrow positioning. J Cell Biol 164( 3): 347-351.
    • (2004) J Cell Biol , vol.164 , Issue.3 , pp. 347-351
    • Glotzer, M.1
  • 49
    • 15244356577 scopus 로고    scopus 로고
    • The molecular requirements for cytokinesis
    • Glotzer M. 2005. The molecular requirements for cytokinesis. Science 307( 5716): 1735-1739.
    • (2005) Science , vol.307 , Issue.5716 , pp. 1735-1739
    • Glotzer, M.1
  • 50
    • 21844441637 scopus 로고    scopus 로고
    • Diverse paths to midcell: assembly of the bacterial cell division machinery
    • Goehring NW, Beckwith J. 2005. Diverse paths to midcell: assembly of the bacterial cell division machinery. Curr Biol 15( 13): R514-R526.
    • (2005) Curr Biol , vol.15 , Issue.13
    • Goehring, N.W.1    Beckwith, J.2
  • 51
    • 11844267151 scopus 로고    scopus 로고
    • Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli
    • Goehring NW, Gueiros-Filho F, Beckwith J. 2005. Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli. Genes Dev 19( 1): 127-137.
    • (2005) Genes Dev , vol.19 , Issue.1 , pp. 127-137
    • Goehring, N.W.1    Gueiros-Filho, F.2    Beckwith, J.3
  • 52
    • 3943102141 scopus 로고    scopus 로고
    • Planar cell polarity signalling controls cell division orientation during zebrafish gastrulation
    • Gong Y, Mo C, Fraser SE. 2004. Planar cell polarity signalling controls cell division orientation during zebrafish gastrulation. Nature 430( 7000): 689-693.
    • (2004) Nature , vol.430 , Issue.7000 , pp. 689-693
    • Gong, Y.1    Mo, C.2    Fraser, S.E.3
  • 53
    • 13844312609 scopus 로고    scopus 로고
    • Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils
    • Gonzalez JM, Velez M, Jimenez M, Alfonso C, Schuck P, Mingorance J, Vicente M, Minton AP, Rivas G. 2005. Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils. Proc Natl Acad Sci U S A 102( 6): 1895-1900.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.6 , pp. 1895-1900
    • Gonzalez, J.M.1    Velez, M.2    Jimenez, M.3    Alfonso, C.4    Schuck, P.5    Mingorance, J.6    Vicente, M.7    Minton, A.P.8    Rivas, G.9
  • 54
    • 78751550466 scopus 로고    scopus 로고
    • Dividing the spoils of growth and the cell cycle: The fission yeast as a model for the study of cytokinesis
    • Goyal A, Takaine M, Simanis V, Nakano K. 2011. Dividing the spoils of growth and the cell cycle: The fission yeast as a model for the study of cytokinesis. Cytoskeleton (Hoboken) 68( 2): 69-88.
    • (2011) Cytoskeleton (Hoboken) , vol.68 , Issue.2 , pp. 69-88
    • Goyal, A.1    Takaine, M.2    Simanis, V.3    Nakano, K.4
  • 55
    • 18044363909 scopus 로고    scopus 로고
    • Cortical actin turnover during cytokinesis requires myosin II
    • Guha M, Zhou M, Wang YL. 2005. Cortical actin turnover during cytokinesis requires myosin II. Curr Biol 15( 8): 732-736.
    • (2005) Curr Biol , vol.15 , Issue.8 , pp. 732-736
    • Guha, M.1    Zhou, M.2    Wang, Y.L.3
  • 57
    • 56549083997 scopus 로고    scopus 로고
    • Mid1p/anillin and the septation initiation network orchestrate contractile ring assembly for cytokinesis
    • Hachet O, Simanis V. 2008. Mid1p/anillin and the septation initiation network orchestrate contractile ring assembly for cytokinesis. Genes Dev 22( 22): 3205-3216.
    • (2008) Genes Dev , vol.22 , Issue.22 , pp. 3205-3216
    • Hachet, O.1    Simanis, V.2
  • 58
    • 0033810918 scopus 로고    scopus 로고
    • ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains
    • Hale CA, Rhee AC, de Boer PA. 2000. ZipA-induced bundling of FtsZ polymers mediated by an interaction between C-terminal domains. J Bacteriol 182( 18): 5153-5166.
    • (2000) J Bacteriol , vol.182 , Issue.18 , pp. 5153-5166
    • Hale, C.A.1    Rhee, A.C.2    de Boer, P.A.3
  • 59
    • 0035853803 scopus 로고    scopus 로고
    • Genetic analysis of the Escherichia coli FtsZ. ZipA interaction in the yeast two-hybrid system. Characterization of FtsZ residues essential for the interactions with ZipA and with FtsA
    • Haney SA, Glasfeld E, Hale C, Keeney D, He Z, de Boer P. 2001. Genetic analysis of the Escherichia coli FtsZ. ZipA interaction in the yeast two-hybrid system. Characterization of FtsZ residues essential for the interactions with ZipA and with FtsA. J Biol Chem 276( 15): 11980-11987.
    • (2001) J Biol Chem , vol.276 , Issue.15 , pp. 11980-11987
    • Haney, S.A.1    Glasfeld, E.2    Hale, C.3    Keeney, D.4    He, Z.5    de Boer, P.6
  • 60
    • 84862189021 scopus 로고    scopus 로고
    • Nucleotide-dependent conformations of FtsZ dimers and force generation observed through molecular dynamics simulations
    • Hsin J, Gopinathan A, Huang KC. 2012. Nucleotide-dependent conformations of FtsZ dimers and force generation observed through molecular dynamics simulations. Proc Natl Acad Sci USA 109( 24): 9432-9437.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.24 , pp. 9432-9437
    • Hsin, J.1    Gopinathan, A.2    Huang, K.C.3
  • 61
    • 0033592949 scopus 로고    scopus 로고
    • The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization
    • Hu Z, Mukherjee A, Pichoff S, Lutkenhaus J. 1999. The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization. Proc Natl Acad Sci U S A 96( 26): 14819-14824.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , Issue.26 , pp. 14819-14824
    • Hu, Z.1    Mukherjee, A.2    Pichoff, S.3    Lutkenhaus, J.4
  • 62
    • 34249318368 scopus 로고    scopus 로고
    • Polarity determinants Tea1p, Tea4p, and Pom1p inhibit division-septum assembly at cell ends in fission yeast
    • Huang Y, Chew TG, Ge W, Balasubramanian MK. 2007. Polarity determinants Tea1p, Tea4p, and Pom1p inhibit division-septum assembly at cell ends in fission yeast. Dev Cell 12( 6): 987-996.
    • (2007) Dev Cell , vol.12 , Issue.6 , pp. 987-996
    • Huang, Y.1    Chew, T.G.2    Ge, W.3    Balasubramanian, M.K.4
  • 63
    • 58249087337 scopus 로고    scopus 로고
    • Assembly of normal actomyosin rings in the absence of Mid1p and cortical nodes in fission yeast
    • Huang Y, Yan H, Balasubramanian MK. 2008. Assembly of normal actomyosin rings in the absence of Mid1p and cortical nodes in fission yeast. J Cell Biol 183( 6): 979-988.
