메뉴 건너뛰기




Volumn 5, Issue 2, 2013, Pages 63-77

Macromolecular interactions of the bacterial division FtsZ protein: From quantitative biochemistry and crowding to reconstructing minimal divisomes in the test tube

Author keywords

Biophysical methods; Mechanistic biochemistry; Physical biochemistry; Protein membrane interactions; Protein protein interactions; Synthetic biology

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 84877036115     PISSN: 18672450     EISSN: 18672469     Source Type: Journal    
DOI: 10.1007/s12551-013-0115-1     Document Type: Review
Times cited : (20)

References (120)
  • 1
    • 79955662274 scopus 로고    scopus 로고
    • Continuous droplet interface crossing encapsulation (cDICE) for high throughput monodisperse vesicle design
    • Abkarian M, Loiseau E, Massiera G (2011) Continuous droplet interface crossing encapsulation (cDICE) for high throughput monodisperse vesicle design. Soft Matter 7: 4610-4614.
    • (2011) Soft Matter , vol.7 , pp. 4610-4614
    • Abkarian, M.1    Loiseau, E.2    Massiera, G.3
  • 2
    • 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
  • 3
    • 84865611230 scopus 로고    scopus 로고
    • Surface-enhanced raman scattering-based detection of the interactions between the essential cell division ftsz protein and bacterial membrane elements
    • Ahijado-Guzman R, Gomez-Puertas P, Alvarez-Puebla RA, Rivas G, Liz-Marzan LM (2012) Surface-enhanced raman scattering-based detection of the interactions between the essential cell division ftsz protein and bacterial membrane elements. ACS Nano 6(8): 7514-7520.
    • (2012) ACS Nano , vol.6 , Issue.8 , pp. 7514-7520
    • Ahijado-Guzman, R.1    Gomez-Puertas, P.2    Alvarez-Puebla, R.A.3    Rivas, G.4    Liz-Marzan, L.M.5
  • 5
    • 79960339327 scopus 로고    scopus 로고
    • Protein-membrane interactions: the virtue of minimal systems in systems biology
    • Arumugam S, Chwastek G, Schwille P (2011) Protein-membrane interactions: the virtue of minimal systems in systems biology. Wiley Interdiscip Rev Syst Biol Med 3(3): 269-280.
    • (2011) Wiley Interdiscip Rev Syst Biol Med , vol.3 , Issue.3 , pp. 269-280
    • Arumugam, S.1    Chwastek, G.2    Schwille, P.3
  • 6
    • 84869467537 scopus 로고    scopus 로고
    • Surface topology engineering of membranes for the mechanical investigation of the tubulin homologue FtsZ
    • Arumugam S, Chwastek G, Fischer-Friedrich E, Ehrig C, Monch I, Schwille P (2012) Surface topology engineering of membranes for the mechanical investigation of the tubulin homologue FtsZ. Angew Chem 51(47): 11858-11862.
    • (2012) Angew Chem , vol.51 , Issue.47 , pp. 11858-11862
    • Arumugam, S.1    Chwastek, G.2    Fischer-Friedrich, E.3    Ehrig, C.4    Monch, I.5    Schwille, P.6
  • 7
    • 26844533680 scopus 로고    scopus 로고
    • Composition gradient static light scattering: a new technique for rapid detection and quantitative characterization of reversible macromolecular hetero-associations in solution
    • Attri AK, Minton AP (2005a) Composition gradient static light scattering: a new technique for rapid detection and quantitative characterization of reversible macromolecular hetero-associations in solution. Anal Biochem 346(1): 132-138.
    • (2005) Anal Biochem , vol.346 , Issue.1 , pp. 132-138
    • Attri, A.K.1    Minton, A.P.2
  • 8
    • 11844292073 scopus 로고    scopus 로고
    • New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins
    • Attri AK, Minton AP (2005b) New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins. Anal Biochem 337(1): 103-110.
    • (2005) Anal Biochem , vol.337 , Issue.1 , pp. 103-110
    • Attri, A.K.1    Minton, A.P.2
  • 9
    • 48449103699 scopus 로고    scopus 로고
    • Protein-membrane interaction probed by single plasmonic nanoparticles
    • Baciu CL, Becker J, Janshoff A, Sonnichsen C (2008) Protein-membrane interaction probed by single plasmonic nanoparticles. Nano Lett 8(6): 1724-1728.
    • (2008) Nano Lett , vol.8 , Issue.6 , pp. 1724-1728
    • Baciu, C.L.1    Becker, J.2    Janshoff, A.3    Sonnichsen, C.4
  • 10
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into nanodiscs
    • Bayburt TH, Sligar SG (2010) Membrane protein assembly into nanodiscs. FEBS Lett 584(9): 1721-1727.
    • (2010) FEBS Lett , vol.584 , Issue.9 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 12
    • 0022447101 scopus 로고
    • Molecular cloning, DNA sequencing, and enzymatic analyses of two Escherichia coli pyruvate oxidase mutants defective in activation by lipids
    • Chang YY, Cronan JE Jr (1986) Molecular cloning, DNA sequencing, and enzymatic analyses of two Escherichia coli pyruvate oxidase mutants defective in activation by lipids. J Bacteriol 167(1): 312-318.
    • (1986) J Bacteriol , vol.167 , Issue.1 , pp. 312-318
    • Chang, Y.Y.1    Cronan Jr., J.E.2
  • 13
    • 20444457941 scopus 로고    scopus 로고
    • Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer
    • Chen Y, Erickson HP (2005) Rapid in vitro assembly dynamics and subunit turnover of FtsZ demonstrated by fluorescence resonance energy transfer. J Biol Chem 280(23): 22549-22554.
