Matches in UGent Biblio for { <https://biblio.ugent.be/publication/3128860#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B419863.
- aggregation creator B419864.
- aggregation creator B419865.
- aggregation creator B419866.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2012".
- aggregation format "application/pdf".
- aggregation hasFormat 3128860.bibtex.
- aggregation hasFormat 3128860.csv.
- aggregation hasFormat 3128860.dc.
- aggregation hasFormat 3128860.didl.
- aggregation hasFormat 3128860.doc.
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- aggregation hasFormat 3128860.txt.
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- aggregation hasFormat 3128860.yaml.
- aggregation isPartOf urn:issn:0282-0080.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Expression analysis of a type S2 EUL-related lectin from rice in Pichia pastoris".
- aggregation abstract "Rice (Oryza sativa) expresses different putative carbohydrate-binding proteins belonging to the class of lectins containing an Euonymus lectin (EUL)-related domain, one of them being OrysaEULS2. The OrysaEULS2 sequence consists of a 56 amino acid N-terminal domain followed by the EUL sequence. In this paper the original sequence of the EUL domain of OrysaEULS2 and some mutant forms have been expressed in Pichia pastoris. Subsequently, the recombinant proteins were purified and their carbohydrate binding properties determined. Analysis of the original protein on the glycan array revealed interaction with mannose containing structures and to a lesser extent with glycans containing lactosamine related structures. It was shown that mutation of tryptophan residue 134 into leucine resulted in an almost complete loss of carbohydrate binding activity of OrysaEULS2. Our results show that the EUL domain in OrysaEULS2 interacts with glycan structures, and hence can be considered as a lectin. However, the binding of the protein with the array is much weaker than that of other EUL-related lectins. Furthermore, our results indicate that gene divergence within the family of EUL-related lectins lead to changes in carbohydrate binding specificity.".
- aggregation authorList BK741455.
- aggregation endPage "479".
- aggregation issue "7".
- aggregation startPage "467".
- aggregation volume "29".
- aggregation aggregates 3128887.
- aggregation isDescribedBy 3128860.
- aggregation similarTo s10719-012-9405-2.
- aggregation similarTo LU-3128860.