| pubmed-article:10785398 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10785398 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:10785398 | lifeskim:mentions | umls-concept:C1011932 | lld:lifeskim |
| pubmed-article:10785398 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:10785398 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:10785398 | lifeskim:mentions | umls-concept:C0009017 | lld:lifeskim |
| pubmed-article:10785398 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:10785398 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:10785398 | pubmed:dateCreated | 2000-6-15 | lld:pubmed |
| pubmed-article:10785398 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10785398 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10785398 | pubmed:abstractText | Leaves of the monocotyledonous plant Polygonatum multiflorum L. (Solomon's seal) contain besides a monocot mannose-binding lectin two galactose/N-acetylgalactosamine (Gal/GalNAc)-binding type 2 ribosome-inactivating proteins (RIPs). Both RIPs were purified using a combination of classical protein purification techniques and affinity chromatography. Although both RIPs consist of protomers of 65 kDa, the P. multiflorum RIP monomer (PMRIPm) occurs as a monomer of approximately 60 kDa, whereas the tetramer (PMRIPt) is a tetramer of 240 kDa. Both RIPs exhibit similar RNA N-glycosidase activity but differ in their specific agglutination activity and carbohydrate-binding specificity, PMRIPt being a GalNAc-specific lectin whereas PMRIPm is Gal/GalNAc-specific. Toxicity tests indicated that both Polygonatum RIPs exhibit a very low cytotoxicity towards human and animal cells. Analysis of the genomic clones encoding both RIPs revealed a high degree of sequence similarity to other type 2 RIPs. Molecular modelling confirmed that both Polygonatum RIPs have a similar structure to ricin. | lld:pubmed |
| pubmed-article:10785398 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10785398 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10785398 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10785398 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10785398 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10785398 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10785398 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10785398 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10785398 | pubmed:month | May | lld:pubmed |
| pubmed-article:10785398 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:10785398 | pubmed:author | pubmed-author:PeumansW JWJ | lld:pubmed |
| pubmed-article:10785398 | pubmed:author | pubmed-author:Van LeuvenFF | lld:pubmed |
| pubmed-article:10785398 | pubmed:author | pubmed-author:RougéPP | lld:pubmed |
| pubmed-article:10785398 | pubmed:author | pubmed-author:CARGOG TGT | lld:pubmed |
| pubmed-article:10785398 | pubmed:author | pubmed-author:HalTT | lld:pubmed |
| pubmed-article:10785398 | pubmed:author | pubmed-author:Van DammeE... | lld:pubmed |
| pubmed-article:10785398 | pubmed:author | pubmed-author:CharelsDD | lld:pubmed |
| pubmed-article:10785398 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10785398 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:10785398 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10785398 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10785398 | pubmed:pagination | 2746-59 | lld:pubmed |
| pubmed-article:10785398 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:10785398 | pubmed:meshHeading | pubmed-meshheading:10785398... | lld:pubmed |
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| pubmed-article:10785398 | pubmed:meshHeading | pubmed-meshheading:10785398... | lld:pubmed |
| pubmed-article:10785398 | pubmed:meshHeading | pubmed-meshheading:10785398... | lld:pubmed |
| pubmed-article:10785398 | pubmed:meshHeading | pubmed-meshheading:10785398... | lld:pubmed |
| pubmed-article:10785398 | pubmed:meshHeading | pubmed-meshheading:10785398... | lld:pubmed |
| pubmed-article:10785398 | pubmed:meshHeading | pubmed-meshheading:10785398... | lld:pubmed |
| pubmed-article:10785398 | pubmed:meshHeading | pubmed-meshheading:10785398... | lld:pubmed |
| pubmed-article:10785398 | pubmed:meshHeading | pubmed-meshheading:10785398... | lld:pubmed |
| pubmed-article:10785398 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10785398 | pubmed:articleTitle | Characterization and molecular cloning of two different type 2 ribosome-inactivating proteins from the monocotyledonous plant Polygonatum multiflorum. | lld:pubmed |
| pubmed-article:10785398 | pubmed:affiliation | Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Belgium. Els.VanDamme@agr.kuleuven.ac.be | lld:pubmed |
| pubmed-article:10785398 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10785398 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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