Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils. - Wikidata - awgldk - TriplyDB

Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils.

Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils.

http://www.wikidata.org/entity/Q33837672

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Functional taxonomy of bacterial hyperstructures The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase Activity Kinetic modeling of the assembly, dynamic steady state, and contraction of the FtsZ ring in prokaryotic cytokinesis Macromolecular interactions of the bacterial division FtsZ protein: from quantitative biochemistry and crowding to reconstructing minimal divisomes in the test tube The structure of FtsZ filaments in vivo suggests a force-generating role in cell division Simple modeling of FtsZ polymers on flat and curved surfaces: correlation with experimental in vitro observations.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.An equilibrium model for the Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue.In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM)Novel recombinant engineered gp41 N-terminal heptad repeat trimers and their potential as anti-HIV-1 therapeutics or microbicides An equilibrium model for linear and closed-loop amyloid fibril formation.FtsZ and the division of prokaryotic cells and organelles.Z ring as executor of bacterial cell division.The Cell Division Protein FtsZ from Streptococcus pneumoniae Exhibits a GTPase Activity Delay.Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits.Conformational Stability of the NH2-Terminal Propeptide of the Precursor of Pulmonary Surfactant Protein SP-B.Characterization of Caulobacter crescentus FtsZ protein using dynamic light scattering Mg(2+)-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue involves the concerted formation of a narrow size distribution of oligomeric species Septum enlightenment: assembly of bacterial division proteins.Energetics and geometry of FtsZ polymers: nucleated self-assembly of single protofilaments.The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast Allosteric models for cooperative polymerization of linear polymers.Modeling the physics of FtsZ assembly and force generation.The eukaryotic cell originated in the integration and redistribution of hyperstructures from communities of prokaryotic cells based on molecular complementarity.Comparing contractile apparatus-driven cytokinesis mechanisms across kingdoms.Redefining the roles of the FtsZ-ring in bacterial cytokinesis.FtsZ bacterial cytoskeletal polymers on curved surfaces: the importance of lateral interactions MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunits The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro.Control by potassium of the size distribution of Escherichia coli FtsZ polymers is independent of GTPase activity.Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads.Reconstitution and organization of Escherichia coli proto-ring elements (FtsZ and FtsA) inside giant unilamellar vesicles obtained from bacterial inner membranes.In vitro reconstitution of the initial stages of the bacterial cell division machinery.Torsion and curvature of FtsZ filaments.Visualization of single Escherichia coli FtsZ filament dynamics with atomic force microscopy.FtsZ Constriction Force - Curved Protofilaments Bending Membranes.Self-Organization of FtsZ Polymers in Solution Reveals Spacer Role of the Disordered C-Terminal Tail.Role of filament annealing in the kinetics and thermodynamics of nucleated polymerization.Molecular dynamics simulation of GTPase activity in polymers of the cell division protein FtsZ.

P2860

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P2860

Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils.

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2005年の論文

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Cooperative behavior of Escher ...... long single-stranded fibrils.

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Cooperative behavior of Escher ...... long single-stranded fibrils.

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Cooperative behavior of Escher ...... long single-stranded fibrils.

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Cooperative behavior of Escher ...... long single-stranded fibrils.

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Cooperative behavior of Escher ...... long single-stranded fibrils.

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Cooperative behavior of Escher ...... long single-stranded fibrils.

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Proceedings of the National Academy of Sciences of the United States of America

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Cooperative behavior of Escher ...... long single-stranded fibrils.

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Allen P Minton

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Carlos Alfonso

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Germán Rivas

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José Manuel González

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Marisela Vélez

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Mercedes Jiménez

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Miguel Vicente

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Peter Schuck

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P2860

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

Ca2+-mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro

Slow polymerization of Mycobacterium tuberculosis FtsZ

On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation

Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?

Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers

The polymerization mechanism of the bacterial cell division protein FtsZ.

Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stability

Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations.

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1895-1900

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10.1073/PNAS.0409517102

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6

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102

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Jesus Mingorance

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8048421

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Escherichia coli

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548572

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