The MinE ring required for proper placement of the division site is a mobile structure that changes its cellular location during the Escherichia coli division cycle.
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Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinERecruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE.Cytokinesis in prokaryotes and eukaryotes: common principles and different solutionsCrystal structure of Helicobacter pylori MinE, a cell division topological specificity factorDynamic structures in Escherichia coli: spontaneous formation of MinE rings and MinD polar zonesDivision site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell polesMolecular Interactions of the Min Protein System Reproduce Spatiotemporal Patterning in Growing and Dividing Escherichia coli CellsMembrane-bound MinDE complex acts as a toggle switch that drives Min oscillation coupled to cytoplasmic depletion of MinD.The MinCDJ system in Bacillus subtilis prevents minicell formation by promoting divisome disassemblyNoise-induced Min phenotypes in E. coli.Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinEDetermination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinCThe Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate CytokinesisCrystal structure of the N-terminal domain of MinC dimerized via domain swappingThe bacterial divisome: ready for its close-upThe N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvatureA multistranded polymer model explains MinDE dynamics in E. coli cell division.Regulation of symmetric bacterial cell division by MinE: What is the role of conformational dynamics?Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins.Asymmetric constriction of dividing Escherichia coli cells induced by expression of a fusion between two min proteins.Cytokinesis in bacteriaA plant MinD homologue rescues Escherichia coli HL1 mutant (DeltaMinDE) in the absence of MinECDP1, a novel component of chloroplast division site positioning system in Arabidopsis.Subcellular Min oscillations as a single-cell reporter of the action of polycations, protamine, and gentamicin on Escherichia coliGonococcal MinD affects cell division in Neisseria gonorrhoeae and Escherichia coli and exhibits a novel self-interaction.Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli.Analysis of MinD mutations reveals residues required for MinE stimulation of the MinD ATPase and residues required for MinC interaction.MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.A polymerization-depolymerization model that accurately generates the self-sustained oscillatory system involved in bacterial division site placementDiversity and versatility of lipid-protein interactions revealed by molecular genetic approaches.Pattern formation in Escherichia coli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site.The double par locus of virulence factor pB171: DNA segregation is correlated with oscillation of ParA.Differential affinities of MinD and MinE to anionic phospholipid influence Min patterning dynamics in vitroSelf-assembly of MinE on the membrane underlies formation of the MinE ring to sustain function of the Escherichia coli Min system.The dimerization function of MinC resides in a structurally autonomous C-terminal domainZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coliExploring intracellular space: function of the Min system in round-shaped Escherichia coliDivision site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains.Mapping the MinE site involved in interaction with the MinD division site selection protein of Escherichia coli.Division accuracy in a stochastic model of Min oscillations in Escherichia coli.
P2860
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P2860
The MinE ring required for proper placement of the division site is a mobile structure that changes its cellular location during the Escherichia coli division cycle.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The MinE ring required for pro ...... cherichia coli division cycle.
@ast
The MinE ring required for pro ...... cherichia coli division cycle.
@en
The MinE ring required for pro ...... cherichia coli division cycle.
@nl
type
label
The MinE ring required for pro ...... cherichia coli division cycle.
@ast
The MinE ring required for pro ...... cherichia coli division cycle.
@en
The MinE ring required for pro ...... cherichia coli division cycle.
@nl
prefLabel
The MinE ring required for pro ...... cherichia coli division cycle.
@ast
The MinE ring required for pro ...... cherichia coli division cycle.
@en
The MinE ring required for pro ...... cherichia coli division cycle.
@nl
P2093
P2860
P356
P1476
The MinE ring required for pro ...... cherichia coli division cycle.
@en
P2093
P2860
P304
P356
10.1073/PNAS.031549298
P407
P577
2001-01-23T00:00:00Z