The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes-Reference-Cited by-同舟云学术

The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes

Published:2006-09 Issue:6 Volume:61 Page:1556-1568
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Mol Microbiol

Author:

Bouckaert Julie,Mackenzie Jenny,de Paz Jose L.,Chipwaza Beatrice,Choudhury Devapriya,Zavialov Anton,Mannerstedt Karin,Anderson Jennifer,Pierard Denis,Wyns Lode,Seeberger Peter H.,Oscarson Stefan,De Greve Henri,Knight Stefan D.

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.2006.05352.x/fullpdf

Reference56 articles.

1. Conservation of the D-mannose-adhesion protein among type 1 fimbriated members of the family Enterobacteriaceae

2. Oligosaccharide and Glycoprotein Microarrays as Tools in HIV Glycobiology

3. Chaperone-Subunit-Usher Interactions Required for Donor Strand Exchange during Bacterial Pilus Assembly

4. Tamm-Horsfall protein knockout mice are more prone to urinary tract infection Rapid Communication

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