    • (2008) J Cell Biol , vol.183 , Issue.6 , pp. 979-988
    • Huang, Y.1    Yan, H.2    Balasubramanian, M.K.3
  • 64
    • 41449086675 scopus 로고    scopus 로고
    • Energetics and geometry of FtsZ polymers: nucleated self-assembly of single protofilaments
    • Huecas S, Llorca O, Boskovic J, Martin-Benito J, Valpuesta JM, Andreu JM. 2008. Energetics and geometry of FtsZ polymers: nucleated self-assembly of single protofilaments. Biophys J 94( 5): 1796-1806.
    • (2008) Biophys J , vol.94 , Issue.5 , pp. 1796-1806
    • Huecas, S.1    Llorca, O.2    Boskovic, J.3    Martin-Benito, J.4    Valpuesta, J.M.5    Andreu, J.M.6
  • 65
    • 33744479995 scopus 로고    scopus 로고
    • A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis
    • Ishikawa S, Kawai Y, Hiramatsu K, Kuwano M, Ogasawara N. 2006. A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis. Mol Microbiol 60( 6): 1364-1380.
    • (2006) Mol Microbiol , vol.60 , Issue.6 , pp. 1364-1380
    • Ishikawa, S.1    Kawai, Y.2    Hiramatsu, K.3    Kuwano, M.4    Ogasawara, N.5
  • 66
    • 79952041482 scopus 로고    scopus 로고
    • Super-resolution imaging of the bacterial cytokinetic protein FtsZ
    • Jennings PC, Cox GC, Monahan LG, Harry EJ. 2010. Super-resolution imaging of the bacterial cytokinetic protein FtsZ. Micron 42: 336-441.
    • (2010) Micron , vol.42 , pp. 336-441
    • Jennings, P.C.1    Cox, G.C.2    Monahan, L.G.3    Harry, E.J.4
  • 67
    • 24944469539 scopus 로고    scopus 로고
    • Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly
    • Jensen SO, Thompson LS, Harry EJ. 2005. Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly. J Bacteriol 187( 18): 6536-6544.
    • (2005) J Bacteriol , vol.187 , Issue.18 , pp. 6536-6544
    • Jensen, S.O.1    Thompson, L.S.2    Harry, E.J.3
  • 68
    • 34548299090 scopus 로고    scopus 로고
    • Three-dimensional arrangement of F-actin in the contractile ring of fission yeast
    • Kamasaki T, Osumi M, Mabuchi I. 2007. Three-dimensional arrangement of F-actin in the contractile ring of fission yeast. J Cell Biol 178( 5): 765-771.
    • (2007) J Cell Biol , vol.178 , Issue.5 , pp. 765-771
    • Kamasaki, T.1    Osumi, M.2    Mabuchi, I.3
  • 69
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova G, Dautin N, Ladant D. 2005. Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J Bacteriol 187( 7): 2233-2243.
    • (2005) J Bacteriol , vol.187 , Issue.7 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 70
    • 84860777141 scopus 로고    scopus 로고
    • Localized dimerization and nucleoid binding drive gradient formation by the bacterial cell division inhibitor MipZ
    • Kiekebusch D, Michie KA, Essen LO, Lowe J, Thanbichler M. 2012. Localized dimerization and nucleoid binding drive gradient formation by the bacterial cell division inhibitor MipZ. Mol Cell 46( 3): 245-259.
    • (2012) Mol Cell , vol.46 , Issue.3 , pp. 245-259
    • Kiekebusch, D.1    Michie, K.A.2    Essen, L.O.3    Lowe, J.4    Thanbichler, M.5
  • 71
    • 0034619765 scopus 로고    scopus 로고
    • Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow
    • Kosako H, Yoshida T, Matsumura F, Ishizaki T, Narumiya S, Inagaki M. 2000. Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow. Oncogene 19( 52): 6059-6064.
    • (2000) Oncogene , vol.19 , Issue.52 , pp. 6059-6064
    • Kosako, H.1    Yoshida, T.2    Matsumura, F.3    Ishizaki, T.4    Narumiya, S.5    Inagaki, M.6
  • 72
    • 82555203013 scopus 로고    scopus 로고
    • ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments
    • Kuchibhatla A, Bhattacharya A, Panda D. 2011. ZipA binds to FtsZ with high affinity and enhances the stability of FtsZ protofilaments. PLoS One 6( 12): e28262.
    • (2011) PLoS One , vol.6 , Issue.12
    • Kuchibhatla, A.1    Bhattacharya, A.2    Panda, D.3
  • 73
    • 79955509029 scopus 로고    scopus 로고
    • Assembly and architecture of precursor nodes during fission yeast cytokinesis
    • Laporte D, Coffman VC, Lee IJ, Wu JQ. 2011. Assembly and architecture of precursor nodes during fission yeast cytokinesis. J Cell Biol 192( 6): 1005-1021.
    • (2011) J Cell Biol , vol.192 , Issue.6 , pp. 1005-1021
    • Laporte, D.1    Coffman, V.C.2    Lee, I.J.3    Wu, J.Q.4
  • 74
    • 34249897760 scopus 로고    scopus 로고
    • Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis
    • Larsen RA, Cusumano C, Fujioka A, Lim-Fong G, Patterson P, Pogliano J. 2007. Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis. Genes Dev 21( 11): 1340-1352.
    • (2007) Genes Dev , vol.21 , Issue.11 , pp. 1340-1352
    • Larsen, R.A.1    Cusumano, C.2    Fujioka, A.3    Lim-Fong, G.4    Patterson, P.5    Pogliano, J.6
  • 75
    • 0043202969 scopus 로고    scopus 로고
    • The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • Li F, Higgs HN. 2003. The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr Biol 13( 15): 1335-1340.
    • (2003) Curr Biol , vol.13 , Issue.15 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 76
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li Z, Trimble MJ, Brun YV, Jensen GJ. 2007. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J 26( 22): 4694-4708.
    • (2007) EMBO J , vol.26 , Issue.22 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 78
    • 0032567760 scopus 로고    scopus 로고
    • Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis
    • Lippincott J, Li R. 1998. Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis. J Cell Biol 140( 2): 355-366.
    • (1998) J Cell Biol , vol.140 , Issue.2 , pp. 355-366
    • Lippincott, J.1    Li, R.2
  • 79
    • 0034656215 scopus 로고    scopus 로고
    • Involvement of PCH family proteins in cytokinesis and actin distribution
    • Lippincott J, Li R. 2000. Involvement of PCH family proteins in cytokinesis and actin distribution. Microsc Res Tech 49( 2): 168-172.
