pubmed-article:3122724 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3122724 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:3122724 | lifeskim:mentions | umls-concept:C0018328 | lld:lifeskim |
pubmed-article:3122724 | lifeskim:mentions | umls-concept:C0085748 | lld:lifeskim |
pubmed-article:3122724 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:3122724 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:3122724 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:3122724 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:3122724 | pubmed:dateCreated | 1988-1-27 | lld:pubmed |
pubmed-article:3122724 | pubmed:abstractText | Besides botulinum C2 toxin, Clostridium botulinum type C produces another ADP-ribosyltransferase, which we termed 'C3'. ADP-ribosyltransferase C3 has a molecular mass of 25 kDa and modifies 21-24 kDa protein(s) in platelet and brain membranes. C3 was about 1000 times more potent than botulinum C1 toxin in ADP-ribosylation of membrane proteins. C3-catalysed ADP-ribosylation of the 21-24 kDa protein(s) was decreased by stable guanosine triphosphates, with the potency order GTP[S] much greater than p[NH]ppG greater than p[CH2]ppG. GTP[S] inhibited the ADP-ribosylation caused by C3 by maximally 70-80%, with half-maximal and maximal effects occurring at 0.3 and 10 microM-GTP[S] respectively. The concomitant addition of GTP decreased the inhibitory effect of GTP[S]. GTP[S]-induced inhibition of ADP-ribosylation was resistant to washing of pretreated platelet membranes. The data suggest that the novel botulinum ADP-ribosyltransferase C3 modifies eukaryotic 21-24 kDa guanine nucleotide-binding protein(s). | lld:pubmed |
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pubmed-article:3122724 | pubmed:language | eng | lld:pubmed |
pubmed-article:3122724 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3122724 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:3122724 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3122724 | pubmed:month | Oct | lld:pubmed |
pubmed-article:3122724 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:3122724 | pubmed:author | pubmed-author:FrevertJJ | lld:pubmed |
pubmed-article:3122724 | pubmed:author | pubmed-author:AktoriesKK | lld:pubmed |
pubmed-article:3122724 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3122724 | pubmed:day | 15 | lld:pubmed |
pubmed-article:3122724 | pubmed:volume | 247 | lld:pubmed |
pubmed-article:3122724 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3122724 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3122724 | pubmed:pagination | 363-8 | lld:pubmed |
pubmed-article:3122724 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:3122724 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3122724 | pubmed:articleTitle | ADP-ribosylation of a 21-24 kDa eukaryotic protein(s) by C3, a novel botulinum ADP-ribosyltransferase, is regulated by guanine nucleotide. | lld:pubmed |
pubmed-article:3122724 | pubmed:affiliation | Rudolf-Buchheim-Institut für Pharmakologie der Universität Giessen, Federal Republic of Germany. | lld:pubmed |
pubmed-article:3122724 | pubmed:publicationType | Journal Article | lld:pubmed |
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