Biochemical analysis of GTPase FlhF which controls the number and position of flagellar formation in marine Vibrio - sprookjes - yvandenbroek - TriplyDB

Biochemical analysis of GTPase FlhF which controls the number and position of flagellar formation in marine Vibrio

Biochemical analysis of GTPase FlhF which controls the number and position of flagellar formation in marine Vibrio

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Biochemical analysis of GTPase FlhF which controls the number and position of flagellar formation in marine Vibrio

http://www.wikidata.org/entity/Q58782865

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article publié dans la revue scientifique Scientific Reports

@fr

im August 2018 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Scientific Reports

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в серпні 2018

@uk

name

Biochemical analysis of GTPase ...... lar formation in marine Vibrio

@en

Biochemical analysis of GTPase ...... lar formation in marine Vibrio

@nl

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Biochemical analysis of GTPase ...... lar formation in marine Vibrio

@en

Biochemical analysis of GTPase ...... lar formation in marine Vibrio

@nl

prefLabel

Biochemical analysis of GTPase ...... lar formation in marine Vibrio

@en

Biochemical analysis of GTPase ...... lar formation in marine Vibrio

@nl

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Scientific Reports

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Biochemical analysis of GTPase ...... lar formation in marine Vibrio

@en

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Akira Mizuno

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

Michio Homma

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Seiji Kojima

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

Shota Kondo

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Yoshino Imura

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P2860

The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site

The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP

Structural basis for the molecular evolution of SRP-GTPase activation by protein

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

How bacteria maintain location and number of flagella?

A self-associating protein critical for chromosome attachment, division, and polar organization in caulobacter

Cyclic diguanosine monophosphate represses bacterial flagella synthesis by interacting with the Walker A motif of the enhancer-binding protein FleQ

The GTPase activity of FlhF is dispensable for flagellar localization, but not motility, in Pseudomonas aeruginosa.

New prospects in studying the bacterial signal recognition particle pathway.

Polar flagellar biosynthesis and a regulator of flagellar number influence spatial parameters of cell division in Campylobacter jejuni

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scholarly article

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10.1038/S41598-018-30531-5

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1

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2018-08-14T00:00:00Z

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