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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE
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Includes an impressive EM image of MinD bound to phospholipid vesicles and assembled into a helical array that deformed the vesicles into tubes in the presence of ATP. Addition of MinE stimulated MinD's ATPase and caused its release from the vesicles.
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Hu Z., Gogol E.P., Lutkenhaus J. Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE. Proc Natl Acad Sci USA. 99:2002;6761-6766 Includes an impressive EM image of MinD bound to phospholipid vesicles and assembled into a helical array that deformed the vesicles into tubes in the presence of ATP. Addition of MinE stimulated MinD's ATPase and caused its release from the vesicles.
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(2002)
Proc Natl Acad Sci USA
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Hu, Z.1
Gogol, E.P.2
Lutkenhaus, J.3
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45
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0037310283
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ATP-dependent interactions between Escherichia coli Min proteins and the phospholipid membrane in vitro
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Lackner L.L., Raskin D.M., de Boer P.A.J. ATP-dependent interactions between Escherichia coli Min proteins and the phospholipid membrane in vitro. J Bacteriol. 185:2003;735-749.
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J Bacteriol
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Lackner, L.L.1
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46
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0037215535
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Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: Role of MinD and MinE
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A more detailed study. In the absence of lipid, ATP causes MinD to dimerize and form a rather unstable complex with MinC. However, MinD binds well to lipid vesicles in the presence of ATP and then recruits MinC. If MinD release via ATP hydrolysis is prevented, MinE can displace MinC that is bound to the MinD-lipid complex but MinC does not displace bound MinE.
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Hu Z., Saez C., Lutkenhaus J. Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE. J Bacteriol. 185:2003;196-203 A more detailed study. In the absence of lipid, ATP causes MinD to dimerize and form a rather unstable complex with MinC. However, MinD binds well to lipid vesicles in the presence of ATP and then recruits MinC. If MinD release via ATP hydrolysis is prevented, MinE can displace MinC that is bound to the MinD-lipid complex but MinC does not displace bound MinE.
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(2003)
J Bacteriol
, vol.185
, pp. 196-203
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Hu, Z.1
Saez, C.2
Lutkenhaus, J.3
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47
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0037699937
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Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles
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••]. The MreB and MinCDE coiled arrays do not appear identical but this point needs to be confirmed by co-labeling the proteins in the same cells.
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••]. The MreB and MinCDE coiled arrays do not appear identical but this point needs to be confirmed by co-labeling the proteins in the same cells.
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(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 7865-7870
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Shih, Y.-L.1
Le, T.2
Rothfield, L.3
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48
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Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms
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Niemann H.H., Knetsch M.L.W., Scherer A., Manstein D.J., Kull F.J. Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms. EMBO J. 20:2001;5813-5821.
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EMBO J
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Niemann, H.H.1
Knetsch, M.L.W.2
Scherer, A.3
Manstein, D.J.4
Kull, F.J.5
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49
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Dynamin and its role in membrane fission
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Hinshaw J.E. Dynamin and its role in membrane fission. Annu Rev Cell Dev Biol. 16:2000;483-519.
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Annu Rev Cell Dev Biol
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Hinshaw, J.E.1
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50
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Three-dimensional reconstruction of dynamin in the constricted state
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Zhang P., Hinshaw J.E. Three-dimensional reconstruction of dynamin in the constricted state. Nat Cell Biol. 3:2001;922-927.
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Nat Cell Biol
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Zhang, P.1
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51
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Structural and functional studies of MinD ATPase: Implications for the molecular recognition of the bacterial cell division apparatus
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Hayashi I., Oyama T., Morikawa K. Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus. EMBO J. 20:2001;1819-1828.
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Cordell S.C., Löwe J. Crystal structure of the bacterial cell division regulator MinD. FEBS Lett. 492:2001;160-165.
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FEBS Lett
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Cordell, S.C.1
Löwe, J.2
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0034989071
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The MinD protein from the hyperthermophilic archaeon Pyrococcus horikoshii: Crystallization and preliminary X-ray analysis
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Sakai N., Itou H., Watanabe N., Yao M., Tanaka I. The MinD protein from the hyperthermophilic archaeon Pyrococcus horikoshii: crystallization and preliminary X-ray analysis. Acta Crystallogr D Biol Crystallogr. 57:2001;896-897.