    • (2005) J Biol Chem , vol.280 , Issue.23 , pp. 22549-22554
    • Chen, Y.1    Erickson, H.P.2
  • 14
    • 34547877610 scopus 로고    scopus 로고
    • Fueling protein DNA interactions inside porous nanocontainers
    • Cisse I, Okumus B, Joo C, Ha T (2007) Fueling protein DNA interactions inside porous nanocontainers. Proc Natl Acad Sci USA 104(31): 12646-12650.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.31 , pp. 12646-12650
    • Cisse, I.1    Okumus, B.2    Joo, C.3    Ha, T.4
  • 15
    • 79960968306 scopus 로고    scopus 로고
    • Micro/nanofabricated environments for synthetic biology
    • Collier CP, Simpson ML (2011) Micro/nanofabricated environments for synthetic biology. Curr Opin Biotechnol 22(4): 516-526.
    • (2011) Curr Opin Biotechnol , vol.22 , Issue.4 , pp. 516-526
    • Collier, C.P.1    Simpson, M.L.2
  • 16
    • 0022424027 scopus 로고
    • Specificity of lipid-protein interactions as determined by spectroscopic techniques
    • Devaux PF, Seigneuret M (1985) Specificity of lipid-protein interactions as determined by spectroscopic techniques. Biochim Biophys Acta 822(1): 63-125.
    • (1985) Biochim Biophys Acta , vol.822 , Issue.1 , pp. 63-125
    • Devaux, P.F.1    Seigneuret, M.2
  • 17
    • 32544450348 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy simulations of photophysical phenomena and molecular interactions: a molecular dynamics/Monte Carlo approach
    • Dix JA, Hom EFY, Verkman AS (2006) Fluorescence correlation spectroscopy simulations of photophysical phenomena and molecular interactions: a molecular dynamics/Monte Carlo approach. J Phys Chem B 110(4): 1896-1906.
    • (2006) J Phys Chem B , vol.110 , Issue.4 , pp. 1896-1906
    • Dix, J.A.1    Hom, E.F.Y.2    Verkman, A.S.3
  • 18
    • 84872856522 scopus 로고    scopus 로고
    • The physiology of bacterial cell division
    • Egan AJ, Vollmer W (2013) The physiology of bacterial cell division. Ann N Y Acad Sci 1277(1): 8-28.
    • (2013) Ann N Y Acad Sci , vol.1277 , Issue.1 , pp. 8-28
    • Egan, A.J.1    Vollmer, W.2
  • 19
    • 77951298407 scopus 로고    scopus 로고
    • Models of macromolecular crowding effects and the need for quantitative comparisons with experiment
    • Elcock AH (2010) Models of macromolecular crowding effects and the need for quantitative comparisons with experiment. Curr Opin Struct Biol 20(2): 196-206.
    • (2010) Curr Opin Struct Biol , vol.20 , Issue.2 , pp. 196-206
    • Elcock, A.H.1
  • 20
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis RJ (2001) Macromolecular crowding: obvious but underappreciated. Trends Biochem Sci 26(10): 597-604.
    • (2001) Trends Biochem Sci , vol.26 , Issue.10 , pp. 597-604
    • Ellis, R.J.1
  • 21
    • 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(23): 9238-9243.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.23 , pp. 9238-9243
    • Erickson, H.P.1
  • 22
    • 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
  • 23
    • 77955897900 scopus 로고    scopus 로고
    • Quantitative characterization of polymer-polymer, protein-protein, and polymer-protein interaction via tracer sedimentation equilibrium
    • Fodeke AA, Minton AP (2010) Quantitative characterization of polymer-polymer, protein-protein, and polymer-protein interaction via tracer sedimentation equilibrium. J Phys Chem B 114(33): 10876-10880.
    • (2010) J Phys Chem B , vol.114 , Issue.33 , pp. 10876-10880
    • Fodeke, A.A.1    Minton, A.P.2
  • 26
    • 33947393232 scopus 로고    scopus 로고
    • The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring
    • Geissler B, Shiomi D, Margolin W (2007) The ftsA* gain-of-function allele of Escherichia coli and its effects on the stability and dynamics of the Z ring. Microbiology 153(Pt 3): 814-825.
    • (2007) Microbiology , vol.153 , Issue.Pt 3 , pp. 814-825
    • Geissler, B.1    Shiomi, D.2    Margolin, W.3
  • 27
    • 0242584670 scopus 로고    scopus 로고
    • Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment
    • González JM, Jiménez M, Vélez M, Mingorance J, Andreu JM, Vicente M, Rivas G (2003) Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment. J Biol Chem 278(39): 37664-37671.
    • (2003) J Biol Chem , vol.278 , Issue.39 , pp. 37664-37671
    • González, J.M.1    Jiménez, M.2    Vélez, M.3    Mingorance, J.4    Andreu, J.M.5    Vicente, M.6    Rivas, G.7
  • 28
    • 13844312609 scopus 로고    scopus 로고
    • Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils
    • González JM, Velez M, Jiménez 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 USA 102(6): 1895-1900.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.6 , pp. 1895-1900
    • González, J.M.1    Velez, M.2    Jiménez, M.3    Alfonso, C.4    Schuck, P.5    Mingorance, J.6    Vicente, M.7    Minton, A.P.8    Rivas, G.9
  • 29
    • 0004235628 scopus 로고    scopus 로고
    • 2nd edn., New York: Copernicus Books (Springer Science + Business Media)
    • Goodsell DS (2010) The machinery of life, 2nd edn. Copernicus Books (Springer Science + Business Media), New York.
    • (2010) The Machinery of Life
    • Goodsell, D.S.1
  • 30
    • 0041931122 scopus 로고    scopus 로고
    • Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges
    • Hall D, Minton AP (2003) Macromolecular crowding: qualitative and semiquantitative successes, quantitative challenges. Biochim Biophys Acta 1649(2): 127-139.