    • (2000) Microsc Res Tech , vol.49 , Issue.2 , pp. 168-172
    • Lippincott, J.1    Li, R.2
  • 80
    • 0033028421 scopus 로고    scopus 로고
    • Recruitment of ZipA to the division site by interaction with FtsZ
    • Liu Z, Mukherjee A, Lutkenhaus J. 1999. Recruitment of ZipA to the division site by interaction with FtsZ. Mol Microbiol 31( 6): 1853-1861.
    • (1999) Mol Microbiol , vol.31 , Issue.6 , pp. 1853-1861
    • Liu, Z.1    Mukherjee, A.2    Lutkenhaus, J.3
  • 81
    • 0032759784 scopus 로고    scopus 로고
    • The straight and curved conformation of FtsZ protofilaments-evidence for rapid exchange of GTP into the curved protofilament
    • Lu C, Erickson HP. 1999. The straight and curved conformation of FtsZ protofilaments-evidence for rapid exchange of GTP into the curved protofilament. Cell Struct Funct 24( 5): 285-290.
    • (1999) Cell Struct Funct , vol.24 , Issue.5 , pp. 285-290
    • Lu, C.1    Erickson, H.P.2
  • 82
    • 0033986992 scopus 로고    scopus 로고
    • Straight and curved conformations of FtsZ are regulated by GTP hydrolysis
    • Lu C, Reedy M, Erickson HP. 2000. Straight and curved conformations of FtsZ are regulated by GTP hydrolysis. J Bacteriol 182( 1): 164-170.
    • (2000) J Bacteriol , vol.182 , Issue.1 , pp. 164-170
    • Lu, C.1    Reedy, M.2    Erickson, H.P.3
  • 83
    • 3042645379 scopus 로고    scopus 로고
    • Identification and functional analysis of the essential and regulatory light chains of the only type II myosin Myo1p in Saccharomyces cerevisiae
    • Luo J, Vallen EA, Dravis C, Tcheperegine SE, Drees B, Bi E. 2004. Identification and functional analysis of the essential and regulatory light chains of the only type II myosin Myo1p in Saccharomyces cerevisiae. J Cell Biol 165( 6): 843-855.
    • (2004) J Cell Biol , vol.165 , Issue.6 , pp. 843-855
    • Luo, J.1    Vallen, E.A.2    Dravis, C.3    Tcheperegine, S.E.4    Drees, B.5    Bi, E.6
  • 84
    • 34548630230 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring
    • Lutkenhaus J. 2007. Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring. Annu Rev Biochem 76: 539-562.
    • (2007) Annu Rev Biochem , vol.76 , pp. 539-562
    • Lutkenhaus, J.1
  • 85
    • 0032786248 scopus 로고    scopus 로고
    • Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ
    • Ma X, Margolin W. 1999. Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ. J Bacteriol 181( 24): 7531-7544.
    • (1999) J Bacteriol , vol.181 , Issue.24 , pp. 7531-7544
    • Ma, X.1    Margolin, W.2
  • 87
    • 0017691824 scopus 로고
    • The effect of myosin antibody on the division of starfish blastomeres
    • Mabuchi I, Okuno M. 1977. The effect of myosin antibody on the division of starfish blastomeres. J Cell Biol 74( 1): 251-263.
    • (1977) J Cell Biol , vol.74 , Issue.1 , pp. 251-263
    • Mabuchi, I.1    Okuno, M.2
  • 88
    • 2642617087 scopus 로고
    • Cleavage furrow isolated from newt eggs: contraction, organization of the actin filaments, and protein components of the furrow
    • Mabuchi I, Tsukita S, Sawai T. 1988. Cleavage furrow isolated from newt eggs: contraction, organization of the actin filaments, and protein components of the furrow. Proc Natl Acad Sci USA 85( 16): 5966-5970.
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.16 , pp. 5966-5970
    • Mabuchi, I.1    Tsukita, S.2    Sawai, T.3
  • 89
    • 77951957095 scopus 로고    scopus 로고
    • Two new families of the FtsZ-tubulin protein superfamily implicated in membrane remodeling in diverse bacteria and archaea
    • Makarova KS, Koonin EV. 2010. Two new families of the FtsZ-tubulin protein superfamily implicated in membrane remodeling in diverse bacteria and archaea. Biol Direct 5: 33.
    • (2010) Biol Direct , vol.5 , pp. 33
    • Makarova, K.S.1    Koonin, E.V.2
  • 90
    • 77957130448 scopus 로고    scopus 로고
    • Evolution of diverse cell division and vesicle formation systems in Archaea
    • Makarova KS, Yutin N, Bell SD, Koonin EV. 2010. Evolution of diverse cell division and vesicle formation systems in Archaea. Nat Rev Microbiol 8( 10): 731-741.
    • (2010) Nat Rev Microbiol , vol.8 , Issue.10 , pp. 731-741
    • Makarova, K.S.1    Yutin, N.2    Bell, S.D.3    Koonin, E.V.4
  • 91
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokaryotic cells and organelles
    • Margolin W. 2005. FtsZ and the division of prokaryotic cells and organelles. Nat Rev Mol Cell Biol 6( 11): 862-871.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.11 , pp. 862-871
    • Margolin, W.1
  • 92
    • 0032213104 scopus 로고    scopus 로고
    • Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site
    • Marston AL, Thomaides HB, Edwards DH, Sharpe ME, Errington J. 1998. Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site. Genes Dev 12( 21): 3419-3430.
    • (1998) Genes Dev , vol.12 , Issue.21 , pp. 3419-3430
    • Marston, A.L.1    Thomaides, H.B.2    Edwards, D.H.3    Sharpe, M.E.4    Errington, J.5
  • 93
    • 79958706892 scopus 로고    scopus 로고
    • Myosin light chain kinases and phosphatase in mitosis and cytokinesis
    • Matsumura F, Yamakita Y, Yamashiro S. 2011. Myosin light chain kinases and phosphatase in mitosis and cytokinesis. Arch Biochem Biophys 510( 2): 76-82.
    • (2011) Arch Biochem Biophys , vol.510 , Issue.2 , pp. 76-82
    • Matsumura, F.1    Yamakita, Y.2    Yamashiro, S.3
  • 94
    • 0022967956 scopus 로고
    • Arrangement of actin filaments and myosin-like filaments in the contractile ring and of actin-like filaments in the mitotic spindle of dividing HeLa cells
    • Maupin P, Pollard TD. 1986. Arrangement of actin filaments and myosin-like filaments in the contractile ring and of actin-like filaments in the mitotic spindle of dividing HeLa cells. J Ultrastruct Mol Struct Res 94( 1): 92-103.
    • (1986) J Ultrastruct Mol Struct Res , vol.94 , Issue.1 , pp. 92-103
    • Maupin, P.1    Pollard, T.D.2
  • 95
    • 84862124625 scopus 로고    scopus 로고
    • Actin depolymerization drives actomyosin ring contraction during budding yeast cytokinesis
    • Mendes Pinto I, Rubinstein B, Kucharavy A, Unruh JR, Li R. 2012. Actin depolymerization drives actomyosin ring contraction during budding yeast cytokinesis. Dev Cell 22( 6): 1247-1260.