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Sakai, N.1
Itou, H.2
Watanabe, N.3
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Tanaka, I.5
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0036295212
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Classification and evolution of P-loop GTPases and related ATPases
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Leipe D.D., Wolf Y.I., Koonin E.V., Aravind L. Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol. 317:2002;41-72.
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J Mol Biol
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Leipe, D.D.1
Wolf, Y.I.2
Koonin, E.V.3
Aravind, L.4
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55
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0037180562
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Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts
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Szeto T.H., Rowland S.L., Rothfield L.I., King G.F. Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts. Proc Natl Acad Sci USA. 99:2002;15693-15698.
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, vol.99
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Szeto, T.H.1
Rowland, S.L.2
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King, G.F.4
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56
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0037241005
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A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum
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Hu Z.L., Lutkenhaus J. A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum. Mol Microbiol. 47:2003;345-355.
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Mol Microbiol
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Hu, Z.L.1
Lutkenhaus, J.2
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57
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0037126071
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Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus
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Martin W., Rujan T., Richly E., Hansen A., Cornelsen S., Lins T., Leister D., Stoebe B., Hasegawa M., Penny D. Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus. Proc Natl Acad Sci USA. 99:2002;12246-12251.
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Proc Natl Acad Sci USA
, vol.99
, pp. 12246-12251
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Martin, W.1
Rujan, T.2
Richly, E.3
Hansen, A.4
Cornelsen, S.5
Lins, T.6
Leister, D.7
Stoebe, B.8
Hasegawa, M.9
Penny, D.10
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58
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0035795421
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FtsZ ring formation at the chloroplast division site in plants
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Vitha S., McAndrew R.S., Osteryoung K.W. FtsZ ring formation at the chloroplast division site in plants. J Cell Biol. 153:2001;111-119.
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J Cell Biol
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Vitha, S.1
McAndrew, R.S.2
Osteryoung, K.W.3
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59
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0036943464
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Overexpression of the Arabidopsis thaliana MinE1 bacterial division inhibitor homologue gene alters chloroplast size and morphology in transgenic Arabidopsis and tobacco plants
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Confocal and electron-microscopy of plants overexpressing MinE1 revealed chloroplasts with abnormal shapes and sizes. This indicates that this protein probably has a similar role to bacterial MinE.
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Reddy M.S.S., Dinkins R., Collins G.B. Overexpression of the Arabidopsis thaliana MinE1 bacterial division inhibitor homologue gene alters chloroplast size and morphology in transgenic Arabidopsis and tobacco plants. Planta. 215:2002;167-176 Confocal and electron-microscopy of plants overexpressing MinE1 revealed chloroplasts with abnormal shapes and sizes. This indicates that this protein probably has a similar role to bacterial MinE.
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(2002)
Planta
, vol.215
, pp. 167-176
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Reddy, M.S.S.1
Dinkins, R.2
Collins, G.B.3
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60
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0037389632
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ARC5, a cytosolic dynamin-like protein from plants, is part of the chloroplast division machinery
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•]) show that a requirement for a dynamin-related protein, with no obvious counterparts in prokaryotes, is common to both types of endosymbiotic organelle. ARC5 is related to a group of dynamin-like proteins that are unique to plants. A GFP-ARC5 fusion protein localizes to a ring at the chloroplast division site and ARC5 mutations cause enlarged, dumbbell-shaped chloroplasts. Import and protease protection assays indicate that the ARC5 ring is positioned on the outer surface of the chloroplast.
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•]) show that a requirement for a dynamin-related protein, with no obvious counterparts in prokaryotes, is common to both types of endosymbiotic organelle. ARC5 is related to a group of dynamin-like proteins that are unique to plants. A GFP-ARC5 fusion protein localizes to a ring at the chloroplast division site and ARC5 mutations cause enlarged, dumbbell-shaped chloroplasts. Import and protease protection assays indicate that the ARC5 ring is positioned on the outer surface of the chloroplast.
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(2003)
Proc Natl Acad Sci U S a
, vol.100
, pp. 4328-4333
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Gao, H.1
Kadirjan-Kalbach, D.2
Froehlich, J.E.3
Osteryoung, K.W.4
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61
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0037339928
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A plant-specific dynamin-related protein forms a ring at the chloroplast division site
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Analysis of synchronized chloroplasts showed the time at which a dynamin-like protein is recruited to chloroplasts, forming a ring on the cytosolic side of the division site in the late stage of division. The ring constricts until division is complete and then disappears.