    • (2003) Biochim Biophys Acta , vol.1649 , Issue.2 , pp. 127-139
    • Hall, D.1    Minton, A.P.2
  • 31
    • 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
  • 32
    • 84868504605 scopus 로고    scopus 로고
    • Reconstitution of the Escherichia coli cell division ZipA-FtsZ complexes in nanodiscs as revealed by electron microscopy
    • Hernández-Rocamora VM, García-Montañés C, Rivas G, Llorca O (2012a) Reconstitution of the Escherichia coli cell division ZipA-FtsZ complexes in nanodiscs as revealed by electron microscopy. J Struct Biol 180(3): 531-538.
    • (2012) J Struct Biol , vol.180 , Issue.3 , pp. 531-538
    • Hernández-Rocamora, V.M.1    García-Montañés, C.2    Rivas, G.3    Llorca, O.4
  • 35
    • 4544297320 scopus 로고    scopus 로고
    • Crowding-induced organization in cells: spontaneous alignment and sorting of filaments with physiological control points
    • Herzfeld J (2004) Crowding-induced organization in cells: spontaneous alignment and sorting of filaments with physiological control points. J Mol Recognit 17(5): 376-381.
    • (2004) J Mol Recognit , vol.17 , Issue.5 , pp. 376-381
    • Herzfeld, J.1
  • 36
    • 84865560483 scopus 로고    scopus 로고
    • Cell biology. Beyond oil and water-phase transitions in cells
    • Hyman AA, Simons K (2012) Cell biology. Beyond oil and water-phase transitions in cells. Science 337(6098): 1047-1049.
    • (2012) Science , vol.337 , Issue.6098 , pp. 1047-1049
    • Hyman, A.A.1    Simons, K.2
  • 37
    • 33749125215 scopus 로고    scopus 로고
    • Biophysical properties of lipids and dynamic membranes
    • Janmey PA, Kinnunen PK (2006) Biophysical properties of lipids and dynamic membranes. Trends Cell Biol 16(10): 538-546.
    • (2006) Trends Cell Biol , vol.16 , Issue.10 , pp. 538-546
    • Janmey, P.A.1    Kinnunen, P.K.2
  • 38
    • 77955699308 scopus 로고    scopus 로고
    • Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria
    • Jiao M, Li HT, Chen J, Minton AP, Liang Y (2010) Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria. Biophys J 99(3): 914-923.
    • (2010) Biophys J , vol.99 , Issue.3 , pp. 914-923
    • Jiao, M.1    Li, H.T.2    Chen, J.3    Minton, A.P.4    Liang, Y.5
  • 39
    • 34447566117 scopus 로고    scopus 로고
    • Quantitative characterization of weak self-association in concentrated solutions of immunoglobulin G via the measurement of sedimentation equilibrium and osmotic pressure
    • Jimenez M, Rivas G, Minton AP (2007) Quantitative characterization of weak self-association in concentrated solutions of immunoglobulin G via the measurement of sedimentation equilibrium and osmotic pressure. Biochemistry 46(28): 8373-8378.
    • (2007) Biochemistry , vol.46 , Issue.28 , pp. 8373-8378
    • Jimenez, M.1    Rivas, G.2    Minton, A.P.3
  • 40
    • 79953208071 scopus 로고    scopus 로고
    • Reconstitution and organization of Escherichia coli proto-ring elements (FtsZ and FtsA) inside giant unilamellar vesicles obtained from bacterial inner membranes
    • Jiménez M, Martos A, Vicente M, Rivas G (2011) Reconstitution and organization of Escherichia coli proto-ring elements (FtsZ and FtsA) inside giant unilamellar vesicles obtained from bacterial inner membranes. J Biol Chem 286(13): 11236-11241.
    • (2011) J Biol Chem , vol.286 , Issue.13 , pp. 11236-11241
    • Jiménez, M.1    Martos, A.2    Vicente, M.3    Rivas, G.4
  • 41
    • 84870187166 scopus 로고    scopus 로고
    • Aqueous phase separation as a possible route to compartmentalization of biological molecules
    • Keating CD (2012) Aqueous phase separation as a possible route to compartmentalization of biological molecules. Acc Chem Res 45(12): 2114-2124.
    • (2012) Acc Chem Res , vol.45 , Issue.12 , pp. 2114-2124
    • Keating, C.D.1
  • 42
    • 84857738215 scopus 로고    scopus 로고
    • Key role of two terminal domains in the bidirectional polymerization of FtsA protein
    • Krupka M, Rivas G, Rico AI, Vicente M (2012) Key role of two terminal domains in the bidirectional polymerization of FtsA protein. J Biol Chem 287(10): 7756-7765.
    • (2012) J Biol Chem , vol.287 , Issue.10 , pp. 7756-7765
    • Krupka, M.1    Rivas, G.2    Rico, A.I.3    Vicente, M.4
  • 43
    • 0035044484 scopus 로고    scopus 로고
    • Self-organisation and orderly processes by individual protein complexes in the bacterial cell
    • Kuthan H (2001) Self-organisation and orderly processes by individual protein complexes in the bacterial cell. Prog Biophys Mol Biol 75(1-2): 1-17.
    • (2001) Prog Biophys Mol Biol , vol.75 , Issue.1-2 , pp. 1-17
    • Kuthan, H.1
  • 45
    • 69249235852 scopus 로고    scopus 로고
    • Biology under construction: in vitro reconstitution of cellular function
    • Liu AP, Fletcher DA (2009) Biology under construction: in vitro reconstitution of cellular function. Nat Rev 10(9): 644-650.
