| pubmed-article:9268331 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C0030933 | lld:lifeskim |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C0059040 | lld:lifeskim |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9268331 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9268331 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:9268331 | pubmed:dateCreated | 1997-10-2 | lld:pubmed |
| pubmed-article:9268331 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9268331 | pubmed:abstractText | Bovine mitochondrial elongation factor Ts (EF-Tsmt) stimulates the activity of Escherichia coli elongation factor Tu (EF-Tu). In contrast, E. coli EF-Ts is unable to stimulate mitochondrial EF-Tu. EF-Tsmt forms a tight complex with E. coli EF-Tu governed by an association constant of 8.6 x 10(10). This value is 100-fold stronger than the binding constant for the formation of the E. coli EF-Tu.Ts complex. To test which domain of EF-Tsmt is important for its strong binding with EF-Tu, chimeras were made between E. coli EF-Ts and EF-Tsmt. Replacing the N-terminal domain of E. coli EF-Ts with that of EF-Tsmt increases its binding to E. coli EF-Tu 2-3-fold. Replacing the N-terminal domain of EF-Tsmt with the corresponding region of E. coli EF-Ts decreases its binding to E. coli EF-Tu approximately 4-5-fold. A chimera consisting of the C-terminal half of E. coli EF-Ts and the N-terminal half of EF-Tsmt binds to E. coli EF-Tu as strongly as EF-Tsmt. A chimera in which Subdomain N of the core of EF-Ts is replaced by the corresponding region of EF-Tsmt binds E. coli EF-Tu approximately 25-fold more tightly than E. coli EF-Ts. Thus, the higher strength of the interaction between EF-Tsmt and EF-Tu can be localized primarily to a single subdomain. | lld:pubmed |
| pubmed-article:9268331 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9268331 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9268331 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9268331 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9268331 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9268331 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9268331 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9268331 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9268331 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9268331 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9268331 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9268331 | pubmed:author | pubmed-author:SpremulliL... | lld:pubmed |
| pubmed-article:9268331 | pubmed:author | pubmed-author:SurJJ | lld:pubmed |
| pubmed-article:9268331 | pubmed:author | pubmed-author:ZhangYY | lld:pubmed |
| pubmed-article:9268331 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9268331 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:9268331 | pubmed:volume | 272 | lld:pubmed |
| pubmed-article:9268331 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9268331 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9268331 | pubmed:pagination | 21956-63 | lld:pubmed |
| pubmed-article:9268331 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9268331 | pubmed:meshHeading | pubmed-meshheading:9268331-... | lld:pubmed |
| pubmed-article:9268331 | pubmed:meshHeading | pubmed-meshheading:9268331-... | lld:pubmed |
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| pubmed-article:9268331 | pubmed:meshHeading | pubmed-meshheading:9268331-... | lld:pubmed |
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| pubmed-article:9268331 | pubmed:meshHeading | pubmed-meshheading:9268331-... | lld:pubmed |
| pubmed-article:9268331 | pubmed:meshHeading | pubmed-meshheading:9268331-... | lld:pubmed |
| pubmed-article:9268331 | pubmed:meshHeading | pubmed-meshheading:9268331-... | lld:pubmed |
| pubmed-article:9268331 | pubmed:meshHeading | pubmed-meshheading:9268331-... | lld:pubmed |
| pubmed-article:9268331 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9268331 | pubmed:articleTitle | Role of domains in Escherichia coli and mammalian mitochondrial elongation factor Ts in the interaction with elongation factor Tu. | lld:pubmed |
| pubmed-article:9268331 | pubmed:affiliation | Department of Chemistry and Lineberger Comprehensive Cancer Research Center, University of North Carolina, Chapel Hill, North Carolina 27599-3290, USA. | lld:pubmed |
| pubmed-article:9268331 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9268331 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:944866 | entrezgene:pubmed | pubmed-article:9268331 | lld:entrezgene |
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