Publications
Found 11 results
Filters: Keyword is Adhesins, Escherichia coli and Author is De Greve, Henri [Clear All Filters]
"Inflammation-Induced Adhesin-Receptor Interaction Provides a Fitness Advantage to Uropathogenic E. coli during Chronic Infection.",
Cell Host Microbe, vol. 20, issue 4, pp. 482-492, 2016 Oct 12.
"Structural and adhesive properties of the long polar fimbriae protein LpfD from adherent-invasive Escherichia coli.",
Acta Crystallogr D Biol Crystallogr, vol. 71, issue Pt 8, pp. 1615-26, 2015 Aug.
"Structural and functional insight into the carbohydrate receptor binding of F4 fimbriae-producing enterotoxigenic Escherichia coli.",
J Biol Chem, vol. 290, issue 13, pp. 8409-19, 2015 Mar 27.
"Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies.",
Vet Res, vol. 46, pp. 14, 2015 Feb 24.
"The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces.",
Acta Crystallogr D Biol Crystallogr, vol. 65, issue Pt 5, pp. 411-20, 2009 May.
"Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG.",
J Mol Biol, vol. 394, issue 5, pp. 957-67, 2009 Dec 18.
"Surface display of the receptor-binding domain of the F17a-G fimbrial adhesin through the autotransporter AIDA-I leads to permeability of bacterial cells.",
Microbiology, vol. 155, issue Pt 2, pp. 468-76, 2009 Feb.
"Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex.",
PLoS One, vol. 3, issue 4, pp. e2040, 2008.
"Chloroplasts assemble the major subunit FaeG of Escherichia coli F4 (K88) fimbriae to strand-swapped dimers.",
J Mol Biol, vol. 368, issue 3, pp. 791-9, 2007 May 4.
"Crystallization of the FaeE chaperone of Escherichia coli F4 fimbriae.",
Acta Crystallogr Sect F Struct Biol Cryst Commun, vol. 61, issue Pt 4, pp. 427-31, 2005 Apr 1.
"The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine.",
Mol Microbiol, vol. 49, issue 3, pp. 705-15, 2003 Aug.