| pubmed-article:8416811 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8416811 | lifeskim:mentions | umls-concept:C1336789 | lld:lifeskim |
| pubmed-article:8416811 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
| pubmed-article:8416811 | lifeskim:mentions | umls-concept:C1441547 | lld:lifeskim |
| pubmed-article:8416811 | lifeskim:mentions | umls-concept:C0205296 | lld:lifeskim |
| pubmed-article:8416811 | lifeskim:mentions | umls-concept:C2004457 | lld:lifeskim |
| pubmed-article:8416811 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:8416811 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8416811 | pubmed:dateCreated | 1993-1-27 | lld:pubmed |
| pubmed-article:8416811 | pubmed:abstractText | Bacteriophage 434 repressor recognizes the operator sequences ACAAG and ACAAT. As the same or similar sequences occur in the enhancer region of HIV-1, 434 repressor was a potential HIV enhancer-binding protein. We found that the interaction of the DNA-binding domain of 434 repressor with a 57-bp HIV enhancer DNA was very weak whereas a 42-residue construct, comprising the recognition helix and four copies of a positively charged segment of the repressor, bound strongly. The results of footprint and cell-free in vitro transcription studies showed that the 42-residue peptide bound preferably to the enhancer region of HIV-1 and acted as an artificial repressor. Replacement of an essential glutamine of the recognition helix by glutamic acid resulted in a partial shift of the sequence specificity of the 42-residue peptide. | lld:pubmed |
| pubmed-article:8416811 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8416811 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8416811 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8416811 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8416811 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8416811 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8416811 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8416811 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8416811 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8416811 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8416811 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8416811 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8416811 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:8416811 | pubmed:author | pubmed-author:SalgamPP | lld:pubmed |
| pubmed-article:8416811 | pubmed:author | pubmed-author:GutteBB | lld:pubmed |
| pubmed-article:8416811 | pubmed:author | pubmed-author:LeiserAA | lld:pubmed |
| pubmed-article:8416811 | pubmed:author | pubmed-author:StoltGG | lld:pubmed |
| pubmed-article:8416811 | pubmed:author | pubmed-author:KlauserSS | lld:pubmed |
| pubmed-article:8416811 | pubmed:author | pubmed-author:CuiTT | lld:pubmed |
| pubmed-article:8416811 | pubmed:author | pubmed-author:WidmannMM | lld:pubmed |
| pubmed-article:8416811 | pubmed:author | pubmed-author:HehlgansTT | lld:pubmed |
| pubmed-article:8416811 | pubmed:author | pubmed-author:VercaS BSB | lld:pubmed |
| pubmed-article:8416811 | pubmed:author | pubmed-author:StädlerKK | lld:pubmed |
| pubmed-article:8416811 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8416811 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:8416811 | pubmed:volume | 315 | lld:pubmed |
| pubmed-article:8416811 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8416811 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8416811 | pubmed:pagination | 51-5 | lld:pubmed |
| pubmed-article:8416811 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:8416811 | pubmed:meshHeading | pubmed-meshheading:8416811-... | lld:pubmed |
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| pubmed-article:8416811 | pubmed:meshHeading | pubmed-meshheading:8416811-... | lld:pubmed |
| pubmed-article:8416811 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8416811 | pubmed:articleTitle | The DNA-binding properties of an artificial 42-residue polypeptide derived from a natural repressor. | lld:pubmed |
| pubmed-article:8416811 | pubmed:affiliation | Biochemisches Institut, Universität Zürich, Switzerland. | lld:pubmed |
| pubmed-article:8416811 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8416811 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8416811 | lld:pubmed |
