ATP-dependent interactions between Escherichia coli Min proteins and the phospholipid membrane in vitro.
about
The Min system and other nucleoid-independent regulators of Z ring positioningMembrane binding of MinE allows for a comprehensive description of Min-protein pattern formationThe bacterial cytoskeletonDivision site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell polesThe ParA/MinD family puts things in their placeMolecular Interactions of the Min Protein System Reproduce Spatiotemporal Patterning in Growing and Dividing Escherichia coli CellsSymmetry and scale orient Min protein patterns in shaped bacterial sculptures.FtsZ placement in nucleoid-free bacteriaAn Optimal Free Energy Dissipation Strategy of the MinCDE Oscillator in Regulating Symmetric Bacterial Cell DivisionNoise-induced Min phenotypes in E. coli.Determination 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 CytokinesisLocalized Dimerization and Nucleoid Binding Drive Gradient Formation by the Bacterial Cell Division Inhibitor MipZCrystal structure of the N-terminal domain of MinC dimerized via domain swappingGenetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilisMapping out Min protein patterns in fully confined fluidic chambersA multistranded polymer model explains MinDE dynamics in E. coli cell division.Critical waves and the length problem of biology.Multiple modes of interconverting dynamic pattern formation by bacterial cell division proteins.Membrane potential is important for bacterial cell divisionChromosome segregation by the Escherichia coli Min system.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.Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches.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.ZipA is required for targeting of DMinC/DicB, but not DMinC/MinD, complexes to septal ring assemblies in Escherichia coliDivided we stand: splitting synthetic cells for their proliferationMin protein patterns emerge from rapid rebinding and membrane interaction of MinE.Mapping the MinE site involved in interaction with the MinD division site selection protein of Escherichia coli.SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over Chromosomes in E. coli.Role of MinD-membrane association in Min protein interactionsZ ring as executor of bacterial cell division.Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymersMembrane binding by MinD involves insertion of hydrophobic residues within the C-terminal amphipathic helix into the bilayer.MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly.Polar flagellar biosynthesis and a regulator of flagellar number influence spatial parameters of cell division in Campylobacter jejuniMechanism of the asymmetric activation of the MinD ATPase by MinE.Towards understanding the molecular basis of bacterial DNA segregation.The switch I and II regions of MinD are required for binding and activating MinC.
P2860
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P2860
ATP-dependent interactions between Escherichia coli Min proteins and the phospholipid membrane in vitro.
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年学术文章
@zh-my
2003年学术文章
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name
ATP-dependent interactions bet ...... hospholipid membrane in vitro.
@en
ATP-dependent interactions bet ...... hospholipid membrane in vitro.
@nl
type
label
ATP-dependent interactions bet ...... hospholipid membrane in vitro.
@en
ATP-dependent interactions bet ...... hospholipid membrane in vitro.
@nl
prefLabel
ATP-dependent interactions bet ...... hospholipid membrane in vitro.
@en
ATP-dependent interactions bet ...... hospholipid membrane in vitro.
@nl
P2093
P2860
P1476
ATP-dependent interactions bet ...... hospholipid membrane in vitro.
@en
P2093
David M Raskin
Laura L Lackner
Piet A J de Boer
P2860
P304
P356
10.1128/JB.185.3.735-749.2003
P407
P577
2003-02-01T00:00:00Z