    • (2009) Nat Rev , vol.10 , Issue.9 , pp. 644-650
    • Liu, A.P.1    Fletcher, D.A.2
  • 46
    • 44049091101 scopus 로고    scopus 로고
    • Spatial regulators for bacterial cell division self-organize into surface waves in vitro
    • Loose M, Fischer-Friedrich E, Ries J, Kruse K, Schwille P (2008) Spatial regulators for bacterial cell division self-organize into surface waves in vitro. Science (New York) 320(5877): 789-792.
    • (2008) Science (New York) , vol.320 , Issue.5877 , pp. 789-792
    • Loose, M.1    Fischer-Friedrich, E.2    Ries, J.3    Kruse, K.4    Schwille, P.5
  • 47
    • 79955571598 scopus 로고    scopus 로고
    • Min protein patterns emerge from rapid rebinding and membrane interaction of MinE
    • Loose M, Fischer-Friedrich E, Herold C, Kruse K, Schwille P (2011a) Min protein patterns emerge from rapid rebinding and membrane interaction of MinE. Nat Struct Mol Biol 18(5): 577-583.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.5 , pp. 577-583
    • Loose, M.1    Fischer-Friedrich, E.2    Herold, C.3    Kruse, K.4    Schwille, P.5
  • 48
    • 79955855203 scopus 로고    scopus 로고
    • Protein self-organization: lessons from the min system
    • Loose M, Kruse K, Schwille P (2011b) Protein self-organization: lessons from the min system. Annu Rev Biophys 40: 315-336.
    • (2011) Annu Rev Biophys , vol.40 , pp. 315-336
    • Loose, M.1    Kruse, K.2    Schwille, P.3
  • 49
    • 71649100145 scopus 로고    scopus 로고
    • Lipid domains and mechanical plasticity of Escherichia coli lipid monolayers
    • Lopez-Montero I, Arriaga LR, Rivas G, Velez M, Monroy F (2010) Lipid domains and mechanical plasticity of Escherichia coli lipid monolayers. Chem Phys Lipids 163(1): 56-63.
    • (2010) Chem Phys Lipids , vol.163 , Issue.1 , pp. 56-63
    • Lopez-Montero, I.1    Arriaga, L.R.2    Rivas, G.3    Velez, M.4    Monroy, F.5
  • 51
    • 84870297573 scopus 로고    scopus 로고
    • Membrane reconstruction of FtsZ-ZipA complex inside giant spherical vesicles made of E. coli lipid: large membrane dilation and analysis of membrane plasticity
    • Lopez-Montero I, Lopez-Navajas P, Mingorance J, Velez M, Vicente M, Monroy F (2013) Membrane reconstruction of FtsZ-ZipA complex inside giant spherical vesicles made of E. coli lipid: large membrane dilation and analysis of membrane plasticity. Biochim Biophys Acta 1828: 687-698.
    • (2013) Biochim Biophys Acta , vol.1828 , pp. 687-698
    • Lopez-Montero, I.1    Lopez-Navajas, P.2    Mingorance, J.3    Velez, M.4    Vicente, M.5    Monroy, F.6
  • 52
    • 0031968795 scopus 로고    scopus 로고
    • FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima-quantitation, GTP hydrolysis, and assembly
    • Lu C, Stricker J, Erickson HP (1998) FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima-quantitation, GTP hydrolysis, and assembly. Cell Motil Cytoskeleton 40(1): 71-86.
    • (1998) Cell Motil Cytoskeleton , vol.40 , Issue.1 , pp. 71-86
    • Lu, C.1    Stricker, J.2    Erickson, H.P.3
  • 53
    • 84867995401 scopus 로고    scopus 로고
    • Bacterial cytokinesis: from Z ring to divisome
    • Lutkenhaus J, Pichoff S, Du S (2012) Bacterial cytokinesis: from Z ring to divisome. Cytoskeleton (Hoboken) 69(10): 778-790.
    • (2012) Cytoskeleton (Hoboken) , vol.69 , Issue.10 , pp. 778-790
    • Lutkenhaus, J.1    Pichoff, S.2    Du, S.3
  • 54
    • 84859579073 scopus 로고    scopus 로고
    • Assembly of MreB filaments on liposome membranes: a synthetic biology approach
    • Maeda YT, Nakadai T, Shin J, Uryu K, Noireaux V, Libchaber A (2012) Assembly of MreB filaments on liposome membranes: a synthetic biology approach. ACS Synth Biol 1(2): 53-59.
    • (2012) ACS Synth Biol , vol.1 , Issue.2 , pp. 53-59
    • Maeda, Y.T.1    Nakadai, T.2    Shin, J.3    Uryu, K.4    Noireaux, V.5    Libchaber, A.6
  • 55
    • 0034192445 scopus 로고    scopus 로고
    • Organelle division: self-assembling GTPase caught in the middle
    • Margolin W (2000) Organelle division: self-assembling GTPase caught in the middle. Curr Biol 10(9): R328-R330.
    • (2000) Curr Biol , vol.10 , Issue.9
    • Margolin, W.1
  • 56
    • 84856457757 scopus 로고    scopus 로고
    • Polymersomes in "gelly" polymersomes: toward structural cell mimicry
    • Marguet M, Sandre O, Lecommandoux S (2012) Polymersomes in "gelly" polymersomes: toward structural cell mimicry. Langmuir 28(4): 2035-2043.
    • (2012) Langmuir , vol.28 , Issue.4 , pp. 2035-2043
    • Marguet, M.1    Sandre, O.2    Lecommandoux, S.3
  • 58
    • 78650435603 scopus 로고    scopus 로고
    • Characterization of self-association and heteroassociation of bacterial cell division proteins FtsZ and ZipA in solution by composition gradient-static light scattering
    • Martos A, Alfonso C, López-Navajas P, Ahijado-Guzman R, Mingorance J, Minton AP, Rivas G (2010) Characterization of self-association and heteroassociation of bacterial cell division proteins FtsZ and ZipA in solution by composition gradient-static light scattering. Biochemistry 49(51): 10780-10787.
