Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres-Reference-Cited by-同舟云学术

Phage tail fibre assembly proteins employ a modular structure to drive the correct folding of diverse fibres

Published:2019-06-17 Issue:10 Volume:4 Page:1645-1653
ISSN:2058-5276
Container-title:Nature Microbiology
language:en
Short-container-title:Nat Microbiol

Author:

North Olesia I.^ORCID,Sakai Kouhei,Yamashita Eiki^ORCID,Nakagawa Atsushi^ORCID,Iwazaki Takuma,Büttner Carina R.,Takeda Shigeki^ORCID,Davidson Alan R.^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Microbiology (medical),Genetics,Applied Microbiology and Biotechnology,Immunology,Microbiology

Link

http://www.nature.com/articles/s41564-019-0477-7.pdf

Reference46 articles.

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2. Wilson, J. H., Luftig, R. B. & Wood, W. B. Interaction of bacteriophage T4 tail fiber components with a lipopolysaccharide fraction from Escherichia coli. J. Mol. Biol. 51, 423–434 (1970).

3. Le, S. et al. Mapping the tail fiber as the receptor binding protein responsible for differential host specificity of Pseudomonas aeruginosa bacteriophages PaP1 and JG004. PLoS ONE 8, e68562 (2013).

4. Grundy, F. J. & Howe, M. M. Involvement of the invertible G segment in bacteriophage Mu tail fiber biosynthesis. Virology 134, 296–317 (1984).

5. Bartual, S. G., Garcia-Doval, C., Alonso, J., Schoehn, G. & van Raaij, M. J. Two-chaperone assisted soluble expression and purification of the bacteriophage T4 long tail fibre protein gp37. Protein Expr. Purif. 70, 116–121 (2010).

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