| pubmed-article:1544437 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1544437 | lifeskim:mentions | umls-concept:C0032086 | lld:lifeskim |
| pubmed-article:1544437 | lifeskim:mentions | umls-concept:C0035552 | lld:lifeskim |
| pubmed-article:1544437 | lifeskim:mentions | umls-concept:C0597295 | lld:lifeskim |
| pubmed-article:1544437 | lifeskim:mentions | umls-concept:C0244777 | lld:lifeskim |
| pubmed-article:1544437 | pubmed:issue | 2-3 | lld:pubmed |
| pubmed-article:1544437 | pubmed:dateCreated | 1992-4-13 | lld:pubmed |
| pubmed-article:1544437 | pubmed:abstractText | Many plants express enzymes which specifically remove an adenine residue from the skeleton of the 28 S RNA in the major subunit of the eukaryotic ribosome (ribosome inactivating proteins, RIPs). The site of action of RIPs (A4324 in the rRNA from rat liver) is in a loop structure whose nucleotide sequence all around the target adenine is also conserved in those species which are completely or partially insensitive to RIPs. In this paper we identify a covalent complex between saporin (the RIP extracted from Saponaria officinalis) and ribosomal proteins from yeast (Saccharomyces cerevisiae), by means of chemical crosslinking and immunological or avidin-biotin detection. The main complex (mol. wt. congruent to 60 kDa) is formed only with a protein from the 60 S subunit of yeast ribosomes, and is not detected with ribosomes from E. coli, a resistant species. This observation supports the hypothesis for a molecular recognition mechanism involving one or more ribosomal proteins, which could provide a 'receptor' site for the toxin and favour optimal binding of the target adenine A4324 to the active site of the RIP. | lld:pubmed |
| pubmed-article:1544437 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1544437 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1544437 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1544437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1544437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1544437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1544437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1544437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1544437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1544437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1544437 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1544437 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1544437 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1544437 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:1544437 | pubmed:author | pubmed-author:BrunoriMM | lld:pubmed |
| pubmed-article:1544437 | pubmed:author | pubmed-author:BellelliAA | lld:pubmed |
| pubmed-article:1544437 | pubmed:author | pubmed-author:IppolitiRR | lld:pubmed |
| pubmed-article:1544437 | pubmed:author | pubmed-author:LendaroEE | lld:pubmed |
| pubmed-article:1544437 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1544437 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:1544437 | pubmed:volume | 298 | lld:pubmed |
| pubmed-article:1544437 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1544437 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1544437 | pubmed:pagination | 145-8 | lld:pubmed |
| pubmed-article:1544437 | pubmed:dateRevised | 2008-7-12 | lld:pubmed |
| pubmed-article:1544437 | pubmed:meshHeading | pubmed-meshheading:1544437-... | lld:pubmed |
| pubmed-article:1544437 | pubmed:meshHeading | pubmed-meshheading:1544437-... | lld:pubmed |
| pubmed-article:1544437 | pubmed:meshHeading | pubmed-meshheading:1544437-... | lld:pubmed |
| pubmed-article:1544437 | pubmed:meshHeading | pubmed-meshheading:1544437-... | lld:pubmed |
| pubmed-article:1544437 | pubmed:meshHeading | pubmed-meshheading:1544437-... | lld:pubmed |
| pubmed-article:1544437 | pubmed:meshHeading | pubmed-meshheading:1544437-... | lld:pubmed |
| pubmed-article:1544437 | pubmed:meshHeading | pubmed-meshheading:1544437-... | lld:pubmed |
| pubmed-article:1544437 | pubmed:meshHeading | pubmed-meshheading:1544437-... | lld:pubmed |
| pubmed-article:1544437 | pubmed:meshHeading | pubmed-meshheading:1544437-... | lld:pubmed |
| pubmed-article:1544437 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1544437 | pubmed:articleTitle | A ribosomal protein is specifically recognized by saporin, a plant toxin which inhibits protein synthesis. | lld:pubmed |
| pubmed-article:1544437 | pubmed:affiliation | Department of Biochemical Sciences, University of Rome La Sapienza, Italy. | lld:pubmed |
| pubmed-article:1544437 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1544437 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1544437 | lld:pubmed |
