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2006
BouckaertJ, MackenzieJ, de PazJL, ChipwazaB, ChoudhuryD, ZavialovA, MannerstedtK, AndersonJ, PierardD, WynsL, SeebergerPH, OscarsonS, De Greve H, KnightSD.  2006.  The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes. Molecular Microbiology. 61(6):1556-1568. Abstract
BouckaertJ, MackenzieJ, de PazJL, ChipwazaB, ChoudhuryD, ZavialovA, MannerstedtK, AndersonJ, PierardD, WynsL, SeebergerPH, OscarsonS, De GreveH, KnightSD.  2006.  The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes. Molecular Microbiology. 61(6):1556-1568.
2005
ButsL, WellensA, Van MolleI, WynsL, LorisR, LahmannM, OscarsonS, De GreveH, BouckaertJ.  2005.  Impact of natural variation in bacterial F17G adhesins on crystallization behaviour. Acta Cryst. D. 61(Pt 8):1149-1159. Abstract
BouckaertJ, BerglundJ, SchembriM, De Genst E, CoolsL, WuhrerM, HungCS, PinknerJ, SlattegardR, ZavialovA, ChoudhuryD, LangermannS, HultgrenSJ, WynsL, KlemmP, OscarsonS, KnightSD, De Greve H.  2005.  Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin. Molecular Microbiology. 55(2):441-455. Abstract
BouckaertJ, BerglundJ, SchembriM, De GenstE, CoolsL, WuhrerM, HungCS, PinknerJ, SlattegardR, ZavialovA, ChoudhuryD, LangermannS, HultgrenSJ, WynsL, KlemmP, OscarsonS, KnightSD, De GreveH.  2005.  Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin. Molecular Microbiology. 55(2):441-455.
2003
ButsL, BouckaertJ, De Genst E, LorisR, OscarsonS, LahmannM, MessensJ, BrosensE, WynsL, De Greve H.  2003.  The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine. Mol. Microbiol.. 49(3):705-715. Abstract
ButsL, LorisR, De GenstE, OscarsonS, LahmannM, MessensJ, BrosensE, WynsL, De GreveH, BouckaertJ.  2003.  Solving the phase problem for carbohydrate-binding proteins using selenium derivatives of their ligands: a case study involving the bacterial F17-G adhesin. Acta Crystallogr. D. 59(Pt 6):1012-1015. Abstract