| pubmed-article:12023903 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12023903 | lifeskim:mentions | umls-concept:C0016767 | lld:lifeskim |
| pubmed-article:12023903 | lifeskim:mentions | umls-concept:C0331059 | lld:lifeskim |
| pubmed-article:12023903 | lifeskim:mentions | umls-concept:C0331057 | lld:lifeskim |
| pubmed-article:12023903 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:12023903 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12023903 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:12023903 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:12023903 | lifeskim:mentions | umls-concept:C0560013 | lld:lifeskim |
| pubmed-article:12023903 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:12023903 | pubmed:dateCreated | 2002-5-23 | lld:pubmed |
| pubmed-article:12023903 | pubmed:abstractText | Sambucus nigra agglutinin I (SNA-I) is a type 2 ribosome-inactivating protein. Site-directed mutagenesis was used to mimic the conversion of the highly active B-chain of fruit-specific SNA (SNA-If) into the completely inactive B-chain of the closely related and naturally occurring loss-of-activity mutant called S. nigra agglutinin lectin-related protein. In the first mutant SNA-If-M1 the high-affinity site 2 of SNA-If was disrupted by replacing the presumed critical residue Asp231 with Glu231. In the double mutant SNA-If-M2, site 1 of SNA-If-M1 was also disrupted by substituting the presumed critical residue Asn48 with Ser48. The parent type 2 ribosome-inactivating protein and both mutants were expressed in Nicotiana tabacum Samsun NN and the recombinant proteins were purified and analysed. Recombinant SNA-If agglutinated rabbit erythrocytes equally well as SNA-If, but both mutants were completely inactive in this test. Binding assays to immobilized galactose and fetuin revealed that the mutation Asp231-->Glu231 reduces the affinity of the B-chain for galactose and fetuin by more than 50%. Furthermore, the introduction of the second mutation Asn48-->Ser48 reduces the binding activity to less than 20% of the original activity. | lld:pubmed |
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| pubmed-article:12023903 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12023903 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12023903 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12023903 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12023903 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12023903 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12023903 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12023903 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12023903 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12023903 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:12023903 | pubmed:author | pubmed-author:ChenYingY | lld:pubmed |
| pubmed-article:12023903 | pubmed:author | pubmed-author:RougePierreP | lld:pubmed |
| pubmed-article:12023903 | pubmed:author | pubmed-author:PeumansWilly... | lld:pubmed |
| pubmed-article:12023903 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:12023903 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12023903 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12023903 | pubmed:volume | 364 | lld:pubmed |
| pubmed-article:12023903 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12023903 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12023903 | pubmed:pagination | 587-92 | lld:pubmed |
| pubmed-article:12023903 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12023903 | pubmed:meshHeading | pubmed-meshheading:12023903... | lld:pubmed |
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| pubmed-article:12023903 | pubmed:meshHeading | pubmed-meshheading:12023903... | lld:pubmed |
| pubmed-article:12023903 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12023903 | pubmed:articleTitle | Mutational analysis of the carbohydrate-binding activity of the NeuAc(alpha-2,6)Gal/GalNAc-specific type 2 ribosome-inactivating protein from elderberry (Sambucus nigra) fruits. | lld:pubmed |
| pubmed-article:12023903 | pubmed:affiliation | Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Willem de Croylaan 42, B-3001 Leuven, Belgium. | lld:pubmed |
| pubmed-article:12023903 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12023903 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