    • (2010) Biochemistry , vol.49 , Issue.51 , pp. 10780-10787
    • Martos, A.1    Alfonso, C.2    López-Navajas, P.3    Ahijado-Guzman, R.4    Mingorance, J.5    Minton, A.P.6    Rivas, G.7
  • 59
    • 84869878393 scopus 로고    scopus 로고
    • Towards a bottom-up reconstitution of bacterial cell division
    • Martos A, Jimenez M, Rivas G, Schwille P (2012a) Towards a bottom-up reconstitution of bacterial cell division. Trends Cell Biol 22(12): 634-643.
    • (2012) Trends Cell Biol , vol.22 , Issue.12 , pp. 634-643
    • Martos, A.1    Jimenez, M.2    Rivas, G.3    Schwille, P.4
  • 60
    • 84862988236 scopus 로고    scopus 로고
    • Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli
    • Martos A, Monterroso B, Zorrilla S, Reija B, Alfonso C, Mingorance J, Rivas G, Jimenez M (2012b) Isolation, characterization and lipid-binding properties of the recalcitrant FtsA division protein from Escherichia coli. PLoS One 7(6): e39829.
    • (2012) PLoS One , vol.7 , Issue.6
    • Martos, A.1    Monterroso, B.2    Zorrilla, S.3    Reija, B.4    Alfonso, C.5    Mingorance, J.6    Rivas, G.7    Jimenez, M.8
  • 62
    • 84867438840 scopus 로고    scopus 로고
    • Synthesizing artificial cells from giant unilamellar vesicles: state-of-the art in the development of microfluidic technology
    • Matosevic S (2012) Synthesizing artificial cells from giant unilamellar vesicles: state-of-the art in the development of microfluidic technology. Bioessays 34(11): 992-1001.
    • (2012) Bioessays , vol.34 , Issue.11 , pp. 992-1001
    • Matosevic, S.1
  • 63
    • 0039940808 scopus 로고    scopus 로고
    • Control of the structural stability of the tubulin dimer by one high affinity bound magnesium ion at nucleotide N-site
    • Menendez M, Rivas G, Diaz JF, Andreu JM (1998) Control of the structural stability of the tubulin dimer by one high affinity bound magnesium ion at nucleotide N-site. J Biol Chem 273(1): 167-176.
    • (1998) J Biol Chem , vol.273 , Issue.1 , pp. 167-176
    • Menendez, M.1    Rivas, G.2    Diaz, J.F.3    Andreu, J.M.4
  • 65
    • 0020668187 scopus 로고
    • The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences
    • Minton AP (1983) The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences. Mol Cell Biochem 55(2): 119-140.
    • (1983) Mol Cell Biochem , vol.55 , Issue.2 , pp. 119-140
    • Minton, A.P.1
  • 66
    • 0025018285 scopus 로고
    • Holobiochemistry: the effect of local environment upon the equilibria and rates of biochemical reactions
    • Minton AP (1990) Holobiochemistry: the effect of local environment upon the equilibria and rates of biochemical reactions. Int J Biochem 22(10): 1063-1067.
    • (1990) Int J Biochem , vol.22 , Issue.10 , pp. 1063-1067
    • Minton, A.P.1
  • 67
    • 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(1): 34-39.
    • (2000) Curr Opin Struct Biol , vol.10 , Issue.1 , pp. 34-39
    • Minton, A.P.1
  • 68
    • 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(14): 10577-10580.
    • (2001) J Biol Chem , vol.276 , Issue.14 , pp. 10577-10580
    • Minton, A.P.1
  • 69
    • 33746813983 scopus 로고    scopus 로고
    • How can biochemical reactions within cells differ from those in test tubes?
    • Minton AP (2006) How can biochemical reactions within cells differ from those in test tubes? J Cell Sci 119(Pt 14): 2863-2869.
    • (2006) J Cell Sci , vol.119 , Issue.Pt 14 , pp. 2863-2869
    • Minton, A.P.1
  • 70
    • 84864951977 scopus 로고    scopus 로고
    • Hard quasispherical particle models for the viscosity of solutions of protein mixtures
    • Minton AP (2012) Hard quasispherical particle models for the viscosity of solutions of protein mixtures. J Phys Chem B 116(31): 9310-9315.
    • (2012) J Phys Chem B , vol.116 , Issue.31 , pp. 9310-9315
    • Minton, A.P.1
  • 71
    • 84872904773 scopus 로고    scopus 로고
    • Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding
    • Minton AP (2013) Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding. Biopolymers 99(4): 239-244.
    • (2013) Biopolymers , vol.99 , Issue.4 , pp. 239-244
    • Minton, A.P.1
  • 72
    • 0019883893 scopus 로고
    • Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase
    • Minton AP, Wilf J (1981) Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 20(17): 4821-4826.
    • (1981) Biochemistry , vol.20 , Issue.17 , pp. 4821-4826
    • Minton, A.P.1    Wilf, J.2
  • 73
    • 84861850277 scopus 로고    scopus 로고
    • Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue involves the concerted formation of a narrow size distribution of oligomeric species
    • Monterroso B, Ahijado-Guzman R, Reija B, Alfonso C, Zorrilla S, Minton AP, Rivas G (2012a) Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue involves the concerted formation of a narrow size distribution of oligomeric species. Biochemistry 51: 4541-4550.
    • (2012) Biochemistry , vol.51 , pp. 4541-4550
    • Monterroso, B.1    Ahijado-Guzman, R.2    Reija, B.3    Alfonso, C.4    Zorrilla, S.5    Minton, A.P.6    Rivas, G.7
  • 74
    • 84864668991 scopus 로고    scopus 로고
    • An equilibrium model for the Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue
    • Monterroso B, Rivas G, Minton AP (2012b) An equilibrium model for the Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue. Biochemistry 51: 6108-6113.
