"Aspergillus fumigatus lectins - how to stay in touch" . "Kostl\u00E1nov\u00E1, Nikola" . "Aspergillus fumigatus lectins - how to stay in touch"@en . "Aspergillus fumigatus lectins - how to stay in touch"@en . . . "Ciocci, Gianluca" . "Saprophytic fungus Aspergillus fumigatus is widespread alergen and an important pathogen for immunocompromised patients as well. Typical way, which many pathogens including Aspergillus utilize for binding to host-cells, is via sugar-binding proteins - lectins. In our research group we combine structural and functional approaches to precisely describe lectins' binding properties. Together with bioinformatics and molecular modeling we build up a complex picture of these biologicaly and medicaly important macromolecules."@cs . . . . . . "RIV/00216224:14310/10:00044026" . "Saprophytic fungus Aspergillus fumigatus is widespread alergen and an important pathogen for immunocompromised patients as well. Typical way, which many pathogens including Aspergillus utilize for binding to host-cells, is via sugar-binding proteins - lectins. In our research group we combine structural and functional approaches to precisely describe lectins' binding properties. Together with bioinformatics and molecular modeling we build up a complex picture of these biologicaly and medicaly important macromolecules."@en . "[3124D0F7859B]" . . "6"^^ . . . "Houser, Josef" . "Aspergillus fumigatus lectins - how to stay in touch" . . . . "P(GA303/09/1168), P(GD301/09/H004), P(LC06030), P(ME08008), R, Z(MSM0021622413)" . . . . . . "Wimmerov\u00E1, Michaela" . . "4"^^ . . "Kom\u00E1rek, Jan" . "Imberty, Anne" . "Aspergillus fumigatus lectin"@en . . "247855" . "Aspergillus fumigatus lectins - how to stay in touch"@cs . . "14310" . "Aspergillus fumigatus lectins - how to stay in touch"@cs . "Saprophytic fungus Aspergillus fumigatus is widespread alergen and an important pathogen for immunocompromised patients as well. Typical way, which many pathogens including Aspergillus utilize for binding to host-cells, is via sugar-binding proteins - lectins. In our research group we combine structural and functional approaches to precisely describe lectins' binding properties. Together with bioinformatics and molecular modeling we build up a complex picture of these biologicaly and medicaly important macromolecules." . "RIV/00216224:14310/10:00044026!RIV11-GA0-14310___" .