An intrinsically disordered linker plays a critical role in bacterial cell division-Reference-Cited by-同舟云学术

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An intrinsically disordered linker plays a critical role in bacterial cell division

Published:2015-01 Issue: Volume:37 Page:3-10
ISSN:1084-9521
Container-title:Seminars in Cell & Developmental Biology
language:en
Short-container-title:Seminars in Cell & Developmental Biology

Author:

Buske P.J.,Mittal Anuradha,Pappu Rohit V.,Levin Petra Anne

Funder

National Institutes of Health

National Science Foundation

Publisher

Elsevier BV

Subject

Cell Biology,Developmental Biology

Reference62 articles.

1. Assembly dynamics of FtsZ rings in Bacillus subtilis and Escherichia coli and effects of FtsZ-regulating proteins;Anderson;J Bacteriol,2004

2. Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins;Buske;J Biol Chem,2012

3. Assembly dynamics of the bacterial cell division protein FTSZ: poised at the edge of stability;Romberg;Annu Rev Microbiol,2003

4. In vivo organization of the FtsZ-ring by ZapA and ZapB revealed by quantitative super-resolution microscopy;Buss;Mol Microbiol,2013

5. In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM);Fu;PLoS ONE,2010

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1. Protein structure–function continuum model: Emerging nexuses between specificity, evolution, and structure;Protein Science;2024-03-27

2. Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution;2024-03-19

3. Crosslinking by ZapD drives the assembly of short FtsZ filaments into toroidal structures in solution;2024-03-19

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5. Escherichia coli FtsZ molecular dynamics simulations;Journal of Biomolecular Structure and Dynamics;2023-05-09

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