Dynamics of interdomain rotation facilitates FtsZ filament assembly-Reference-Cited by-同舟云学术

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Dynamics of interdomain rotation facilitates FtsZ filament assembly

Published:2024-06 Issue:6 Volume:300 Page:107336
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Chakraborty Joyeeta,Poddar Sakshi,Dutta Soumyajit,Bahulekar Vaishnavi,Harne Shrikant,Srinivasan Ramanujam,Gayathri Pananghat^ORCID

Funder

India Ministry of Science & Technology Department of Biotechnology

Ministry of Education

European Synchrotron Radiation Facility

Indian Institute of Science Education and Research Pune

Science and Engineering Research Board

Department of Atomic Energy, Government of India

National Cancer Institute - Singapore

Department of Science and Technology, Ministry of Science and Technology, India

Publisher

Elsevier BV

Reference66 articles.

1. Cell shape and division in Escherichia coli: experiments with shape and division mutants;Begg;J. Bacteriol.,1985

2. Tubulin and FtsZ form a distinct family of GTPases;Nogales;Nat. Struct. Biol.,1998

3. FtsZ ring structure associated with division in Escherichia coli;Bi;Nature,1991

4. Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli;Hale;Cell,1997

5. Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein;Ma;Proc. Natl. Acad. Sci. U. S. A.,1996

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