MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunits - Wikidata - wikimedia - TriplyDB

MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunits

MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunits

http://www.wikidata.org/entity/Q42563460

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The Nucleoid Occlusion SlmA Protein Accelerates the Disassembly of the FtsZ Protein Polymers without Affecting Their GTPase Activity MinCDE exploits the dynamic nature of FtsZ filaments for its spatial regulation 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.Bacterial cytoskeleton and implications for new antibiotic targets.FtsZ Polymers Tethered to the Membrane by ZipA Are Susceptible to Spatial Regulation by Min Waves.Intrinsic characteristics of Min proteins on the cell division of Helicobacter pylori.MinC/MinD copolymers are not required for Min function.Control by potassium of the size distribution of Escherichia coli FtsZ polymers is independent of GTPase activity.MinC, MinD, and MinE drive counter-oscillation of early-cell-division proteins prior to Escherichia coli septum formation.MinC and FtsZ mutant analysis provides insight into MinC/MinD-mediated Z Ring disassembly.

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P2860

MinC protein shortens FtsZ protofilaments by preferentially interacting with GDP-bound subunits

http://www.wikidata.org/entity/Q42563460

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

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2013年论文

@zh-cn

name

MinC protein shortens FtsZ pro ...... acting with GDP-bound subunits

@en

MinC protein shortens FtsZ pro ...... acting with GDP-bound subunits

@nl

type

label

MinC protein shortens FtsZ pro ...... acting with GDP-bound subunits

@en

MinC protein shortens FtsZ pro ...... acting with GDP-bound subunits

@nl

prefLabel

MinC protein shortens FtsZ pro ...... acting with GDP-bound subunits

@en

MinC protein shortens FtsZ pro ...... acting with GDP-bound subunits

@nl

P1433

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P356

JBC.M113.483222

P1433

Journal of Biological Chemistry

P1476

MinC protein shortens FtsZ pro ...... acting with GDP-bound subunits

@en

P2093

Belén Reija

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

Concepción García-Montañés

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

William Margolin

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

P2860

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

Crystal structure of the bacterial cell division inhibitor MinC.

Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC

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

Spatial regulators for bacterial cell division self-organize into surface waves in vitro

Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis

Wnt isoform-specific interactions with coreceptor specify inhibition or potentiation of signaling by LRP6 antibodies

An improved assay for nanomole amounts of inorganic phosphate

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

P304

24625-24635

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P31

scholarly article

P356

10.1074/JBC.M113.483222

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P407

P433

34

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P478

288

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P50

Begoña Monterroso

Víctor M. Hernández-Rocamora

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2013-07-12T00:00:00Z

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23853099

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P932

3750160

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