| pubmed-article:10535945 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:10535945 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:10535945 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:10535945 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:10535945 | lifeskim:mentions | umls-concept:C0162782 | lld:lifeskim |
| pubmed-article:10535945 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:10535945 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10535945 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:10535945 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:10535945 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:10535945 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:10535945 | pubmed:dateCreated | 1999-12-10 | lld:pubmed |
| pubmed-article:10535945 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10535945 | pubmed:abstractText | Double-stranded RNA deaminase I (ADAR1) contains the Z-DNA binding domain Zalpha. Here we report the solution structure of free Zalpha and map the interaction surface with Z-DNA, confirming roles previously assigned to residues by mutagenesis. Comparison with the crystal structure of the (Zalpha)(2)/Z-DNA complex shows that most Z-DNA contacting residues in free Zalpha are prepositioned to bind Z-DNA, thus minimizing the entropic cost of binding. Comparison with homologous (alpha+beta)helix-turn-helix/B-DNA complexes suggests that binding of Zalpha to B-DNA is disfavored by steric hindrance, but does not eliminate the possibility that related domains may bind to both B- and Z-DNA. | lld:pubmed |
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| pubmed-article:10535945 | pubmed:keyword | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10535945 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10535945 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10535945 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10535945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10535945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10535945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10535945 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10535945 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:10535945 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10535945 | pubmed:author | pubmed-author:TurnerC JCJ | lld:pubmed |
| pubmed-article:10535945 | pubmed:author | pubmed-author:RichAA | lld:pubmed |
| pubmed-article:10535945 | pubmed:author | pubmed-author:HerbertAA | lld:pubmed |
| pubmed-article:10535945 | pubmed:author | pubmed-author:LowenhauptKK | lld:pubmed |
| pubmed-article:10535945 | pubmed:author | pubmed-author:SchadeMM | lld:pubmed |
| pubmed-article:10535945 | pubmed:author | pubmed-author:KühneRR | lld:pubmed |
| pubmed-article:10535945 | pubmed:author | pubmed-author:SchmiederPP | lld:pubmed |
| pubmed-article:10535945 | pubmed:author | pubmed-author:OschkinatHH | lld:pubmed |
| pubmed-article:10535945 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10535945 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:10535945 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:10535945 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10535945 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10535945 | pubmed:pagination | 12465-70 | lld:pubmed |
| pubmed-article:10535945 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10535945 | pubmed:meshHeading | pubmed-meshheading:10535945... | lld:pubmed |
| pubmed-article:10535945 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10535945 | pubmed:articleTitle | The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA. | lld:pubmed |
| pubmed-article:10535945 | pubmed:affiliation | Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. | lld:pubmed |
| pubmed-article:10535945 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10535945 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10535945 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:10535945 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:103 | entrezgene:pubmed | pubmed-article:10535945 | lld:entrezgene |
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