Negative-stain electron microscopy of inside-out FtsZ rings reconstituted on artificial membrane tubules show ribbons of protofilaments.
about
In the beginning, Escherichia coli assembled the proto-ring: an initial phase of divisionThe bacterial divisome: ready for its close-upThe bacterial cytoskeleton: more than twisted filaments.In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopyHigh throughput 3D super-resolution microscopy reveals Caulobacter crescentus in vivo Z-ring organization.MinCDE exploits the dynamic nature of FtsZ filaments for its spatial regulationMultifunctional roles for the protein translocation machinery in RNA anchoring to the endoplasmic reticulum.Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division.Remodeling of the Z-Ring Nanostructure during the Streptococcus pneumoniae Cell Cycle Revealed by Photoactivated Localization MicroscopyDistinct functions of chloroplast FtsZ1 and FtsZ2 in Z-ring structure and remodeling.Structural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC.Defining the rate-limiting processes of bacterial cytokinesisRapid in vitro assembly of Caulobacter crescentus FtsZ protein at pH 6.5 and 7.2.Giant vesicles: a powerful tool to reconstruct bacterial division assemblies in cell-like compartments.Bacterial Nucleoid Occlusion: Multiple Mechanisms for Preventing Chromosome Bisection During Cell Division.FtsZ-ring Architecture and Its Control by MinCD.Probing for Binding Regions of the FtsZ Protein Surface through Site-Directed Insertions: Discovery of Fully Functional FtsZ-Fluorescent ProteinsReconstitution of Protein Dynamics Involved in Bacterial Cell Division.Functional Analysis of the Chloroplast Division Complex Using Schizosaccharomyces pombe as a Heterologous Expression System.Influence of FtsZ GTPase activity and concentration on nanoscale Z-ring structure in vivo revealed by three-dimensional Superresolution imaging.The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide.ZipA and FtsA* stabilize FtsZ-GDP miniring structures.Understanding nucleotide-regulated FtsZ filament dynamics and the monomer assembly switch with large-scale atomistic simulations.The Chloroplast Tubulin Homologs FtsZA and FtsZB from the Red Alga Galdieria sulphuraria Co-assemble into Dynamic Filaments.Three-Dimensional Superresolution Imaging of the FtsZ Ring during Cell Division of the Cyanobacterium Prochlorococcus.FtsZ Constriction Force - Curved Protofilaments Bending Membranes.Self-Organization of FtsZ Polymers in Solution Reveals Spacer Role of the Disordered C-Terminal Tail.Asynchronous division by non-ring FtsZ in the gammaproteobacterial symbiont of Robbea hypermnestra.Lateral interactions between protofilaments of the bacterial tubulin homolog FtsZ are essential for cell division
P2860
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P2860
Negative-stain electron microscopy of inside-out FtsZ rings reconstituted on artificial membrane tubules show ribbons of protofilaments.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Negative-stain electron micros ...... how ribbons of protofilaments.
@ast
Negative-stain electron micros ...... how ribbons of protofilaments.
@en
type
label
Negative-stain electron micros ...... how ribbons of protofilaments.
@ast
Negative-stain electron micros ...... how ribbons of protofilaments.
@en
prefLabel
Negative-stain electron micros ...... how ribbons of protofilaments.
@ast
Negative-stain electron micros ...... how ribbons of protofilaments.
@en
P2093
P2860
P1433
P1476
Negative-stain electron micros ...... how ribbons of protofilaments.
@en
P2093
Harold P Erickson
Masaki Osawa
Sara L Milam
P2860
P356
10.1016/J.BPJ.2012.05.035
P407
P577
2012-07-01T00:00:00Z