Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli. - Wikidata - awgldk - TriplyDB

Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli.

Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli.

http://www.wikidata.org/entity/Q42190364

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Crystal Structure and Site-directed Mutational Analysis Reveals Key Residues Involved in Escherichia coli ZapA Function The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain In the beginning, Escherichia coli assembled the proto-ring: an initial phase of division The bacterial divisome: ready for its close-up Identification of the SlmA active site responsible for blocking bacterial cytokinetic ring assembly over the chromosome Structure and Mutational Analyses of Escherichia coli ZapD Reveal Charged Residues Involved in FtsZ Filament Bundling In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy The bypass of ZipA by overexpression of FtsN requires a previously unknown conserved FtsN motif essential for FtsA-FtsN interaction supporting a model in which FtsA monomers recruit late cell division proteins to the Z ring Crystallization and preliminary X-ray crystallographic analysis of Z-ring-associated protein (ZapD) from Escherichia coli 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.A multi-layered protein network stabilizes the Escherichia coli FtsZ-ring and modulates constriction dynamics.Common Cell Shape Evolution of Two Nasopharyngeal Pathogens.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 A mutation in Escherichia coli ftsZ bypasses the requirement for the essential division gene zipA and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundling 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 cytokinesis Structural and Biochemical Studies Reveal a Putative FtsZ Recognition Site on the Z-ring Stabilizer ZapD.Splitsville: structural and functional insights into the dynamic bacterial Z ring.Disassembly of the divisome in Escherichia coli: evidence that FtsZ dissociates before compartmentalization.Bacterial cytokinesis: From Z ring to divisome.The physiology of bacterial cell division.FtsZ ring stability: of bundles, tubules, crosslinks, and curves.From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division?Cell division in Corynebacterineae ZapE is a novel cell division protein interacting with FtsZ and modulating the Z-ring dynamics The keepers of the ring: regulators of FtsZ assembly.Functional analysis of the cyclophilin PpiB role in bacterial cell division.ZapA and ZapB form an FtsZ-independent structure at midcell.Identification of agents targeting FtsZ assembly.Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking.Assembly and activation of the Escherichia coli divisome.The Escherichia coli divisome: born to divide.ClpXP and ClpAP control the Escherichia coli division protein ZapC by proteolysis.Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli.Escherichia coli FtsA forms lipid-bound minirings that antagonize lateral interactions between FtsZ protofilaments.Two dynamin-like proteins stabilize FtsZ rings during Streptomyces sporulation.The hypermorph FtsA* protein has an in vivo role in relieving the Escherichia coli proto-ring block caused by excess ZapC.Interactions among the early Escherichia coli divisome proteins revealed by bimolecular fluorescence complementation.FzlA, an essential regulator of FtsZ filament curvature, controls constriction rate during Caulobacter division.

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P2860

Identification of ZapD as a cell division factor that promotes the assembly of FtsZ in Escherichia coli.

http://www.wikidata.org/entity/Q42190364

description

2012 nî lūn-bûn

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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2012年學術文章

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2012年學術文章

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name

Identification of ZapD as a ce ...... y of FtsZ in Escherichia coli.

@en

Identification of ZapD as a ce ...... y of FtsZ in Escherichia coli.

@nl

type

label

Identification of ZapD as a ce ...... y of FtsZ in Escherichia coli.

@en

Identification of ZapD as a ce ...... y of FtsZ in Escherichia coli.

@nl

prefLabel

Identification of ZapD as a ce ...... y of FtsZ in Escherichia coli.

@en

Identification of ZapD as a ce ...... y of FtsZ in Escherichia coli.

@nl

P1433

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Journal of Bacteriology

P1476

Identification of ZapD as a ce ...... y of FtsZ in Escherichia coli.

@en

P2093

Anuradha Janakiraman

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

Eugene Rivkin

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Guoxiang Fan

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Jorge Durand-Heredia

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Jorge Morales

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P2860

Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection

Dynamic assembly of FtsZ regulated by GTP hydrolysis.

OMA 2011: orthology inference among 1000 complete genomes

Growth rate-dependent regulation of medial FtsZ ring formation

Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast

Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division

One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products

Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research

FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one.

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

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3189-3198

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10.1128/JB.00176-12

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12

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194

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2012-04-13T00:00:00Z

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Escherichia coli

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3370873

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