Analysis of MinD mutations reveals residues required for MinE stimulation of the MinD ATPase and residues required for MinC interaction.
about
Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factorThe ParA/MinD family puts things in their placeDetermination 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 MinCStructure of the pilus assembly protein TadZ from Eubacterium rectale: implications for polar localizationLocalized Dimerization and Nucleoid Binding Drive Gradient Formation by the Bacterial Cell Division Inhibitor MipZThe Yeast Nbp35-Cfd1 Cytosolic Iron-Sulfur Cluster Scaffold Is an ATPaseA multistranded polymer model explains MinDE dynamics in E. coli cell division.A new multicompartmental reaction-diffusion modeling method links transient membrane attachment of E. coli MinE to E-ring formation.Chromosome segregation by the Escherichia coli Min system.Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli.MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA.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.Geometry-induced protein pattern formation.Molecular Cloning, Expression of minD Gene from Lactobacillus acidophilus VTCC-B-871 and Analyses to Identify Lactobacillus rhamnosus PN04 from Vietnam Hottuynia cordata Thunb.Spatial control of the cell division site by the Min system in Escherichia coli.MinC/MinD copolymers are not required for Min function.Bacterial ApbC protein has two biochemical activities that are required for in vivo function.The MinD homolog FlhG regulates the synthesis of the single polar flagellum of Vibrio alginolyticus.SIMIBI twins in protein targeting and localization.Staphylococcus aureus operates protein-tyrosine phosphorylation through a specific mechanism.MinC and FtsZ mutant analysis provides insight into MinC/MinD-mediated Z Ring disassembly.Robust Min-system oscillation in the presence of internal photosynthetic membranes in cyanobacteria.The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide.
P2860
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P2860
Analysis of MinD mutations reveals residues required for MinE stimulation of the MinD ATPase and residues required for MinC interaction.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Analysis of MinD mutations rev ...... required for MinC interaction.
@ast
Analysis of MinD mutations rev ...... required for MinC interaction.
@en
type
label
Analysis of MinD mutations rev ...... required for MinC interaction.
@ast
Analysis of MinD mutations rev ...... required for MinC interaction.
@en
prefLabel
Analysis of MinD mutations rev ...... required for MinC interaction.
@ast
Analysis of MinD mutations rev ...... required for MinC interaction.
@en
P2093
P2860
P1476
Analysis of MinD mutations rev ...... required for MinC interaction
@en
P2093
Cristian Saez
Huaijin Zhou
Joe Lutkenhaus
Sandra Cox
Zonglin Hu
P2860
P304
P356
10.1128/JB.187.2.629-638.2005
P407
P577
2005-01-01T00:00:00Z