pubmed-article:2838728 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2838728 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:2838728 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:2838728 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:2838728 | lifeskim:mentions | umls-concept:C0022895 | lld:lifeskim |
pubmed-article:2838728 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:2838728 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2838728 | pubmed:dateCreated | 1988-8-11 | lld:pubmed |
pubmed-article:2838728 | pubmed:abstractText | The FNR protein of E. coli is a transcriptional activator required for the expression of genes involved in anaerobic respiratory pathways. Site-directed mutagenesis was used to alter three amino acids in the recognition helix of the putative DNA-binding domain of FNR, with the aim of changing its specificity to that of the cyclic AMP receptor protein (CRP). In the presence of the mutant protein (FNR-215) expression of the lac operon was activated during anaerobiosis and unaffected by glucose. FNR-215 did not have a uniform effect on the expression of other cAMP-CRP-dependent genes, but the results demonstrate the fundamental similarity between FNR- and CRP-mediated transcriptional activation. | lld:pubmed |
pubmed-article:2838728 | pubmed:language | eng | lld:pubmed |
pubmed-article:2838728 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2838728 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2838728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2838728 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2838728 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2838728 | pubmed:month | Jul | lld:pubmed |
pubmed-article:2838728 | pubmed:issn | 0950-382X | lld:pubmed |
pubmed-article:2838728 | pubmed:author | pubmed-author:GuestJ RJR | lld:pubmed |
pubmed-article:2838728 | pubmed:author | pubmed-author:SpiroSS | lld:pubmed |
pubmed-article:2838728 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2838728 | pubmed:volume | 1 | lld:pubmed |
pubmed-article:2838728 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2838728 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2838728 | pubmed:pagination | 53-8 | lld:pubmed |
pubmed-article:2838728 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:2838728 | pubmed:meshHeading | pubmed-meshheading:2838728-... | lld:pubmed |
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pubmed-article:2838728 | pubmed:meshHeading | pubmed-meshheading:2838728-... | lld:pubmed |
pubmed-article:2838728 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:2838728 | pubmed:articleTitle | Activation of the lac operon of Escherichia coli by a mutant FNR protein. | lld:pubmed |
pubmed-article:2838728 | pubmed:affiliation | Department of Microbiology, University of Sheffield, UK. | lld:pubmed |
pubmed-article:2838728 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2838728 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:945908 | entrezgene:pubmed | pubmed-article:2838728 | lld:entrezgene |
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