    • (2012) Biochemistry , vol.51 , pp. 6108-6113
    • Monterroso, B.1    Rivas, G.2    Minton, A.P.3
  • 75
    • 79960335864 scopus 로고    scopus 로고
    • Modulation of functionally significant conformational equilibria in adenylate kinase by high concentrations of trimethylamine oxide attributed to volume exclusion
    • Nagarajan S, Amir D, Grupi A, Goldenberg DP, Minton AP, Haas E (2011) Modulation of functionally significant conformational equilibria in adenylate kinase by high concentrations of trimethylamine oxide attributed to volume exclusion. Biophys J 100(12): 2991-2999.
    • (2011) Biophys J , vol.100 , Issue.12 , pp. 2991-2999
    • Nagarajan, S.1    Amir, D.2    Grupi, A.3    Goldenberg, D.P.4    Minton, A.P.5    Haas, E.6
  • 76
    • 0031912354 scopus 로고    scopus 로고
    • Morphogenesis of Escherichia coli
    • Nanninga N (1998) Morphogenesis of Escherichia coli. Microbiol Mol Biol Rev 62(1): 110-129.
    • (1998) Microbiol Mol Biol Rev , vol.62 , Issue.1 , pp. 110-129
    • Nanninga, N.1
  • 77
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • Nath A, Atkins WM, Sligar SG (2007) Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins. Biochemistry 46(8): 2059-2069.
    • (2007) Biochemistry , vol.46 , Issue.8 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 78
    • 79952775158 scopus 로고    scopus 로고
    • Development of an artificial cell, from self-organization to computation and self-reproduction
    • Noireaux V, Maeda YT, Libchaber A (2011) Development of an artificial cell, from self-organization to computation and self-reproduction. Proc Natl Acad Sci USA 108(9): 3473-3480.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.9 , pp. 3473-3480
    • Noireaux, V.1    Maeda, Y.T.2    Libchaber, A.3
  • 79
    • 0036063886 scopus 로고    scopus 로고
    • Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain
    • Ohashi T, Hale CA, de Boer PA, Erickson HP (2002) Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain. J Bacteriol 184(15): 4313-4315.
    • (2002) J Bacteriol , vol.184 , Issue.15 , pp. 4313-4315
    • Ohashi, T.1    Hale, C.A.2    de Boer, P.A.3    Erickson, H.P.4
  • 80
    • 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
  • 81
    • 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
  • 82
    • 84873286335 scopus 로고    scopus 로고
    • A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein
    • Pazos M, Natale P, Vicente M (2012) A specific role for the ZipA protein in cell division: stabilization of the FtsZ protein. J Biol Chem 288(5): 3219-3226.
    • (2012) J Biol Chem , vol.288 , Issue.5 , pp. 3219-3226
    • Pazos, M.1    Natale, P.2    Vicente, M.3
  • 83
    • 84855714089 scopus 로고    scopus 로고
    • From polymeric nanoreactors to artificial organelles
    • Peters RJRW, Louzao I, van Hest JCM (2012) From polymeric nanoreactors to artificial organelles. Chem Sci 3(2): 335-342.
    • (2012) Chem Sci , vol.3 , Issue.2 , pp. 335-342
    • Peters, R.J.R.W.1    Louzao, I.2    van Hest, J.C.M.3
  • 84
    • 84876062242 scopus 로고    scopus 로고
    • Formation of protein complexes in crowded environments-From in vitro to in vivo
    • doi:10.1016/j.febslet.2013.01.007
    • Phillip Y, Schreiber G (2013) Formation of protein complexes in crowded environments-From in vitro to in vivo. FEBS Lett. doi: 10. 1016/j. febslet. 2013. 01. 007.
    • (2013) FEBS Lett
    • Phillip, Y.1    Schreiber, G.2
  • 85
    • 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
  • 86
    • 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
  • 87
    • 67249144043 scopus 로고    scopus 로고
    • FtsZ condensates: an in vitro electron microscopy study
    • Popp D, Iwasa M, Narita A, Erickson HP, Maeda Y (2009) FtsZ condensates: an in vitro electron microscopy study. Biopolymers 91(5): 340-350.
    • (2009) Biopolymers , vol.91 , Issue.5 , pp. 340-350
    • Popp, D.1    Iwasa, M.2    Narita, A.3    Erickson, H.P.4    Maeda, Y.5
  • 88
    • 0032079008 scopus 로고    scopus 로고
    • Biophysical compensation mechanisms buffering E-coli protein-nucleic acid interactions against changing environments
    • Record MT, Courtenay ES, Cayley S, Guttman HJ (1998) Biophysical compensation mechanisms buffering E-coli protein-nucleic acid interactions against changing environments. Trends Biochem Sci 23(5): 190-194.
    • (1998) Trends Biochem Sci , vol.23 , Issue.5 , pp. 190-194
    • Record, M.T.1    Courtenay, E.S.2    Cayley, S.3    Guttman, H.J.4
  • 89
    • 80052265964 scopus 로고    scopus 로고
    • Development of a homogeneous fluorescence anisotropy assay to monitor and measure FtsZ assembly in solution
    • Reija B, Monterroso B, Jiménez M, Vicente M, Rivas G, Zorrilla S (2011) Development of a homogeneous fluorescence anisotropy assay to monitor and measure FtsZ assembly in solution. Anal Biochem 418(1): 89-96.