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Miyagishima S.Y., Nishida K., Mori T., Matsuzaki M., Higashiyama T., Kuroiwa H., Kuroiwa T. A plant-specific dynamin-related protein forms a ring at the chloroplast division site. Plant Cell. 15:2003;655-665 Analysis of synchronized chloroplasts showed the time at which a dynamin-like protein is recruited to chloroplasts, forming a ring on the cytosolic side of the division site in the late stage of division. The ring constricts until division is complete and then disappears.
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(2003)
Plant Cell
, vol.15
, pp. 655-665
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Miyagishima, S.Y.1
Nishida, K.2
Mori, T.3
Matsuzaki, M.4
Higashiyama, T.5
Kuroiwa, H.6
Kuroiwa, T.7
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62
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0037452622
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Dynamic recruitment of dynamin for final mitochondrial severance in a primitive red alga
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Previously, FtsZ was shown to localize to mitochondria in primitive algae on the inside surface of the division site. Here, it is shown that FtsZ, dynamin and the MD ring, an electron-dense structure on the cytoplasmic side of the mitochondrial membrane, act during different phases of division. Before final separation, dynamin patches are recruited externally, to the midpoint of the constricted MD ring.
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Nishida K., Takahara M., Miyagishima S., Kuroiwa H., Matsuzaki M., Kuroiwa T. Dynamic recruitment of dynamin for final mitochondrial severance in a primitive red alga. Proc Natl Acad Sci USA. 100:2003;2146-2151 Previously, FtsZ was shown to localize to mitochondria in primitive algae on the inside surface of the division site. Here, it is shown that FtsZ, dynamin and the MD ring, an electron-dense structure on the cytoplasmic side of the mitochondrial membrane, act during different phases of division. Before final separation, dynamin patches are recruited externally, to the midpoint of the constricted MD ring.
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(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 2146-2151
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Nishida, K.1
Takahara, M.2
Miyagishima, S.3
Kuroiwa, H.4
Matsuzaki, M.5
Kuroiwa, T.6
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64
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0036938981
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Chloroplast division machinery as revealed by immunofluorescence and electron microscopy
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The behaviour of FtsZ and PD rings, both components of the chloroplast division machinery, was followed during the course of division. FtsZ forms a ring on the stromal division site before invagination starts. Then the inner (stromal) and outer (cytosolic) PD rings appear. The FtsZ ring remains at the leading edge of the constriction but does not change width although the volume of the outer PD ring gradually increases. The FtsZ ring disappears before the final stage of chloroplast constriction.
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Kuroiwa H., Mori T., Takahara M., Miyagishima S., Kuroiwa T. Chloroplast division machinery as revealed by immunofluorescence and electron microscopy. Planta. 215:2002;185-190 The behaviour of FtsZ and PD rings, both components of the chloroplast division machinery, was followed during the course of division. FtsZ forms a ring on the stromal division site before invagination starts. Then the inner (stromal) and outer (cytosolic) PD rings appear. The FtsZ ring remains at the leading edge of the constriction but does not change width although the volume of the outer PD ring gradually increases. The FtsZ ring disappears before the final stage of chloroplast constriction.
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(2002)
Planta
, vol.215
, pp. 185-190
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Kuroiwa, H.1
Mori, T.2
Takahara, M.3
Miyagishima, S.4
Kuroiwa, T.5
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65
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0031966243
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The division apparatus of plastids and mitochondria
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Kuroiwa T., Kuroiwa H., Sakai A., Takahashi H., Toda K., Itoh R. The division apparatus of plastids and mitochondria. Int Rev Cytol. 181:1998;1-41.
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Int Rev Cytol
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Kuroiwa, T.1
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Sakai, A.3
Takahashi, H.4
Toda, K.5
Itoh, R.6
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66
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Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
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Kruse T., Møller-Jensen J., Løbner-Olesen A., Gerdes K. Dysfunctional MreB inhibits chromosome segregation in Escherichia coli. EMBO J. 22:2003;5283-5292.
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EMBO J
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Kruse, T.1
Møller-Jensen, J.2
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Gerdes, K.4
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67
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0037396401
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Actin's prokaryotic homologs
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Egelman E.H. Actin's prokaryotic homologs. Curr Opin Struct Biol. 13:2003;244-248.
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Curr Opin Struct Biol
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Egelman, E.H.1
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