N-terminal truncation enables crystallization of the receptor-binding domain of the FedF bacterial adhesin-Reference-Cited by-同舟云学术

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N-terminal truncation enables crystallization of the receptor-binding domain of the FedF bacterial adhesin

Published:2006-11-30 Issue:12 Volume:62 Page:1278-1282
ISSN:1744-3091
Container-title:Acta Crystallographica Section F Structural Biology and Crystallization Communications
language:
Short-container-title:Acta Cryst Sect F

Author:

De Kerpel Maia,Van Molle Inge,Brys Lea,Wyns Lode,De Greve Henri,Bouckaert Julie

Publisher

International Union of Crystallography (IUCr)

Subject

Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics

Link

http://journals.iucr.org/f/issues/2006/12/00/bw5175/bw5175.pdf

Cited by 11 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. Effect of Gravity on Bacterial Adhesion to Heterogeneous Surfaces;Pathogens;2023-07-15

2. Immunoglobulin-fold containing bacterial adhesins: molecular and structural perspectives in host tissue colonization and infection;FEMS Microbiology Letters;2020-12-23

3. Duality of β-glucan microparticles: antigen carrier and immunostimulants;International Journal of Nanomedicine;2016-05

4. Nanobody Mediated Inhibition of Attachment of F18 Fimbriae Expressing Escherichia coli;PLoS ONE;2014-12-11

5. Structural Sampling of Glycan Interaction Profiles Reveals Mucosal Receptors for Fimbrial Adhesins of Enterotoxigenic Escherichia coli;Biology;2013-07-01

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