    • (2012) Dev Cell , vol.22 , Issue.6 , pp. 1247-1260
    • Mendes Pinto, I.1    Rubinstein, B.2    Kucharavy, A.3    Unruh, J.R.4    Li, R.5
  • 96
    • 33644778043 scopus 로고    scopus 로고
    • Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ
    • Michie KA, Monahan LG, Beech PL, Harry EJ. 2006. Trapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ. J Bacteriol 188( 5): 1680-1690.
    • (2006) J Bacteriol , vol.188 , Issue.5 , pp. 1680-1690
    • Michie, K.A.1    Monahan, L.G.2    Beech, P.L.3    Harry, E.J.4
  • 97
    • 79551679528 scopus 로고    scopus 로고
    • Influence of cell geometry on division-plane positioning
    • Minc N, Burgess D, Chang F. 2011. Influence of cell geometry on division-plane positioning. Cell 144( 3): 414-426.
    • (2011) Cell , vol.144 , Issue.3 , pp. 414-426
    • Minc, N.1    Burgess, D.2    Chang, F.3
  • 98
    • 20144383298 scopus 로고    scopus 로고
    • Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy
    • Mingorance J, Tadros M, Vicente M, Gonzalez JM, Rivas G, Velez M. 2005. Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy. J Biol Chem 280( 21): 20909-20914.
    • (2005) J Biol Chem , vol.280 , Issue.21 , pp. 20909-20914
    • Mingorance, J.1    Tadros, M.2    Vicente, M.3    Gonzalez, J.M.4    Rivas, G.5    Velez, M.6
  • 100
    • 40749094742 scopus 로고    scopus 로고
    • Cytokinesis: catch and drag
    • Mishra M, Oliferenko S. 2008. Cytokinesis: catch and drag. Curr Biol 18( 6): R247-R250.
    • (2008) Curr Biol , vol.18 , Issue.6
    • Mishra, M.1    Oliferenko, S.2
  • 102
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T, Kirschner M. 1984. Dynamic instability of microtubule growth. Nature 312( 5991): 237-242.
    • (1984) Nature , vol.312 , Issue.5991 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 103
    • 70449586634 scopus 로고    scopus 로고
    • Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria
    • Monahan LG, Robinson A, Harry EJ. 2009. Lateral FtsZ association and the assembly of the cytokinetic Z ring in bacteria. Mol Microbiol 74( 4): 1004-1017.
    • (2009) Mol Microbiol , vol.74 , Issue.4 , pp. 1004-1017
    • Monahan, L.G.1    Robinson, A.2    Harry, E.J.3
  • 104
    • 77955039647 scopus 로고    scopus 로고
    • Cell division intersects with cell geometry
    • Moseley J, Nurse P. 2010. Cell division intersects with cell geometry. Cell 142( 2): 184-192.
    • (2010) Cell , vol.142 , Issue.2 , pp. 184-192
    • Moseley, J.1    Nurse, P.2
  • 105
    • 0034600952 scopus 로고    scopus 로고
    • The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography
    • Mosyak L, Zhang Y, Glasfeld E, Haney S, Stahl M, Seehra J, Somers WS. 2000. The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J 19( 13): 3179-3191.
    • (2000) EMBO J , vol.19 , Issue.13 , pp. 3179-3191
    • Mosyak, L.1    Zhang, Y.2    Glasfeld, E.3    Haney, S.4    Stahl, M.5    Seehra, J.6    Somers, W.S.7
  • 106
    • 2942694648 scopus 로고    scopus 로고
    • Myosin-II reorganization during mitosis is controlled temporally by its dephosphorylation and spatially by Mid1 in fission yeast
    • Motegi F, Mishra M, Balasubramanian MK, Mabuchi I. 2004. Myosin-II reorganization during mitosis is controlled temporally by its dephosphorylation and spatially by Mid1 in fission yeast. J Cell Biol 165( 5): 685-695.
    • (2004) J Cell Biol , vol.165 , Issue.5 , pp. 685-695
    • Motegi, F.1    Mishra, M.2    Balasubramanian, M.K.3    Mabuchi, I.4
  • 107
    • 0024720146 scopus 로고
    • Actively replicating nucleoids influence positioning of division sites in Escherichia coli filaments forming cells lacking DNA
    • Mulder E, Woldringh CL. 1989. Actively replicating nucleoids influence positioning of division sites in Escherichia coli filaments forming cells lacking DNA. J Bacteriol 171( 8): 4303-4314.
    • (1989) J Bacteriol , vol.171 , Issue.8 , pp. 4303-4314
    • Mulder, E.1    Woldringh, C.L.2
  • 108
    • 0031049976 scopus 로고    scopus 로고
    • Myosin II-independent processes in mitotic cells of Dictyostelium discoideum: redistribution of the nuclei, re-arrangement of the actin system and formation of the cleavage furrow
    • Neujahr R, Heizer C, Gerisch G. 1997. Myosin II-independent processes in mitotic cells of Dictyostelium discoideum: redistribution of the nuclei, re-arrangement of the actin system and formation of the cleavage furrow. J Cell Sci 110( Pt 2): 123-137.
    • (1997) J Cell Sci , vol.110 , Issue.PART 2 , pp. 123-137
    • Neujahr, R.1    Heizer, C.2    Gerisch, G.3
  • 109
    • 31644438188 scopus 로고    scopus 로고
    • Centralspindlin regulates ECT2 and RhoA accumulation at the equatorial cortex during cytokinesis
    • Nishimura Y, Yonemura S. 2006. Centralspindlin regulates ECT2 and RhoA accumulation at the equatorial cortex during cytokinesis. J Cell Sci 119( Pt 1): 104-114.
    • (2006) J Cell Sci , vol.119 , Issue.PART 1 , pp. 104-114
    • Nishimura, Y.1    Yonemura, S.2
  • 110
    • 0034026122 scopus 로고    scopus 로고
    • Mammalian spindle orientation and position respond to changes in cell shape in a dynein-dependent fashion
    • O'Connell CB, Wang YL. 2000. Mammalian spindle orientation and position respond to changes in cell shape in a dynein-dependent fashion. Mol Biol Cell 11( 5): 1765-1774.
    • (2000) Mol Biol Cell , vol.11 , Issue.5 , pp. 1765-1774
    • O'Connell, C.B.1    Wang, Y.L.2
  • 112
    • 79960160278 scopus 로고    scopus 로고
    • Inside-out Z rings-constriction with and without GTP hydrolysis
    • Osawa M, Erickson HP. 2011. Inside-out Z rings-constriction with and without GTP hydrolysis. Mol Microbiol 81( 2): 571-579.
    • (2011) Mol Microbiol , vol.81 , Issue.2 , pp. 571-579
    • Osawa, M.1    Erickson, H.P.2
  • 113
    • 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( 5877): 792-794.
