| pubmed-article:19636838 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19636838 | lifeskim:mentions | umls-concept:C0025552 | lld:lifeskim |
| pubmed-article:19636838 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:19636838 | lifeskim:mentions | umls-concept:C0231881 | lld:lifeskim |
| pubmed-article:19636838 | lifeskim:mentions | umls-concept:C0183210 | lld:lifeskim |
| pubmed-article:19636838 | lifeskim:mentions | umls-concept:C1516050 | lld:lifeskim |
| pubmed-article:19636838 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19636838 | pubmed:dateCreated | 2009-7-28 | lld:pubmed |
| pubmed-article:19636838 | pubmed:abstractText | Zn/Co binding to homodimeric CzrA de-represses transcription of the czr (cobalt zinc resistance) operon in Staphylococcus aureus. Essentially complete backbone and stereospecific methyl group resonance assignments for apo-, Zn2 and a 42 kDa apo-CzrA-DNA complex are presented. | lld:pubmed |
| pubmed-article:19636838 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19636838 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19636838 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19636838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19636838 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19636838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19636838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19636838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19636838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19636838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19636838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19636838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19636838 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19636838 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:19636838 | pubmed:issn | 1874-270X | lld:pubmed |
| pubmed-article:19636838 | pubmed:author | pubmed-author:GiedrocDavid... | lld:pubmed |
| pubmed-article:19636838 | pubmed:author | pubmed-author:ArunkumarAlph... | lld:pubmed |
| pubmed-article:19636838 | pubmed:author | pubmed-author:PennellaMario... | lld:pubmed |
| pubmed-article:19636838 | pubmed:author | pubmed-author:KongXiangming... | lld:pubmed |
| pubmed-article:19636838 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19636838 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:19636838 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19636838 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19636838 | pubmed:pagination | 99-101 | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:meshHeading | pubmed-meshheading:19636838... | lld:pubmed |
| pubmed-article:19636838 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:19636838 | pubmed:articleTitle | Resonance assignments of the metal sensor CzrA in the apo-, Zn2- and DNA-bound (42 kDa) states. | lld:pubmed |
| pubmed-article:19636838 | pubmed:affiliation | Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA. | lld:pubmed |
| pubmed-article:19636838 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19636838 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:19636838 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19636838 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19636838 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19636838 | lld:pubmed |