    • (2011) Anal Biochem , vol.418 , Issue.1 , pp. 89-96
    • Reija, B.1    Monterroso, B.2    Jiménez, M.3    Vicente, M.4    Rivas, G.5    Zorrilla, S.6
  • 91
    • 4544353906 scopus 로고    scopus 로고
    • Non-ideal tracer sedimentation equilibrium: a powerful tool for the characterization of macromolecular interactions in crowded solutions
    • Rivas G, Minton AP (2004) Non-ideal tracer sedimentation equilibrium: a powerful tool for the characterization of macromolecular interactions in crowded solutions. J Mol Recognit 17(5): 362-367.
    • (2004) J Mol Recognit , vol.17 , Issue.5 , pp. 362-367
    • Rivas, G.1    Minton, A.P.2
  • 92
    • 0033587619 scopus 로고    scopus 로고
    • Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: theory, experiment, and biological significance
    • Rivas G, Fernandez JA, Minton AP (1999) Direct observation of the self-association of dilute proteins in the presence of inert macromolecules at high concentration via tracer sedimentation equilibrium: theory, experiment, and biological significance. Biochemistry 38(29): 9379-9388.
    • (1999) Biochemistry , vol.38 , Issue.29 , pp. 9379-9388
    • Rivas, G.1    Fernandez, J.A.2    Minton, A.P.3
  • 93
    • 0040735625 scopus 로고    scopus 로고
    • Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly
    • Rivas G, López A, Mingorance J, Ferrándiz MJ, Zorrilla S, Minton AP, Vicente M, Andreu JM (2000) Magnesium-induced linear self-association of the FtsZ bacterial cell division protein monomer. The primary steps for FtsZ assembly. The J Biol Chem 275(16): 11740-11749.
    • (2000) The J Biol Chem , vol.275 , Issue.16 , pp. 11740-11749
    • Rivas, G.1    López, A.2    Mingorance, J.3    Ferrándiz, M.J.4    Zorrilla, S.5    Minton, A.P.6    Vicente, M.7    Andreu, J.M.8
  • 94
    • 0035853141 scopus 로고    scopus 로고
    • Direct observation of the enhancement of noncooperative protein self-assembly by macromolecular crowding: Indefinite linear self-association of bacterial cell division protein FtsZ
    • Rivas G, Fernandez JA, Minton AP (2001) Direct observation of the enhancement of noncooperative protein self-assembly by macromolecular crowding: Indefinite linear self-association of bacterial cell division protein FtsZ. Proc Natl Acad Sci USA 98(6): 3150-3155.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.6 , pp. 3150-3155
    • Rivas, G.1    Fernandez, J.A.2    Minton, A.P.3
  • 95
    • 0038191051 scopus 로고    scopus 로고
    • Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle
    • Rueda S, Vicente M, Mingorance J (2003) Concentration and assembly of the division ring proteins FtsZ, FtsA, and ZipA during the Escherichia coli cell cycle. J Bacteriol 185(11): 3344-3351.
    • (2003) J Bacteriol , vol.185 , Issue.11 , pp. 3344-3351
    • Rueda, S.1    Vicente, M.2    Mingorance, J.3
  • 96
    • 82555170224 scopus 로고    scopus 로고
    • Independence between GTPase active sites in the Escherichia coli cell division protein FtsZ
    • Salvarelli E, Krupka M, Rivas G, Vicente M, Mingorance J (2011) Independence between GTPase active sites in the Escherichia coli cell division protein FtsZ. FEBS Lett 585(24): 3880-3883.
    • (2011) FEBS Lett , vol.585 , Issue.24 , pp. 3880-3883
    • Salvarelli, E.1    Krupka, M.2    Rivas, G.3    Vicente, M.4    Mingorance, J.5
  • 98
    • 84864658884 scopus 로고    scopus 로고
    • Model membrane platforms to study protein-membrane interactions
    • Sezgin E, Schwille P (2012) Model membrane platforms to study protein-membrane interactions. Mol Membr Biol 29(5): 144-154.
    • (2012) Mol Membr Biol , vol.29 , Issue.5 , pp. 144-154
    • Sezgin, E.1    Schwille, P.2
  • 99
    • 66749128608 scopus 로고    scopus 로고
    • The role of biomacromolecular crowding, ionic strength, and physicochemical gradients in the complexities of life's emergence
    • Spitzer J, Poolman B (2009) The role of biomacromolecular crowding, ionic strength, and physicochemical gradients in the complexities of life's emergence. Microbiol Mol Biol Rev 73(2): 371-388.
    • (2009) Microbiol Mol Biol Rev , vol.73 , Issue.2 , pp. 371-388
    • Spitzer, J.1    Poolman, B.2
  • 101
    • 84866719247 scopus 로고    scopus 로고
    • 3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesis
    • Strauss MP, Liew AT, Turnbull L, Whitchurch CB, Monahan LG, Harry EJ (2012) 3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesis. PLoS Biol 10(9): e1001389.
    • (2012) PLoS Biol , vol.10 , Issue.9
    • Strauss, M.P.1    Liew, A.T.2    Turnbull, L.3    Whitchurch, C.B.4    Monahan, L.G.5    Harry, E.J.6
  • 102
    • 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 USA 99(5): 3171-3175.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.5 , pp. 3171-3175
    • Stricker, J.1    Maddox, P.2    Salmon, E.D.3    Erickson, H.P.4
  • 103
    • 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
  • 104
    • 80052724799 scopus 로고    scopus 로고
    • Transformation of actoHMM assembly confined in cell-sized liposome
    • Takiguchi K, Negishi M, Tanaka-Takiguchi Y, Homma M, Yoshikawa K (2011) Transformation of actoHMM assembly confined in cell-sized liposome. Langmuir 27(18): 11528-11535.