    • (2008) Science , vol.320 , Issue.5877 , pp. 792-794
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 114
    • 70450224670 scopus 로고    scopus 로고
    • Curved FtsZ protofilaments generate bending forces on liposome membranes
    • Osawa M, Anderson DE, Erickson HP. 2009. Curved FtsZ protofilaments generate bending forces on liposome membranes. EMBO J 28( 22): 3476-3484.
    • (2009) EMBO J , vol.28 , Issue.22 , pp. 3476-3484
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 116
    • 33845467072 scopus 로고    scopus 로고
    • The cell-end factor pom1p inhibits mid1p in specification of the cell division plane in fission yeast
    • Padte NN, Martin SG, Howard M, Chang F. 2006. The cell-end factor pom1p inhibits mid1p in specification of the cell division plane in fission yeast. Curr Biol 16( 24): 2480-2487.
    • (2006) Curr Biol , vol.16 , Issue.24 , pp. 2480-2487
    • Padte, N.N.1    Martin, S.G.2    Howard, M.3    Chang, F.4
  • 117
    • 0033836519 scopus 로고    scopus 로고
    • Analysis of mid1p, a protein required for placement of the cell division site, reveals a link between the nucleus and the cell surface in fission yeast
    • Paoletti A, Chang F. 2000. Analysis of mid1p, a protein required for placement of the cell division site, reveals a link between the nucleus and the cell surface in fission yeast. Mol Biol Cell 11( 8): 2757-2773.
    • (2000) Mol Biol Cell , vol.11 , Issue.8 , pp. 2757-2773
    • Paoletti, A.1    Chang, F.2
  • 118
    • 0030940119 scopus 로고    scopus 로고
    • Two active states of the Ras-related Bud1/Rsr1 protein bind to different effectors to determine yeast cell polarity
    • Park HO, Bi E, Pringle JR, Herskowitz I. 1997. Two active states of the Ras-related Bud1/Rsr1 protein bind to different effectors to determine yeast cell polarity. Proc Natl Acad Sci USA 94( 9): 4463-4468.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.9 , pp. 4463-4468
    • Park, H.O.1    Bi, E.2    Pringle, J.R.3    Herskowitz, I.4
  • 119
    • 0037026486 scopus 로고    scopus 로고
    • Actin dynamics in the contractile ring during cytokinesis in fission yeast
    • Pelham RJ, Chang F. 2002. Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature 419( 6902): 82-86.
    • (2002) Nature , vol.419 , Issue.6902 , pp. 82-86
    • Pelham, R.J.1    Chang, F.2
  • 121
    • 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( 2): 487-499.
    • (2007) Mol Microbiol , vol.64 , Issue.2 , pp. 487-499
    • Peters, P.C.1    Migocki, M.D.2    Thoni, C.3    Harry, E.J.4
  • 122
    • 0034750707 scopus 로고    scopus 로고
    • Escherichia coli division inhibitor MinCD blocks septation by preventing Z-ring formation
    • Pichoff S, Lutkenhaus J. 2001. Escherichia coli division inhibitor MinCD blocks septation by preventing Z-ring formation. J Bacteriol 183( 22): 6630-6635.
    • (2001) J Bacteriol , vol.183 , Issue.22 , pp. 6630-6635
    • Pichoff, S.1    Lutkenhaus, J.2
  • 123
    • 0037084109 scopus 로고    scopus 로고
    • Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli
    • Pichoff S, Lutkenhaus J. 2002. Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli. EMBO J 21( 4): 685-693.
    • (2002) EMBO J , vol.21 , Issue.4 , pp. 685-693
    • Pichoff, S.1    Lutkenhaus, J.2
  • 124
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • Pichoff S, Lutkenhaus J. 2005. Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol Microbiol 55( 6): 1722-1734.
    • (2005) Mol Microbiol , vol.55 , Issue.6 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 125
    • 84155167132 scopus 로고    scopus 로고
    • FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins
    • Pichoff S, Shen B, Sullivan B, Lutkenhaus J. 2012. FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins. Mol Microbiol 83( 1): 151-167.
    • (2012) Mol Microbiol , vol.83 , Issue.1 , pp. 151-167
    • Pichoff, S.1    Shen, B.2    Sullivan, B.3    Lutkenhaus, J.4
  • 126
    • 28244444494 scopus 로고    scopus 로고
    • Cytokinesis: welcome to the Rho zone
    • Piekny A, Werner M, Glotzer M. 2005. Cytokinesis: welcome to the Rho zone. Trends Cell Biol 15( 12): 651-658.
    • (2005) Trends Cell Biol , vol.15 , Issue.12 , pp. 651-658
    • Piekny, A.1    Werner, M.2    Glotzer, M.3
  • 127
    • 84861137359 scopus 로고    scopus 로고
    • Deconvolution of the cellular force-generating subsystems that govern cytokinesis furrow ingression
    • Poirier CC, Ng WP, Robinson DN, Iglesias PA. 2012. Deconvolution of the cellular force-generating subsystems that govern cytokinesis furrow ingression. PLoS Comput Biol 8( 4): e1002467.
    • (2012) PLoS Comput Biol , vol.8 , Issue.4
    • Poirier, C.C.1    Ng, W.P.2    Robinson, D.N.3    Iglesias, P.A.4
  • 128
    • 75749110614 scopus 로고    scopus 로고
    • Mechanics of cytokinesis in eukaryotes
    • Pollard TD. 2010. Mechanics of cytokinesis in eukaryotes. Curr Opin Cell Biol 22( 1): 50-56.
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.1 , pp. 50-56
    • Pollard, T.D.1
  • 129
    • 75149124357 scopus 로고    scopus 로고
    • Understanding cytokinesis: lessons from fission yeast
    • Pollard TD, Wu JQ. 2010. Understanding cytokinesis: lessons from fission yeast. Nat Rev Mol Cell Biol 11( 2): 149-155.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.2 , pp. 149-155
    • Pollard, T.D.1    Wu, J.Q.2
  • 130
    • 77951235277 scopus 로고    scopus 로고
    • Suprastructures and dynamic properties of Mycobacterium tuberculosis FtsZ
    • Popp D, Iwasa M, Erickson HP, Narita A, Maeda Y, Robinson RC. 2010. Suprastructures and dynamic properties of Mycobacterium tuberculosis FtsZ. J Biol Chem 285( 15): 11281-11289.
    • (2010) J Biol Chem , vol.285 , Issue.15 , pp. 11281-11289
    • Popp, D.1    Iwasa, M.2    Erickson, H.P.3    Narita, A.4    Maeda, Y.5    Robinson, R.C.6
  • 131
    • 84866144681 scopus 로고    scopus 로고
    • Contributions of turgor pressure, the contractile ring, and septum assembly to forces in cytokinesis in fission yeast
    • Proctor SA, Minc N, Boudaoud A, Chang F. 2012. Contributions of turgor pressure, the contractile ring, and septum assembly to forces in cytokinesis in fission yeast. Curr Biol 22( 17): 1601-1608.
