Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinE-Reference-Cited by-同舟云学术

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Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinE

Published:2010-10-11 Issue:43 Volume:107 Page:18416-18421
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Ghasriani H.,Ducat T.,Hart C. T.,Hafizi F.,Chang N.,Al-Baldawi A.,Ayed S. H.,Lundstrom P.,Dillon J.-A. R.,Goto N. K.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference43 articles.

1. Min Oscillation in Bacteria

2. Topological regulation of cell division in Escherichia coli involves rapid pole to pole oscillation of the division inhibitor MinC under the control of MinD and MinE

3. MinDE-Dependent Pole-to-Pole Oscillation of Division Inhibitor MinC in Escherichia coli

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

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

Cited by 38 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Positioning of cellular components by the ParA/MinD family of ATPases;Current Opinion in Microbiology;2024-06

2. Dissecting the phase separation and oligomerization activities of the carboxysome positioning protein McdB;eLife;2023-09-05

3. Robust and resource-optimal dynamic pattern formation of Min proteinsin vivo;2023-08-16

4. Interaction of the bacterial division regulator MinE with lipid bicelles studied by NMR spectroscopy;Journal of Biological Chemistry;2023-04

5. Dissecting the phase separation and oligomerization activities of the carboxysome positioning protein McdB;2022-04-28

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