    • (2011) Langmuir , vol.27 , Issue.18 , pp. 11528-11535
    • Takiguchi, K.1    Negishi, M.2    Tanaka-Takiguchi, Y.3    Homma, M.4    Yoshikawa, K.5
  • 107
    • 79551513164 scopus 로고    scopus 로고
    • Single-molecule approaches to characterizing kinetics of biomolecular interactions
    • van Oijen AM (2010) Single-molecule approaches to characterizing kinetics of biomolecular interactions. Curr Opin Biotechnol 22(1): 75-80.
    • (2010) Curr Opin Biotechnol , vol.22 , Issue.1 , pp. 75-80
    • van Oijen, A.M.1
  • 108
    • 79251640891 scopus 로고    scopus 로고
    • An inventory of the bacterial macromolecular components and their spatial organization
    • Vendeville A, Lariviere D, Fourmentin E (2011) An inventory of the bacterial macromolecular components and their spatial organization. FEMS Microbiol Rev 35(2): 395-414.
    • (2011) FEMS Microbiol Rev , vol.35 , Issue.2 , pp. 395-414
    • Vendeville, A.1    Lariviere, D.2    Fourmentin, E.3
  • 109
    • 84907343179 scopus 로고    scopus 로고
    • Crystal ball: Will test tubes ever undergo division?
    • Vicente M (2013) Crystal ball: Will test tubes ever undergo division? Microbiol Biotechnol 6: 3-16.
    • (2013) Microbiol Biotechnol , vol.6 , pp. 3-16
    • Vicente, M.1
  • 110
    • 33745209434 scopus 로고    scopus 로고
    • The order of the ring: assembly of Escherichia coli cell division components
    • Vicente M, Rico AI (2006) The order of the ring: assembly of Escherichia coli cell division components. Mol Microbiol 61(1): 5-8.
    • (2006) Mol Microbiol , vol.61 , Issue.1 , pp. 5-8
    • Vicente, M.1    Rico, A.I.2
  • 111
    • 77951716555 scopus 로고    scopus 로고
    • Giant vesicles: preparations and applications
    • Walde P, Cosentino K, Engel H, Stano P (2010) Giant vesicles: preparations and applications. ChemBioChem 11(7): 848-865.
    • (2010) ChemBioChem , vol.11 , Issue.7 , pp. 848-865
    • Walde, P.1    Cosentino, K.2    Engel, H.3    Stano, P.4
  • 112
    • 0019890347 scopus 로고
    • Evidence for protein self-association induced by excluded volume. Myoglobin in the presence of globular proteins
    • Wilf J, Minton AP (1981) Evidence for protein self-association induced by excluded volume. Myoglobin in the presence of globular proteins. Biochim Biophys Acta 670(3): 316-322.
    • (1981) Biochim Biophys Acta , vol.670 , Issue.3 , pp. 316-322
    • Wilf, J.1    Minton, A.P.2
  • 113
    • 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
  • 114
    • 0034682668 scopus 로고    scopus 로고
    • The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins
    • Zhang B, Zhang Y, Wang Z, Zheng Y (2000) The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins. J Biol Chem 275(33): 25299-25307.
    • (2000) J Biol Chem , vol.275 , Issue.33 , pp. 25299-25307
    • Zhang, B.1    Zhang, Y.2    Wang, Z.3    Zheng, Y.4
  • 115
    • 84876034428 scopus 로고    scopus 로고
    • Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling
    • doi:10.1016/j.febslet.2013.01.064
    • Zhou HX (2013) Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling. FEBS Lett. doi: 10. 1016/j. febslet. 2013. 01. 064.
    • (2013) FEBS Lett
    • Zhou, H.X.1
  • 116
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences
    • Zhou HX, Rivas G, Minton AP (2008) Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu Rev Biophys 37: 375-397.
    • (2008) Annu Rev Biophys , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 117
    • 84872000068 scopus 로고    scopus 로고
    • Reconstitution of pole-to-pole oscillations of min proteins in microengineered polydimethylsiloxane compartments
    • Zieske K, Schwille P (2012) Reconstitution of pole-to-pole oscillations of min proteins in microengineered polydimethylsiloxane compartments. Angew Chem 52(1): 459-462.
    • (2012) Angew Chem , vol.52 , Issue.1 , pp. 459-462
    • Zieske, K.1    Schwille, P.2
  • 118
    • 33750510057 scopus 로고    scopus 로고
    • Shape and compaction of Escherichia coli nucleoids
    • Zimmerman SB (2006) Shape and compaction of Escherichia coli nucleoids. J Struct Biol 156(2): 255-261.
    • (2006) J Struct Biol , vol.156 , Issue.2 , pp. 255-261
    • Zimmerman, S.B.1
  • 119
    • 1642285049 scopus 로고    scopus 로고
    • Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: theory and application to concentrated solutions of ribonuclease
    • Zorrilla S, Jimenez M, Lillo P, Rivas G, Minton AP (2004a) Sedimentation equilibrium in a solution containing an arbitrary number of solute species at arbitrary concentrations: theory and application to concentrated solutions of ribonuclease. Biophys Chem 108(1-3): 89-100.
    • (2004) Biophys Chem , vol.108 , Issue.1-3 , pp. 89-100
    • Zorrilla, S.1    Jimenez, M.2    Lillo, P.3    Rivas, G.4    Minton, A.P.5
  • 120
    • 4544321668 scopus 로고    scopus 로고
    • Protein self-association in crowded protein solutions: a time-resolved fluorescence polarization study
    • Zorrilla S, Rivas G, Acuna AU, Lillo MP (2004b) Protein self-association in crowded protein solutions: a time-resolved fluorescence polarization study. Protein Sci 13(11): 2960-2969.
    • (2004) Protein Sci , vol.13 , Issue.11 , pp. 2960-2969
    • Zorrilla, S.1    Rivas, G.2    Acuna, A.U.3    Lillo, M.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.