    • (2012) Curr Biol , vol.22 , Issue.17 , pp. 1601-1608
    • Proctor, S.A.1    Minc, N.2    Boudaoud, A.3    Chang, F.4
  • 132
    • 69449106111 scopus 로고    scopus 로고
    • Negative membrane curvature as a cue for subcellular localization of a bacterial protein
    • Ramamurthi KS, Losick R. 2009. Negative membrane curvature as a cue for subcellular localization of a bacterial protein. Proc Natl Acad Sci USA 106( 32): 13541-13545.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.32 , pp. 13541-13545
    • Ramamurthi, K.S.1    Losick, R.2
  • 133
    • 62149141206 scopus 로고    scopus 로고
    • Geometric cue for protein localization in a bacterium
    • Ramamurthi KS, Lecuyer S, Stone HA, Losick R. 2009. Geometric cue for protein localization in a bacterium. Science 323( 5919): 1354-1357.
    • (2009) Science , vol.323 , Issue.5919 , pp. 1354-1357
    • Ramamurthi, K.S.1    Lecuyer, S.2    Stone, H.A.3    Losick, R.4
  • 134
    • 0035154634 scopus 로고    scopus 로고
    • Deletion of the cell-division inhibitor MinC results in lysis of Neisseria gonorrhoeae
    • Ramirez-Arcos S, Szeto J, Beveridge T, Victor C, Francis F, Dillon J. 2001. Deletion of the cell-division inhibitor MinC results in lysis of Neisseria gonorrhoeae. Microbiology 147( Pt 1): 225-237.
    • (2001) Microbiology , vol.147 , Issue.PART 1 , pp. 225-237
    • Ramirez-Arcos, S.1    Szeto, J.2    Beveridge, T.3    Victor, C.4    Francis, F.5    Dillon, J.6
  • 135
    • 0002768045 scopus 로고
    • Experiments concerning the cleavage stimulus in sand dollar eggs
    • Rappaport R. 1961. Experiments concerning the cleavage stimulus in sand dollar eggs. J Exp Zool 148: 81-89.
    • (1961) J Exp Zool , vol.148 , pp. 81-89
    • Rappaport, R.1
  • 136
    • 0022049941 scopus 로고
    • Repeated furrow formation from a single mitotic apparatus in cylindrical sand dollar eggs
    • Rappaport R. 1985. Repeated furrow formation from a single mitotic apparatus in cylindrical sand dollar eggs. J Exp Zool 234( 1): 167-171.
    • (1985) J Exp Zool , vol.234 , Issue.1 , pp. 167-171
    • Rappaport, R.1
  • 137
    • 0032743092 scopus 로고    scopus 로고
    • MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli
    • Raskin DM, de Boer PA. 1999a. MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coli. J Bacteriol 181( 20): 6419-6424.
    • (1999) J Bacteriol , vol.181 , Issue.20 , pp. 6419-6424
    • Raskin, D.M.1    de Boer, P.A.2
  • 138
    • 0033609139 scopus 로고    scopus 로고
    • Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli
    • Raskin DM, de Boer PA. 1999b. Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc Natl Acad Sci USA 96( 9): 4971-4976.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.9 , pp. 4971-4976
    • Raskin, D.M.1    de Boer, P.A.2
  • 139
    • 0033522467 scopus 로고    scopus 로고
    • ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division
    • RayChaudhuri D. 1999. ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division. EMBO J 18( 9): 2372-2383.
    • (1999) EMBO J , vol.18 , Issue.9 , pp. 2372-2383
    • RayChaudhuri, D.1
  • 143
    • 84859230735 scopus 로고    scopus 로고
    • The Min system and nucleoid occlusion are not required for identifying the division site in Bacillus subtilis but ensure its efficient utilization
    • Rodrigues CD, Harry EJ. 2012. The Min system and nucleoid occlusion are not required for identifying the division site in Bacillus subtilis but ensure its efficient utilization. PLoS Genet 8( 3): e1002561.
    • (2012) PLoS Genet , vol.8 , Issue.3
    • Rodrigues, C.D.1    Harry, E.J.2
  • 144
    • 0032161950 scopus 로고    scopus 로고
    • Elevated expression of chitinase 1 and chitin synthesis in myosin II-deficient Saccharomyces cerevisiae
    • Rodriguez-Medina JR, Cruz JA, Robbins PW, Bi E, Pringle JR. 1998. Elevated expression of chitinase 1 and chitin synthesis in myosin II-deficient Saccharomyces cerevisiae. Cell Mol Biol (Noisy-le-grand) 44( 6): 919-925.
    • (1998) Cell Mol Biol (Noisy-le-grand) , vol.44 , Issue.6 , pp. 919-925
    • Rodriguez-Medina, J.R.1    Cruz, J.A.2    Robbins, P.W.3    Bi, E.4    Pringle, J.R.5
  • 145
    • 0035853825 scopus 로고    scopus 로고
    • Polymerization of FtsZ, a bacterial homolog of tubulin. is assembly cooperative?
    • Romberg L, Simon M, Erickson HP. 2001. Polymerization of FtsZ, a bacterial homolog of tubulin. is assembly cooperative? J Biol Chem 276( 15): 11743-11753.
    • (2001) J Biol Chem , vol.276 , Issue.15 , pp. 11743-11753
    • Romberg, L.1    Simon, M.2    Erickson, H.P.3
  • 146
    • 30544445654 scopus 로고    scopus 로고
    • Spatial control of bacterial division-site placement
    • Rothfield L, Taghbalout A, Shih YL. 2005. Spatial control of bacterial division-site placement. Nat Rev Microbiol 3( 12): 959-968.
    • (2005) Nat Rev Microbiol , vol.3 , Issue.12 , pp. 959-968
    • Rothfield, L.1    Taghbalout, A.2    Shih, Y.L.3
  • 147
  • 148
    • 58149230938 scopus 로고    scopus 로고
    • A role for the ESCRT system in cell division in archaea
    • Samson RY, Obita T, Freund SM, Williams RL, Bell SD. 2008. A role for the ESCRT system in cell division in archaea. Science 322( 5908): 1710-1713.
    • (2008) Science , vol.322 , Issue.5908 , pp. 1710-1713
    • Samson, R.Y.1    Obita, T.2    Freund, S.M.3    Williams, R.L.4    Bell, S.D.5
  • 149
    • 78651468723 scopus 로고    scopus 로고
    • Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division
    • Samson RY, Obita T, Hodgson B, Shaw MK, Chong PL, Williams RL, Bell SD. 2011. Molecular and structural basis of ESCRT-III recruitment to membranes during archaeal cell division. Mol Cell 41( 2): 186-196.
    • (2011) Mol Cell , vol.41 , Issue.2 , pp. 186-196
    • Samson, R.Y.1    Obita, T.2    Hodgson, B.3    Shaw, M.K.4    Chong, P.L.5    Williams, R.L.6    Bell, S.D.7
  • 150
    • 0019310212 scopus 로고
    • Banding and polarity of actin filaments in interphase and cleaving cells
    • Sanger JM, Sanger JW. 1980. Banding and polarity of actin filaments in interphase and cleaving cells. J Cell Biol 86( 2): 568-575.
