The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site
about
The Min system and other nucleoid-independent regulators of Z ring positioningDynamic 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.Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division siteCrystal structure of Helicobacter pylori MinE, a cell division topological specificity factorThe evolution of the cytoskeletonDivision site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell polesRapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coliThe MinCDJ system in Bacillus subtilis prevents minicell formation by promoting divisome disassemblyStructural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus.Crystal structure of the bacterial cell division inhibitor MinC.Structure of the pilus assembly protein TadZ from Eubacterium rectale: implications for polar localizationBms1p, a novel GTP-binding protein, and the related Tsr1p are required for distinct steps of 40S ribosome biogenesis in yeast.Cell age dependent concentration of Escherichia coli divisome proteins analyzed with ImageJ and ObjectJMapping out Min protein patterns in fully confined fluidic chambersA multistranded polymer model explains MinDE dynamics in E. coli cell division.Spiral architecture of the nucleoid in Bdellovibrio bacteriovorus.Asymmetric constriction of dividing Escherichia coli cells induced by expression of a fusion between two min proteins.GTPase activity and biochemical characterization of a recombinant cotton fiber annexin.Cytokinesis in bacteriaGNA33 of Neisseria meningitidis is a lipoprotein required for cell separation, membrane architecture, and virulence.A plant MinD homologue rescues Escherichia coli HL1 mutant (DeltaMinDE) in the absence of MinESubcellular Min oscillations as a single-cell reporter of the action of polycations, protamine, and gentamicin on Escherichia coliThe HP0256 gene product is involved in motility and cell envelope architecture of Helicobacter pyloriGonococcal MinD affects cell division in Neisseria gonorrhoeae and Escherichia coli and exhibits a novel self-interaction.MinDE-dependent pole-to-pole oscillation of division inhibitor MinC in Escherichia coliBacterial cell division: a moveable feast.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.Genetic and structural analysis of the Bacteroides conjugative transposon CTn341.Escherichia coli mrsC is an allele of hflB, encoding a membrane-associated ATPase and protease that is required for mRNA decay.Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation.Pattern formation in Escherichia coli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site.Self-assembly of MinE on the membrane underlies formation of the MinE ring to sustain function of the Escherichia coli Min system.Identification and characterization of an active plasmid partition mechanism for the novel Lactococcus lactis plasmid pCI2000Membrane redistribution of the Escherichia coli MinD protein induced by MinE.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 coliMorphogenesis of Escherichia coliExploring intracellular space: function of the Min system in round-shaped Escherichia coli
P2860
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P2860
The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site
description
1991 nî lūn-bûn
@nan
1991 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
The MinD protein is a membrane ...... Escherichia coli division site
@ast
The MinD protein is a membrane ...... Escherichia coli division site
@en
The MinD protein is a membrane ...... Escherichia coli division site
@nl
type
label
The MinD protein is a membrane ...... Escherichia coli division site
@ast
The MinD protein is a membrane ...... Escherichia coli division site
@en
The MinD protein is a membrane ...... Escherichia coli division site
@nl
prefLabel
The MinD protein is a membrane ...... Escherichia coli division site
@ast
The MinD protein is a membrane ...... Escherichia coli division site
@en
The MinD protein is a membrane ...... Escherichia coli division site
@nl
P2093
P2860
P1433
P1476
The MinD protein is a membrane ...... Escherichia coli division site
@en
P2093
L I Rothfield
P A de Boer
R E Crossley
P2860
P304
P407
P577
1991-12-01T00:00:00Z