Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check - Wikidata - wikimedia - TriplyDB

Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check

Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check

http://www.wikidata.org/entity/Q27666090

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Chromosomal macrodomains and associated proteins: implications for DNA organization and replication in gram negative bacteria Chromosome architecture is a key element of bacterial cellular organization The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase Activity Evidence for divisome localization mechanisms independent of the Min system and SlmA in Escherichia coli SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid Structural and functional basis of transcriptional regulation by TetR family protein CprB from S. coelicolor A3(2)In the beginning, Escherichia coli assembled the proto-ring: an initial phase of division Structure of AmtR, the global nitrogen regulator of Corynebacterium glutamicum, in free and DNA-bound forms Identification of the SlmA active site responsible for blocking bacterial cytokinetic ring assembly over the chromosome A moonlighting enzyme links Escherichia coli cell size with central metabolism Identification of Preferred DNA-Binding Sites for the Thermus thermophilus Transcriptional Regulator SbtR by the Combinatorial Approach REPSA Macromolecular interactions of the bacterial division FtsZ protein: from quantitative biochemistry and crowding to reconstructing minimal divisomes in the test tube Proteolysis-Dependent Remodeling of the Tubulin Homolog FtsZ at the Division Septum in Escherichia coli.In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy Late assembly of the Vibrio cholerae cell division machinery postpones septation to the last 10% of the cell cycle.Divided we stand: splitting synthetic cells for their proliferation The Min system and nucleoid occlusion are not required for identifying the division site in Bacillus subtilis but ensure its efficient utilization.Bacillus subtilis SepF binds to the C-terminus of FtsZ.Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist.LocZ is a new cell division protein involved in proper septum placement in Streptococcus pneumoniae.The interplay of ClpXP with the cell division machinery in Escherichia coli.The Kil peptide of bacteriophage λ blocks Escherichia coli cytokinesis via ZipA-dependent inhibition of FtsZ assembly Location of dual sites in E. coli FtsZ important for degradation by ClpXP; one at the C-terminus and one in the disordered linker.Oligomerization of FtsZ converts the FtsZ tail motif (conserved carboxy-terminal peptide) into a multivalent ligand with high avidity for partners ZipA and SlmA.SlmA antagonism of FtsZ assembly employs a two-pronged mechanism like MinCD.FtsZ filament capping by MciZ, a developmental regulator of bacterial division.A model for Escherichia coli chromosome packaging supports transcription factor-induced DNA domain formation Escherichia coli low-molecular-weight penicillin-binding proteins help orient septal FtsZ, and their absence leads to asymmetric cell division and branching.Robustness and accuracy of cell division in Escherichia coli in diverse cell shapes Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits.RefZ facilitates the switch from medial to polar division during spore formation in Bacillus subtilis.Global analysis of transcriptional regulators in Staphylococcus aureus.Genome conformation capture reveals that the Escherichia coli chromosome is organized by replication and transcription.Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ.A replication-inhibited unsegregated nucleoid at mid-cell blocks Z-ring formation and cell division independently of SOS and the SlmA nucleoid occlusion protein in Escherichia coli.Bacterial cytokinesis: From Z ring to divisome.Comparing contractile apparatus-driven cytokinesis mechanisms across kingdoms.The physiology of bacterial cell division.How to get (a)round: mechanisms controlling growth and division of coccoid bacteria.The TetR family of regulators.

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Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check

http://www.wikidata.org/entity/Q27666090

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2011 nî lūn-bûn

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2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունվարին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

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2011年论文

@wuu

name

Molecular mechanism by which t ...... mA, keeps cytokinesis in check

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Molecular mechanism by which t ...... mA, keeps cytokinesis in check

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Molecular mechanism by which t ...... mA, keeps cytokinesis in check

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type

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Molecular mechanism by which t ...... mA, keeps cytokinesis in check

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Molecular mechanism by which t ...... mA, keeps cytokinesis in check

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Molecular mechanism by which t ...... mA, keeps cytokinesis in check

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Molecular mechanism by which t ...... mA, keeps cytokinesis in check

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Molecular mechanism by which t ...... mA, keeps cytokinesis in check

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Molecular mechanism by which t ...... mA, keeps cytokinesis in check

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The EMBO Journal

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Molecular mechanism by which t ...... mA, keeps cytokinesis in check

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P2093

Brian F Pickering

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

Maria A Schumacher

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

Nam Ky Tonthat

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

Shoudan Liang

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

Tushar K Beuria

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

William Margolin

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

P2860

Model-based analysis of ChIP-Seq (MACS)

Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE

Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing

Determination of domain structure of proteins from X-ray solution scattering

Global rigid body modeling of macromolecular complexes against small-angle scattering data

Reconstitution of contractile FtsZ rings in liposomes

Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles

The human genome browser at UCSC

MEME: discovering and analyzing DNA and protein sequence motifs

Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli

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154-64

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scholarly article

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4516353

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10.1038/EMBOJ.2010.288

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1

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30

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Michael W Van Dyke

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2011-01-05T00:00:00Z

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49640959

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21113127

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3020112

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