| pubmed-article:16026786 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16026786 | lifeskim:mentions | umls-concept:C0026926 | lld:lifeskim |
| pubmed-article:16026786 | lifeskim:mentions | umls-concept:C0332285 | lld:lifeskim |
| pubmed-article:16026786 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:16026786 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:16026786 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:16026786 | pubmed:dateCreated | 2005-7-26 | lld:pubmed |
| pubmed-article:16026786 | pubmed:abstractText | We report the identification of a novel two-component system in Mycobacterium tuberculosis. We show that the putative histidine kinase with the genomic locus tag Rv3220c is able to self-phosphorylate in the presence of Mg2+/ATP and subsequently transfer the phosphoryl group to a novel response regulator PdtaR. This creates a biochemical link between the two proteins and establishes a newly identified two component system, which acts at the level of transcriptional antitermination. We also suggest that this system has potential for the development of lead compounds for inhibition of phosphotransfer. | lld:pubmed |
| pubmed-article:16026786 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16026786 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16026786 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16026786 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16026786 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16026786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16026786 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16026786 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16026786 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16026786 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:16026786 | pubmed:author | pubmed-author:NowakElzbieta... | lld:pubmed |
| pubmed-article:16026786 | pubmed:author | pubmed-author:TuckerPaul... | lld:pubmed |
| pubmed-article:16026786 | pubmed:author | pubmed-author:MorthJ... | lld:pubmed |
| pubmed-article:16026786 | pubmed:author | pubmed-author:GosmannSylviS | lld:pubmed |
| pubmed-article:16026786 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16026786 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:16026786 | pubmed:volume | 579 | lld:pubmed |
| pubmed-article:16026786 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16026786 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16026786 | pubmed:pagination | 4145-8 | lld:pubmed |
| pubmed-article:16026786 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:16026786 | pubmed:meshHeading | pubmed-meshheading:16026786... | lld:pubmed |
| pubmed-article:16026786 | pubmed:meshHeading | pubmed-meshheading:16026786... | lld:pubmed |
| pubmed-article:16026786 | pubmed:meshHeading | pubmed-meshheading:16026786... | lld:pubmed |
| pubmed-article:16026786 | pubmed:meshHeading | pubmed-meshheading:16026786... | lld:pubmed |
| pubmed-article:16026786 | pubmed:meshHeading | pubmed-meshheading:16026786... | lld:pubmed |
| pubmed-article:16026786 | pubmed:meshHeading | pubmed-meshheading:16026786... | lld:pubmed |
| pubmed-article:16026786 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16026786 | pubmed:articleTitle | A novel two-component system found in Mycobacterium tuberculosis. | lld:pubmed |
| pubmed-article:16026786 | pubmed:affiliation | European Molecular Biology Laboratory (EMBL) Hamburg, Notkestrasse 85, 22603 Hamburg, Germany. | lld:pubmed |
| pubmed-article:16026786 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16026786 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16026786 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16026786 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
