Structure-Based Drug Design and Optimization of Mannoside Bacterial FimH Antagonists-Reference-Cited by-同舟云学术

Structure-Based Drug Design and Optimization of Mannoside Bacterial FimH Antagonists

Published:2010-05-27 Issue:12 Volume:53 Page:4779-4792
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Han Zhenfu¹,Pinkner Jerome S.²,Ford Bradley³,Obermann Robert¹,Nolan William¹,Wildman Scott A.¹,Hobbs Doug¹,Ellenberger Tom¹,Cusumano Corinne K.²,Hultgren Scott J.²,Janetka James W.¹

Affiliation:

1. Department of Biochemistry and Molecular Biophysics

2. Department of Molecular Microbiology, Center for Women’s Infectious Disease Research

3. Department of Pathology and Immunology

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm100438s

Reference39 articles.

1. Structural biology of the chaperone–usher pathway of pilus biogenesis

2. Molecular Variations in Klebsiella pneumoniae and Escherichia coli FimH Affect Function and Pathogenesis in the Urinary Tract

3. Positive selection identifies an in vivo role for FimH during urinary tract infection in addition to mannose binding

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

5. Type 1 pilus-mediated bacterial invasion of bladder epithelial cells

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