SepF, a novel FtsZ-interacting protein required for a late step in cell division
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3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesisBeyond the cytoskeleton: mesoscale assemblies and their function in spatial organizationThe MinCDJ system in Bacillus subtilis prevents minicell formation by promoting divisome disassemblyNovel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell divisionStructural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ringBacterial actin and tubulin homologs in cell growth and divisionCharacterization of CrgA, a new partner of the Mycobacterium tuberculosis peptidoglycan polymerization complexesCharacterisation of ATP-dependent Mur ligases involved in the biogenesis of cell wall peptidoglycan in Mycobacterium tuberculosisA new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilisControl of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilisAn expanded protein-protein interaction network in Bacillus subtilis reveals a group of hubs: Exploration by an integrative approachLarge ring polymers align FtsZ polymers for normal septum formationPositive control of cell division: FtsZ is recruited by SsgB during sporulation of StreptomycesRequirement of essential Pbp2x and GpsB for septal ring closure in Streptococcus pneumoniae D39.Regulated intramembrane proteolysis of FtsL protein and the control of cell division in Bacillus subtilis.Two-step assembly dynamics of the Bacillus subtilis divisome.The YlmG protein has a conserved function related to the distribution of nucleoids in chloroplasts and cyanobacteria.Evolution of diverse cell division and vesicle formation systems in ArchaeaEzrA contributes to the regulation of cell size in Staphylococcus aureus.FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins.Identification of Escherichia coli ZapC (YcbW) as a component of the division apparatus that binds and bundles FtsZ polymersFunctional domain analysis of the cell division inhibitor EzrA.Structure and function of a spectrin-like regulator of bacterial cytokinesis.Tetracycline hypersensitivity of an ezrA mutant links GalE and TseB (YpmB) to cell divisionStructural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC.Towards the development of Bacillus subtilis as a cell factory for membrane proteins and protein complexes.AhrC and Eep are biofilm infection-associated virulence factors in Enterococcus faecalis.The conserved DNA-binding protein WhiA is involved in cell division in Bacillus subtilis.Effects of rhodomyrtone on Gram-positive bacterial tubulin homologue FtsZ.Cytoskeletal proteins of actinobacteria.Cell division and DNA segregation in Streptomyces: how to build a septum in the middle of nowhere?The structure, function, and regulation of Mycobacterium FtsZ.The physiology of bacterial cell division.Multidimensional view of the bacterial cytoskeleton.FtsZ ring stability: of bundles, tubules, crosslinks, and curves.From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division?Cell division in CorynebacterineaeThe keepers of the ring: regulators of FtsZ assembly.PipY, a Member of the Conserved COG0325 Family of PLP-Binding Proteins, Expands the Cyanobacterial Nitrogen Regulatory Network.Cell wall-deficient, L-form bacteria in the 21st century: a personal perspective.
P2860
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P2860
SepF, a novel FtsZ-interacting protein required for a late step in cell division
description
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2006
@ast
im Februar 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2006/02/01)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/02/01)
@nl
наукова стаття, опублікована в лютому 2006
@uk
مقالة علمية (نشرت في فبراير 2006)
@ar
name
SepF, a novel FtsZ-interacting protein required for a late step in cell division
@ast
SepF, a novel FtsZ-interacting protein required for a late step in cell division
@en
SepF, a novel FtsZ-interacting protein required for a late step in cell division
@nl
type
label
SepF, a novel FtsZ-interacting protein required for a late step in cell division
@ast
SepF, a novel FtsZ-interacting protein required for a late step in cell division
@en
SepF, a novel FtsZ-interacting protein required for a late step in cell division
@nl
prefLabel
SepF, a novel FtsZ-interacting protein required for a late step in cell division
@ast
SepF, a novel FtsZ-interacting protein required for a late step in cell division
@en
SepF, a novel FtsZ-interacting protein required for a late step in cell division
@nl
P2093
P2860
P3181
P1476
SepF, a novel FtsZ-interacting protein required for a late step in cell division
@en
P2093
Jean-Christophe Meile
Leendert W. Hamoen
Philippe Noirot
Wouter de Jong
P2860
P304
P3181
P356
10.1111/J.1365-2958.2005.04987.X
P407
P577
2006-02-01T00:00:00Z