| pubmed-article:3122025 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3122025 | lifeskim:mentions | umls-concept:C0009055 | lld:lifeskim |
| pubmed-article:3122025 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:3122025 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:3122025 | lifeskim:mentions | umls-concept:C0596543 | lld:lifeskim |
| pubmed-article:3122025 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:3122025 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:3122025 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3122025 | pubmed:dateCreated | 1988-2-10 | lld:pubmed |
| pubmed-article:3122025 | pubmed:abstractText | Exoenzyme C3 from Clostridium botulinum types C and D specifically ADP-ribosylated a 21-kilodalton cellular protein, p21.bot. Guanyl nucleotides protected the substrate against denaturation, which implies that p21.bot is a G protein. When introduced into the interior of cells, purified exoenzyme C3 ADP-ribosylated intracellular p21.bot and changed its function. NIH 3T3, PC12, and other cells rapidly underwent temporary morphological alterations that were in certain respects similar to those seen after microinjection of cloned ras proteins. When injected into Xenopus oocytes, C3 induced migration of germinal vesicles and potentiated the cholera toxin-sensitive augmentation of germinal vesicle breakdown by progesterone, also as caused by ras proteins. Nevertheless, p21.bot was immunologically distinct from p21ras. | lld:pubmed |
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| pubmed-article:3122025 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:3122025 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3122025 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3122025 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:3122025 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:3122025 | pubmed:author | pubmed-author:BoquetPP | lld:pubmed |
| pubmed-article:3122025 | pubmed:author | pubmed-author:GillD MDM | lld:pubmed |
| pubmed-article:3122025 | pubmed:author | pubmed-author:PopoffM RMR | lld:pubmed |
| pubmed-article:3122025 | pubmed:author | pubmed-author:RubinE JEJ | lld:pubmed |
| pubmed-article:3122025 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3122025 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:3122025 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3122025 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3122025 | pubmed:pagination | 418-26 | lld:pubmed |
| pubmed-article:3122025 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:3122025 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3122025 | pubmed:articleTitle | Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum. | lld:pubmed |
| pubmed-article:3122025 | pubmed:affiliation | Department of Molecular Biology and Microbiology, School of Medicine, Tufts University, Boston, Massachusetts 02111. | lld:pubmed |
| pubmed-article:3122025 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3122025 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3122025 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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