| pubmed-article:9383408 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9383408 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9383408 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:9383408 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:9383408 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:9383408 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:9383408 | lifeskim:mentions | umls-concept:C0205296 | lld:lifeskim |
| pubmed-article:9383408 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:9383408 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:9383408 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9383408 | pubmed:dateCreated | 1998-1-14 | lld:pubmed |
| pubmed-article:9383408 | pubmed:abstractText | Zinc-finger proteins of the Cys2His2 type constitute an important family of DNA-binding proteins. Each zinc-finger domain has three residues that are thought to be important in determining DNA binding site specificity. Proteins have been designed previously by combining zinc-finger domains with a fixed sequence framework with different DNA-contacting residues. | lld:pubmed |
| pubmed-article:9383408 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9383408 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9383408 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9383408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9383408 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9383408 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9383408 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9383408 | pubmed:issn | 1074-5521 | lld:pubmed |
| pubmed-article:9383408 | pubmed:author | pubmed-author:BergJ MJM | lld:pubmed |
| pubmed-article:9383408 | pubmed:author | pubmed-author:ShiYY | lld:pubmed |
| pubmed-article:9383408 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9383408 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:9383408 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9383408 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9383408 | pubmed:pagination | 83-9 | lld:pubmed |
| pubmed-article:9383408 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9383408 | pubmed:meshHeading | pubmed-meshheading:9383408-... | lld:pubmed |
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| pubmed-article:9383408 | pubmed:meshHeading | pubmed-meshheading:9383408-... | lld:pubmed |
| pubmed-article:9383408 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:9383408 | pubmed:articleTitle | A direct comparison of the properties of natural and designed zinc-finger proteins. | lld:pubmed |
| pubmed-article:9383408 | pubmed:affiliation | Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. | lld:pubmed |
| pubmed-article:9383408 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9383408 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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