Zobrazeno 1 - 10
of 52
pro vyhledávání: '"E. J. M. Van Damme"'
Transcriptional profiling of the lectin ArathEULS3 from Arabidopsis thaliana toward abiotic stresses
Autor:
B. Al Atalah, E. J. M. Van Damme, Nausicaä Lannoo, Lore Eggermont, J. Van Hove, K. De Schutter, Karolina Stefanowicz
Publikováno v:
Journal of Plant Physiology. 171:1763-1773
The family of EUL-related lectins groups all proteins with an Euonymus lectin (EUL) domain, a protein motif which is highly conserved throughout the plant kingdom and occurs as part of many chimeric proteins with different domain architectures. The S
Publikováno v:
Communications in agricultural and applied biological sciences. 80(2)
Entomotoxic proteins are produced by plants in defence against insect herbivory. Some carbohydrate-binding proteins exhibit strong insecticidal activity affecting the survival, growth, development and feeding behavior of phytophagous insects. The occ
Autor:
Herman Egberink, P L Delputte, E. J. M. Van Damme, F J U M van der Meer, Jan Balzarini, B. J. Haijema, Nancy Schuurman, C. A. M. de Haan, Willy J. Peumans
Publikováno v:
Antiviral Research
Coronaviruses are important human and animal pathogens, the relevance of which increased due to the emergence of new human coronaviruses like SARS-CoV, HKU1 and NL63. Together with toroviruses, arteriviruses, and roniviruses the coronaviruses belong
Autor:
I. Pohlmeyer, Uwe Pfüller, Udo Schumacher, E. J. M. Van Damme, Julia Jörns, U. Neumann, Willy J. Peumans
Publikováno v:
Journal of Veterinary Medicine Series A. 52:138-146
Summary Carbohydrates on epithelial cell surfaces play an important role as attachment sites for different microorganisms like bacteria, viruses and protozoa. To obtain more information about the distribution of carbohydrates on the luminal surface a
Publikováno v:
Journal of virological methods. 211
In this paper, the potential role of aphids in viroid transmission was explored. Apterous aphids were fed on pospiviroid-infected plants and viroid targets in the aphids were consequently quantified through RT-qPCR and localized within the aphid body
Autor:
E. J. M. Van Damme, Willy J. Peumans, Milos Grim, Zdenek Halata, P. Valášek, Uwe Pfüller, Udo Schumacher, O. Naňka
Publikováno v:
Anatomy and Embryology. 204:407-411
The lectin binding pattern of muscular microvessels in chick, quail and chick/quail chimeras was analysed. Paraffin wax sections of muscles from embryonic and adult animals were used. The biotin-labelled lectins were detected by avidin-alkaline phosp
Autor:
Christel Verboven, Anja Rabijns, E. J. M. Van Damme, Annick Barre, C. J. De Ranter, Willy J. Peumans, Pierre Rougé
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 44:470-478
The structure of the bark lectin RPbAI (isoform A4) from Robinia pseudoacacia has been determined by protein crystallography both in the free form and complexed with N-acetylgalactosamine. The free form is refined at 1.80 A resolution to an R-factor
Autor:
Zdenek Halata, K. Sames, B. Asmus, Roland Moll, Ingrid Moll, Udo Schumacher, Willy J. Peumans, E. J. M. Van Damme
Publikováno v:
Experimental Dermatology. 10:100-109
Changes in carbohydrate residue expression and in proteoglycan distribution occur during different stages of tumor development and progression. However, few data concerning carbohydrate residue analysis as performed by lectin histochemistry and prote
Publikováno v:
Bioscience Reports. 19:411-419
UDA (Urtica dioica agglutinin) contains two hevein like domains with two non-identical interacting sites and is specific for chitooligosaccharides. The binding of chitooligosaccharides to UDA was studied by Isothermal Titration Calorimetry. Each site
Autor:
Anthony K. Allen, E. J. M. Van Damme, L.M. Wright, Colin D. Reynolds, Willy J. Peumans, Annick Barre, Pierre Rougé, F. Van Leuven
Publikováno v:
Biochemical Journal. 340:299-308
Two lectins have been isolated from bluebell (Scilla campanulata) bulbs. From their isolation by affinity chromatography, they are characterized as a mannose-binding lectin (SCAman) and a fetuin-binding lectin (SCAfet). SCAman preferentially binds ol