Dynamic assembly of FtsZ regulated by GTP hydrolysis. - Test2 - elhamkhani - TriplyDB

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

http://www.wikidata.org/entity/Q24533005

about

Septal localization of FtsQ, an essential cell division protein in Escherichia coli Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus The bacterial cytoskeleton Site-specific mutations of FtsZ--effects on GTPase and in vitro assembly Molecular mechanisms for the evolution of bacterial morphologies and growth modes The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography Crystal structure of the cell division protein FtsA from Thermotoga maritima Filament Formation of the FtsZ/Tubulin-like Protein TubZ from the Bacillus cereus pXO1 Plasmid Crystal Structure and Site-directed Mutational Analysis Reveals Key Residues Involved in Escherichia coli ZapA Function The bacterial divisome: ready for its close-up Tubulin and FtsZ structures: functional and therapeutic implications Slow polymerization of Mycobacterium tuberculosis FtsZ Kinetic modeling of the assembly, dynamic steady state, and contraction of the FtsZ ring in prokaryotic cytokinesis Identification of the SlmA active site responsible for blocking bacterial cytokinetic ring assembly over the chromosome GTPase activity of mycobacterial FtsZ is impaired due to its transphosphorylation by the eukaryotic-type Ser/Thr kinase, PknA Large ring polymers align FtsZ polymers for normal septum formation Cytological and biochemical characterization of the FtsA cell division protein of Bacillus subtilis A moonlighting enzyme links Escherichia coli cell size with central metabolism Structure prediction of magnetosome-associated proteins.Investigating intracellular dynamics of FtsZ cytoskeleton with photoactivation single-molecule tracking FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.Crystallization and preliminary X-ray data analysis of the pXO1 plasmid-partitioning factor TubZ from Bacillus cereus.Polymerization of Ftsz, a bacterial homolog of tubulin. is assembly cooperative?Temperature-regulated formation of mycelial mat-like biofilms by Legionella pneumophila.Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils.The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization.Polymerization of bacteriophage phi 29 replication protein p1 into protofilament sheets.Tubulin-like protofilaments in Ca2+-induced FtsZ sheets.ZipA is a MAP-Tau homolog and is essential for structural integrity of the cytokinetic FtsZ ring during bacterial cell division.Pattern formation in Escherichia coli: a model for the pole-to-pole oscillations of Min proteins and the localization of the division site.The pH dependence of polymerization and bundling by the essential bacterial cytoskeletal protein FtsZ The polymerization mechanism of the bacterial cell division protein FtsZ.GTP-dependent heteropolymer formation and bundling of chloroplast FtsZ1 and FtsZ2.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.The lethal effect of a benzamide derivative, 3-methoxybenzamide, can be suppressed by mutations within a cell division gene, ftsZ, in Bacillus subtilis.Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ Deletion of the min operon results in increased thermosensitivity of an ftsZ84 mutant and abnormal FtsZ ring assembly, placement, and disassembly.Assembly of an FtsZ mutant deficient in GTPase activity has implications for FtsZ assembly and the role of the Z ring in cell division

P2860

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P2860

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

http://www.wikidata.org/entity/Q24533005

description

1998 nî lūn-bûn

@nan

1998 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի հունվարին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

Dynamic assembly of FtsZ regulated by GTP hydrolysis

@nl

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

@ast

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

@en

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

@en-gb

type

label

Dynamic assembly of FtsZ regulated by GTP hydrolysis

@nl

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

@ast

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

@en

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

@en-gb

prefLabel

Dynamic assembly of FtsZ regulated by GTP hydrolysis

@nl

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

@ast

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

@en

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

@en-gb

P1433

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P2860

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Q24533005-7E7C2D12-BE4F-4BFF-A1AC-4FBBFA75A8A9

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P932

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P356

P1433

The EMBO Journal

P1476

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

@en

P2093

A Mukherjee

http://www.w3.org/2001/XMLSchema#string

J Lutkenhaus

http://www.w3.org/2001/XMLSchema#string

P2860

FtsZ ring structure associated with division in Escherichia coli

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

Polycation-induced assembly of purified tubulin

GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules

FtsA is localized to the septum in an FtsZ-dependent manner.

Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated.

Microtubule dynamic instability and GTP hydrolysis.

Inactivation of FtsI inhibits constriction of the FtsZ cytokinetic ring and delays the assembly of FtsZ rings at potential division sites.

Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein.

Mutations in ftsZ that confer resistance to SulA affect the interaction of FtsZ with GTP.

P304

462-469

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1093/EMBOJ/17.2.462

http://www.w3.org/2001/XMLSchema#string

P407

P433

2

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P478

17

http://www.w3.org/2001/XMLSchema#string

P577

1998-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

13799068

http://www.w3.org/2001/XMLSchema#string

P698

9430638

http://www.w3.org/2001/XMLSchema#string

P932

1170397

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