Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
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3D-SIM super resolution microscopy reveals a bead-like arrangement for FtsZ and the division machinery: implications for triggering cytokinesisReconstitution of contractile FtsZ rings in liposomesSite-specific mutations of FtsZ--effects on GTPase and in vitro assemblyBacterial Filament Systems: Toward Understanding Their Emergent Behavior and Cellular FunctionsThe Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase ActivityMolecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in checkFtsZ Protofilaments Use a Hinge-Opening Mechanism for Constrictive Force GenerationBacterial actin and tubulin homologs in cell growth and divisionKinetic modeling of the assembly, dynamic steady state, and contraction of the FtsZ ring in prokaryotic cytokinesisGenetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilisGTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknALarge-scale functional purification of recombinant HIV-1 capsidWhy are bacteria different from eukaryotes?Insight into the assembly properties and functional organisation of the magnetotactic bacterial actin-like homolog, MamKTrapping of a spiral-like intermediate of the bacterial cytokinetic protein FtsZ.FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.Nucleotide-dependent conformations of FtsZ dimers and force generation observed through molecular dynamics simulations.In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopySeptin assemblies form by diffusion-driven annealing on membranesHigh throughput 3D super-resolution microscopy reveals Caulobacter crescentus in vivo Z-ring organization.MinCDE exploits the dynamic nature of FtsZ filaments for its spatial regulationBtubA-BtubB heterodimer is an essential intermediate in protofilament assemblyIn vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM)Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils.Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy sourceThe polymerization mechanism of the bacterial cell division protein FtsZ.Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stabilityAssembly of an FtsZ mutant deficient in GTPase activity has implications for FtsZ assembly and the role of the Z ring in cell divisionRapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching.Drug discovery targeting cell division proteins, microtubules and FtsZ.A rapid fluorescence assay for FtsZ assembly indicates cooperative assembly with a dimer nucleus.GTPase activity, structure, and mechanical properties of filaments assembled from bacterial cytoskeleton protein MreB.FtsZ and the division of prokaryotic cells and organelles.Z ring as executor of bacterial cell division.A model of membrane contraction predicting initiation and completion of bacterial cell division.Subcellular protein localization by using a genetically encoded fluorescent amino acid.The Cell Division Protein FtsZ from Streptococcus pneumoniae Exhibits a GTPase Activity Delay.Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins.Studies on the dissociation and urea-induced unfolding of FtsZ support the dimer nucleus polymerization mechanism.Characterization of the FtsZ C-Terminal Variable (CTV) Region in Z-Ring Assembly and Interaction with the Z-Ring Stabilizer ZapD in E. coli Cytokinesis
P2860
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P2860
Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
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
Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
@ast
Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
@en
type
label
Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
@ast
Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
@en
prefLabel
Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
@ast
Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
@en
P2093
P2860
P356
P1476
Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?
@en
P2093
P2860
P304
11743-11753
P356
10.1074/JBC.M009033200
P407
P577
2001-01-04T00:00:00Z