    • (1980) J Cell Biol , vol.86 , Issue.2 , pp. 568-575
    • Sanger, J.M.1    Sanger, J.W.2
  • 151
    • 0014342963 scopus 로고
    • Cytokinesis: filaments in the cleavage furrow
    • Schroeder TE. 1968. Cytokinesis: filaments in the cleavage furrow. Exp Cell Res 53( 1): 272-276.
    • (1968) Exp Cell Res , vol.53 , Issue.1 , pp. 272-276
    • Schroeder, T.E.1
  • 152
    • 0348087045 scopus 로고    scopus 로고
    • A Formin homology protein and a profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans
    • Severson AF, Baillie DL, Bowerman B. 2002. A Formin homology protein and a profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans. Curr Biol 12( 24): 2066-2075.
    • (2002) Curr Biol , vol.12 , Issue.24 , pp. 2066-2075
    • Severson, A.F.1    Baillie, D.L.2    Bowerman, B.3
  • 153
    • 37749010497 scopus 로고    scopus 로고
    • Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function
    • Shiomi D, Margolin W. 2008. Compensation for the loss of the conserved membrane targeting sequence of FtsA provides new insights into its function. Mol Microbiol 67( 3): 558-569.
    • (2008) Mol Microbiol , vol.67 , Issue.3 , pp. 558-569
    • Shiomi, D.1    Margolin, W.2
  • 154
    • 0029806810 scopus 로고    scopus 로고
    • The dmf1/mid1 gene is essential for correct positioning of the division septum in fission yeast
    • Sohrmann M, Fankhauser C, Brodbeck C, Simanis V. 1996. The dmf1/mid1 gene is essential for correct positioning of the division septum in fission yeast. Genes Dev 10( 21): 2707-2719.
    • (1996) Genes Dev , vol.10 , Issue.21 , pp. 2707-2719
    • Sohrmann, M.1    Fankhauser, C.2    Brodbeck, C.3    Simanis, V.4
  • 155
    • 84860585556 scopus 로고    scopus 로고
    • Growth rate and ring width variability of teak, Tectona grandis (Verbenaceae) in an unmanaged forest in East Timor
    • Sousa VB, Cardoso S, Quilho T, Pereira H. 2012. Growth rate and ring width variability of teak, Tectona grandis (Verbenaceae) in an unmanaged forest in East Timor. Rev Biol Trop 60( 1): 483-494.
    • (2012) Rev Biol Trop , vol.60 , Issue.1 , pp. 483-494
    • Sousa, V.B.1    Cardoso, S.2    Quilho, T.3    Pereira, H.4
  • 156
    • 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 MK. 2008. The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast. Genes Dev 22( 13): 1741-1746.
    • (2008) Genes Dev , vol.22 , Issue.13 , pp. 1741-1746
    • Srinivasan, R.1    Mishra, M.2    Wu, L.3    Yin, Z.4    Balasubramanian, M.K.5
  • 158
    • 0037022642 scopus 로고    scopus 로고
    • Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching
    • Stricker J, Maddox P, Salmon ED, Erickson HP. 2002. Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc Natl Acad Sci U S A 99( 5): 3171-3175.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.5 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3    Erickson, H.P.4
  • 159
    • 0035145619 scopus 로고    scopus 로고
    • Influence of the nucleoid on placement of FtsZ and MinE rings in Escherichia coli
    • Sun Q, Margolin W. 2001. Influence of the nucleoid on placement of FtsZ and MinE rings in Escherichia coli. J Bacteriol 183( 4): 1413-1422.
    • (2001) J Bacteriol , vol.183 , Issue.4 , pp. 1413-1422
    • Sun, Q.1    Margolin, W.2
  • 160
    • 2942547429 scopus 로고    scopus 로고
    • Effects of perturbing nucleoid structure on nucleoid occlusion-mediated toporegulation of FtsZ ring assembly
    • Sun Q, Margolin W. 2004. Effects of perturbing nucleoid structure on nucleoid occlusion-mediated toporegulation of FtsZ ring assembly. J Bacteriol 186( 12): 3951-3959.
    • (2004) J Bacteriol , vol.186 , Issue.12 , pp. 3951-3959
    • Sun, Q.1    Margolin, W.2
  • 161
    • 77955489876 scopus 로고    scopus 로고
    • Cytoskeletal cross-linking and bundling in motor-independent contraction
    • Sun SX, Walcott S, Wolgemuth CW. 2010. Cytoskeletal cross-linking and bundling in motor-independent contraction. Curr Biol 20( 15): R649-R654.
    • (2010) Curr Biol , vol.20 , Issue.15
    • Sun, S.X.1    Walcott, S.2    Wolgemuth, C.W.3
  • 162
    • 0035681803 scopus 로고    scopus 로고
    • Gonococcal MinD affects cell division in Neisseria gonorrhoeae and Escherichia coli and exhibits a novel self-interaction
    • Szeto J, Ramirez-Arcos S, Raymond C, Hicks LD, Kay CM, Dillon JA. 2001. Gonococcal MinD affects cell division in Neisseria gonorrhoeae and Escherichia coli and exhibits a novel self-interaction. J Bacteriol 183( 21): 6253-6264.
    • (2001) J Bacteriol , vol.183 , Issue.21 , pp. 6253-6264
    • Szeto, J.1    Ramirez-Arcos, S.2    Raymond, C.3    Hicks, L.D.4    Kay, C.M.5    Dillon, J.A.6
  • 163
    • 84861151969 scopus 로고    scopus 로고
    • FtsA forms actin-like protofilaments
    • Szwedziak P, Wang Q, Freund SM, Lowe J. 2012. FtsA forms actin-like protofilaments. EMBO J 31( 10): 2249-2260.
    • (2012) EMBO J , vol.31 , Issue.10 , pp. 2249-2260
    • Szwedziak, P.1    Wang, Q.2    Freund, S.M.3    Lowe, J.4
  • 164
    • 7944234757 scopus 로고    scopus 로고
    • Organization of a sterol-rich membrane domain by cdc15p during cytokinesis in fission yeast
    • Takeda T, Kawate T, Chang F. 2004. Organization of a sterol-rich membrane domain by cdc15p during cytokinesis in fission yeast. Nat Cell Biol 6( 11): 1142-1144.
    • (2004) Nat Cell Biol , vol.6 , Issue.11 , pp. 1142-1144
    • Takeda, T.1    Kawate, T.2    Chang, F.3
  • 165
    • 33745699284 scopus 로고    scopus 로고
    • MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter
    • Thanbichler M, Shapiro L. 2006. MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter. Cell 126( 1): 147-162.
