Moderately thermostable phage Φ11 Cro repressor has novel DNA-binding capacity and physicochemical properties-Reference-Cited by-同舟云学术

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Moderately thermostable phage Φ11 Cro repressor has novel DNA-binding capacity and physicochemical properties

Published:2009-03-31 Issue:3 Volume:42 Page:160-165
ISSN:1976-6696
Container-title:BMB Reports
language:en
Short-container-title:BMB Reports

Author:

Das Malabika,Ganguly Tridib,Bandhu Amitava,Mondal Rajkrishna,Chanda Palas K.,Jana Biswanath,Sau Subrata

Publisher

Korean Society for Biochemistry and Molecular Biology - BMB Reports

Subject

Molecular Biology,Biochemistry,General Medicine

Link

http://ocean.kisti.re.kr/downfile/crosscheck/ksbmb/JAKO200910103445991.pdf

Reference19 articles.

1. Structure of phage 434 cro protein at 2.35 Å resolution

2. Refined structure of Cro repressor protein from bacteriophage λ suggests both flexibility and plasticity

3. Retroevolution of Cro toward a stable monomer

4. Secondary Structure Switching in Cro Protein Evolution

5. N15 Cro and λ Cro: Orthologous DNA-binding domains with completely different but equally effective homodimer interfaces

Cited by 13 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. The cofactors and domains of a staphylococcal capsule-producing enzyme preserve its structure, stability, shape and dimerization ability;The Journal of Biochemistry;2023-02-07

2. Studies on the gene regulation involved in the lytic–lysogenic switch in Staphylococcus aureus temperate bacteriophage Phi11;The Journal of Biochemistry;2020-07-23

3. Multiple Mechanisms Are Involved in Repression of Filamentous Phage SW1 Transcription by the DNA-Binding Protein FpsR;Journal of Molecular Biology;2019-03

4. Dimerization ability, denaturation mechanism, and the stability of a staphylococcal phage repressor and its two domains;International Journal of Biological Macromolecules;2019-03

5. Cloning, overexpression and purification of a novel two-domain protein of Staphylococcus aureus phage Phi11;Protein Expression and Purification;2019-02

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