| pubmed-article:795651 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:795651 | lifeskim:mentions | umls-concept:C1524059 | lld:lifeskim |
| pubmed-article:795651 | lifeskim:mentions | umls-concept:C0597295 | lld:lifeskim |
| pubmed-article:795651 | lifeskim:mentions | umls-concept:C0039947 | lld:lifeskim |
| pubmed-article:795651 | lifeskim:mentions | umls-concept:C1704686 | lld:lifeskim |
| pubmed-article:795651 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:795651 | pubmed:dateCreated | 1977-3-31 | lld:pubmed |
| pubmed-article:795651 | pubmed:abstractText | The inhibition by thiostrepton of the initiation of protein synthesis is exerted at a different level from the inhibition of reactions mediated by EF-Tu and EF-G in the elongation of protein synthesis. The presence of thiostrepton on the 50-S subunit completely prevents the binding of the EF-Tu - GTP - aa-tRNA complex and EF-G - GTP complex to the 70-S ribosome, resulting in cessation of protein synthesis at a concentration of 1 muM thiostrepton. On the other hand, during initiation thiostrepton impairs the coupling of the 50-S subunit with the 30-S initiation complex, indirectly causing inhibition of IF-2-dependent reactions. Impairment of the coupling is strongly influenced by the conditions of incubation. Since formation of formylmethionylpuromycin and the IF-2-dependent GTP hydrolysis are inhibited to the same extent and recycling of IF-2 can take place in the presence of thiostrepton, we conclude that the basic mechanism of inhibition of initiation differs from that of inhibition of elongation. | lld:pubmed |
| pubmed-article:795651 | pubmed:language | eng | lld:pubmed |
| pubmed-article:795651 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:795651 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:795651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:795651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:795651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:795651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:795651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:795651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:795651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:795651 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:795651 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:795651 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:795651 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:795651 | pubmed:author | pubmed-author:NaaktgeborenN... | lld:pubmed |
| pubmed-article:795651 | pubmed:author | pubmed-author:RoobolKK | lld:pubmed |
| pubmed-article:795651 | pubmed:author | pubmed-author:VoormaH OHO | lld:pubmed |
| pubmed-article:795651 | pubmed:author | pubmed-author:GubbensJJ | lld:pubmed |
| pubmed-article:795651 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:795651 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:795651 | pubmed:volume | 70 | lld:pubmed |
| pubmed-article:795651 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:795651 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:795651 | pubmed:pagination | 39-47 | lld:pubmed |
| pubmed-article:795651 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-A... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-M... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-T... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-M... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-K... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-E... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-R... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-R... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-P... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-G... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-P... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-P... | lld:pubmed |
| pubmed-article:795651 | pubmed:meshHeading | pubmed-meshheading:795651-T... | lld:pubmed |
| pubmed-article:795651 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:795651 | pubmed:articleTitle | The mode of action of thiostrepton in the initiation of protein synthesis. | lld:pubmed |
| pubmed-article:795651 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:795651 | lld:pubmed |
