Conserved <scp>GTPase</scp> mechanism in bacterial <scp>FtsZ</scp> and archaeal tubulin filaments-Reference-Cited by-同舟云学术

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Conserved GTPase mechanism in bacterial FtsZ and archaeal tubulin filaments

Published:2022-11-16 Issue: Volume: Page:
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:The FEBS Journal

Author:

Andreu José M.¹^ORCID,Ruiz Federico M.¹^ORCID,Fernández‐Tornero Carlos¹^ORCID

Affiliation:

1. Centro de Investigaciones Biológicas Margarita Salas CSIC Madrid Spain

Funder

Ministerio de Ciencia e Innovación

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.16675

Reference30 articles.

1. Tubulin and FtsZ form a distinct family of GTPases

2. Dynamic instability of microtubule growth

3. GTPase activity–coupled treadmilling of the bacterial tubulin FtsZ organizes septal cell wall synthesis

4. Structural insights into FtsZ protofilament formation

5. FtsZ filament structures in different nucleotide states reveal the mechanism of assembly dynamics

Cited by 2 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. Dynamic self-association of archaeal tubulin-like protein CetZ1 drivesHaloferax volcaniimorphogenesis;2024-04-08

2. New broad-spectrum and potent antibacterial agents with dual-targeting mechanism: Promoting FtsZ polymerization and disrupting bacterial membranes;European Journal of Medicinal Chemistry;2024-01

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