Structure, Folding and Stability of FimA, the Main Structural Subunit of Type 1 Pili from Uropathogenic Escherichia coli Strains-Reference-Cited by-同舟云学术

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Structure, Folding and Stability of FimA, the Main Structural Subunit of Type 1 Pili from Uropathogenic Escherichia coli Strains

Published:2011-09 Issue:3 Volume:412 Page:520-535
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Puorger Chasper,Vetsch Michael,Wider Gerhard,Glockshuber Rudi

Funder

Swiss National Science Foundation

Swiss Federal Institute of Technology Zurich within the framework of the National Center for Competence in Research Structural Biology Program

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference66 articles.

1. FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens;Zavialov;FEMS Microbiol. Rev.,2007

2. Structural biology of the chaperone–usher pathway of pilus biogenesis;Waksman;Nat. Rev., Microbiol.,2009

3. FimH adhesin of type 1 pili is assembled into a fibrillar tip structure in the Enterobacteriaceae;Jones;Proc. Natl Acad. Sci. USA,1995

4. X-ray structure of the FimC–FimH chaperone–adhesin complex from uropathogenic Escherichia coli;Choudhury;Science,1999

5. Uroplakin Ia is the urothelial receptor for uropathogenic Escherichia coli: evidence from in vitro FimH binding;Zhou;J. Cell Sci.,2001

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