| pubmed-article:3413113 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3413113 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:3413113 | lifeskim:mentions | umls-concept:C0424972 | lld:lifeskim |
| pubmed-article:3413113 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:3413113 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:3413113 | pubmed:dateCreated | 1988-10-13 | lld:pubmed |
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| pubmed-article:3413113 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3413113 | pubmed:abstractText | At least nine different bacterial proteins belong to the LysR family. The gene sequence for one of these proteins is presented here. Six others (Escherichia coli LysR, IlvY, CysB; Salmonella typhimurium MetR; Rhizobium NodD; and Enterobacter cloacae AmpR) are known to activate other genes. Based on sequence alignments, each member of this family is predicted to have a helix-turn-helix DNA binding motif near its amino terminus. The combined evidence indicates that all nine proteins are related by common ancestry, are similarly folded, and are not detectably related to other known bacterial regulatory proteins. The DNA database searching procedure and other methods used in this study should be useful in detecting other groups of related proteins. | lld:pubmed |
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| pubmed-article:3413113 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3413113 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3413113 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3413113 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3413113 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:3413113 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:3413113 | pubmed:author | pubmed-author:CalvoJ MJM | lld:pubmed |
| pubmed-article:3413113 | pubmed:author | pubmed-author:WallaceJ CJC | lld:pubmed |
| pubmed-article:3413113 | pubmed:author | pubmed-author:HenikoffSS | lld:pubmed |
| pubmed-article:3413113 | pubmed:author | pubmed-author:HaughnG WGW | lld:pubmed |
| pubmed-article:3413113 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3413113 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:3413113 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3413113 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3413113 | pubmed:pagination | 6602-6 | lld:pubmed |
| pubmed-article:3413113 | pubmed:dateRevised | 2010-9-9 | lld:pubmed |
| pubmed-article:3413113 | pubmed:meshHeading | pubmed-meshheading:3413113-... | lld:pubmed |
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| pubmed-article:3413113 | pubmed:meshHeading | pubmed-meshheading:3413113-... | lld:pubmed |
| pubmed-article:3413113 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3413113 | pubmed:articleTitle | A large family of bacterial activator proteins. | lld:pubmed |
| pubmed-article:3413113 | pubmed:affiliation | Fred Hutchinson Cancer Research Center, Seattle, WA 98104. | lld:pubmed |
| pubmed-article:3413113 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3413113 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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