    • (2006) Cell , vol.126 , Issue.1 , pp. 147-162
    • Thanbichler, M.1    Shapiro, L.2
  • 166
    • 0037326058 scopus 로고    scopus 로고
    • Direct evidence for a critical role of myosin II in budding yeast cytokinesis and the evolvability of new cytokinetic mechanisms in the absence of myosin II
    • Tolliday N, Pitcher M, Li R. 2003. Direct evidence for a critical role of myosin II in budding yeast cytokinesis and the evolvability of new cytokinetic mechanisms in the absence of myosin II. Mol Biol Cell 14( 2): 798-809.
    • (2003) Mol Biol Cell , vol.14 , Issue.2 , pp. 798-809
    • Tolliday, N.1    Pitcher, M.2    Li, R.3
  • 168
    • 0035897404 scopus 로고    scopus 로고
    • A mechanism for nuclear positioning in fission yeast based on microtubule pushing
    • Tran PT, Marsh L, Doye V, Inoue S, Chang F. 2001. A mechanism for nuclear positioning in fission yeast based on microtubule pushing. J Cell Biol 153( 2): 397-411.
    • (2001) J Cell Biol , vol.153 , Issue.2 , pp. 397-411
    • Tran, P.T.1    Marsh, L.2    Doye, V.3    Inoue, S.4    Chang, F.5
  • 169
    • 0017356210 scopus 로고
    • Geometry of cell division in Staphylococcus aureus
    • Tzagoloff H, Novick R. 1977. Geometry of cell division in Staphylococcus aureus. J Bacteriol 129( 1): 343-350.
    • (1977) J Bacteriol , vol.129 , Issue.1 , pp. 343-350
    • Tzagoloff, H.1    Novick, R.2
  • 171
    • 37849017207 scopus 로고    scopus 로고
    • Assembly mechanism of the contractile ring for cytokinesis by fission yeast
    • Vavylonis D, Wu JQ, Hao S, O'Shaughnessy B, Pollard TD. 2008. Assembly mechanism of the contractile ring for cytokinesis by fission yeast. Science 319( 5859): 97-100.
    • (2008) Science , vol.319 , Issue.5859 , pp. 97-100
    • Vavylonis, D.1    Wu, J.Q.2    Hao, S.3    O'Shaughnessy, B.4    Pollard, T.D.5
  • 172
    • 33847307444 scopus 로고    scopus 로고
    • Interphase microtubules determine the initial alignment of the mitotic spindle
    • Vogel SK, Raabe I, Dereli A, Maghelli N, Tolic-Norrelykke I. 2007. Interphase microtubules determine the initial alignment of the mitotic spindle. Curr Biol 17( 5): 438-444.
    • (2007) Curr Biol , vol.17 , Issue.5 , pp. 438-444
    • Vogel, S.K.1    Raabe, I.2    Dereli, A.3    Maghelli, N.4    Tolic-Norrelykke, I.5
  • 173
    • 48249083745 scopus 로고    scopus 로고
    • mDia2 induces the actin scaffold for the contractile ring and stabilizes its position during cytokinesis in NIH 3T3 cells
    • Watanabe S, Ando Y, Yasuda S, Hosoya H, Watanabe N, Ishizaki T, Narumiya S. 2008. mDia2 induces the actin scaffold for the contractile ring and stabilizes its position during cytokinesis in NIH 3T3 cells. Mol Biol Cell 19( 5): 2328-2338.
    • (2008) Mol Biol Cell , vol.19 , Issue.5 , pp. 2328-2338
    • Watanabe, S.1    Ando, Y.2    Yasuda, S.3    Hosoya, H.4    Watanabe, N.5    Ishizaki, T.6    Narumiya, S.7
  • 174
    • 0020614748 scopus 로고
    • On the mechanisms of cytokinesis in animal cells
    • White JG, Borisy GG. 1983. On the mechanisms of cytokinesis in animal cells. J Theor Biol 101( 2): 289-316.
    • (1983) J Theor Biol , vol.101 , Issue.2 , pp. 289-316
    • White, J.G.1    Borisy, G.G.2
  • 175
    • 78650917468 scopus 로고    scopus 로고
    • Positive control of cell division: FtsZ is recruited by SsgB during sporulation of Streptomyces
    • Willemse J, Borst JW, de Waal E, Bisseling T, van Wezel GP. 2011. Positive control of cell division: FtsZ is recruited by SsgB during sporulation of Streptomyces. Genes Dev 25( 1): 89-99.
    • (2011) Genes Dev , vol.25 , Issue.1 , pp. 89-99
    • Willemse, J.1    Borst, J.W.2    de Waal, E.3    Bisseling, T.4    van Wezel, G.P.5
  • 176
    • 0001734652 scopus 로고
    • The mechanics and mechanism of cleavage
    • Wolpert L. 1960. The mechanics and mechanism of cleavage. Int Rev Cytol 10: 163-216.
    • (1960) Int Rev Cytol , vol.10 , pp. 163-216
    • Wolpert, L.1
  • 177
  • 178
    • 2942752105 scopus 로고    scopus 로고
    • Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis
    • Wu LJ, Errington J. 2004. Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis. Cell 117( 7): 915-925.
    • (2004) Cell , vol.117 , Issue.7 , pp. 915-925
    • Wu, L.J.1    Errington, J.2
  • 179
    • 83855160828 scopus 로고    scopus 로고
    • Nucleoid occlusion and bacterial cell division
    • Wu LJ, Errington J. 2012. Nucleoid occlusion and bacterial cell division. Nat Rev Microbiol 10( 1): 8-12.
    • (2012) Nat Rev Microbiol , vol.10 , Issue.1 , pp. 8-12
    • Wu, L.J.1    Errington, J.2
  • 180
    • 67650435786 scopus 로고    scopus 로고
    • Noc protein binds to specific DNA sequences to coordinate cell division with chromosome segregation
    • Wu LJ, Ishikawa S, Kawai Y, Oshima T, Ogasawara N, Errington J. 2009. Noc protein binds to specific DNA sequences to coordinate cell division with chromosome segregation. EMBO J 28( 13): 1940-1952.
    • (2009) EMBO J , vol.28 , Issue.13 , pp. 1940-1952
    • Wu, L.J.1    Ishikawa, S.2    Kawai, Y.3    Oshima, T.4    Ogasawara, N.5    Errington, J.6
  • 181
    • 18844414788 scopus 로고    scopus 로고
    • Balance of actively generated contractile and resistive forces controls cytokinesis dynamics
    • Zhang W, Robinson DN. 2005. Balance of actively generated contractile and resistive forces controls cytokinesis dynamics. Proc Natl Acad Sci USA 102( 20): 7186-7191.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.20 , pp. 7186-7191
    • Zhang, W.1    Robinson, D.N.2
  • 182
    • 38749139916 scopus 로고    scopus 로고
    • Distinct pathways for the early recruitment of myosin II and actin to the cytokinetic furrow
    • Zhou M, Wang YL. 2008. Distinct pathways for the early recruitment of myosin II and actin to the cytokinetic furrow. Mol Biol Cell 19( 1): 318-326.
    • (2008) Mol Biol Cell , vol.19 , Issue.1 , pp. 318-326
    • Zhou, M.1    Wang, Y.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.