Detailed Information on Publication Record
2010
Aspergillus fumigatus lectins - how to stay in touch
HOUSER, Josef, Jan KOMÁREK, Nikola KOSTLÁNOVÁ, Gianluca CIOCCI, Anne IMBERTY et. al.Basic information
Original name
Aspergillus fumigatus lectins - how to stay in touch
Name in Czech
Lektiny Aspergillus fumigatus - jak zůstat v kontaktu
Name (in English)
Aspergillus fumigatus lectins - how to stay in touch
Authors
HOUSER, Josef (203 Czech Republic, belonging to the institution), Jan KOMÁREK (203 Czech Republic, belonging to the institution), Nikola KOSTLÁNOVÁ (203 Czech Republic, belonging to the institution), Gianluca CIOCCI (380 Italy), Anne IMBERTY (250 France) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution)
Edition
XIV.Setkání biochemiků a molekulárních biologů, 2010
Other information
Language
Czech
Type of outcome
Konferenční abstrakt
Field of Study
10600 1.6 Biological sciences
Country of publisher
Czech Republic
Confidentiality degree
není předmětem státního či obchodního tajemství
RIV identification code
RIV/00216224:14310/10:00044026
Organization unit
Faculty of Science
ISBN
978-80-210-5164-5
Keywords (in Czech)
Aspergillus fumigatus lektin
Keywords in English
Aspergillus fumigatus lectin
Změněno: 6/1/2011 10:17, Mgr. Josef Houser, Ph.D.
V originále
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.
In English
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.
Links
GA303/09/1168, research and development project |
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GD301/09/H004, research and development project |
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LC06030, research and development project |
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ME08008, research and development project |
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MSM0021622413, plan (intention) |
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