| pubmed-article:11738048 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11738048 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:11738048 | lifeskim:mentions | umls-concept:C0035693 | lld:lifeskim |
| pubmed-article:11738048 | lifeskim:mentions | umls-concept:C0073240 | lld:lifeskim |
| pubmed-article:11738048 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:11738048 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:11738048 | lifeskim:mentions | umls-concept:C0870071 | lld:lifeskim |
| pubmed-article:11738048 | lifeskim:mentions | umls-concept:C1705535 | lld:lifeskim |
| pubmed-article:11738048 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:11738048 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:11738048 | pubmed:dateCreated | 2001-12-13 | lld:pubmed |
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| pubmed-article:11738048 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11738048 | pubmed:abstractText | Aquifex aeolicus Ribonuclease III (Aa-RNase III) belongs to the family of Mg(2+)-dependent endonucleases that show specificity for double-stranded RNA (dsRNA). RNase III is conserved in all known bacteria and eukaryotes and has 1-2 copies of a 9-residue consensus sequence, known as the RNase III signature motif. The bacterial RNase III proteins are the simplest, consisting of two domains: an N-terminal endonuclease domain, followed by a double-stranded RNA binding domain (dsRBD). The three-dimensional structure of the dsRBD in Escherichia coli RNase III has been elucidated; no structural information is available for the endonuclease domain of any RNase III. | lld:pubmed |
| pubmed-article:11738048 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11738048 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11738048 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11738048 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11738048 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:11738048 | pubmed:author | pubmed-author:CourtD LDL | lld:pubmed |
| pubmed-article:11738048 | pubmed:author | pubmed-author:TaoX MXM | lld:pubmed |
| pubmed-article:11738048 | pubmed:author | pubmed-author:WaughD SDS | lld:pubmed |
| pubmed-article:11738048 | pubmed:author | pubmed-author:TropeaJ EJE | lld:pubmed |
| pubmed-article:11738048 | pubmed:author | pubmed-author:BlaszczykJJ | lld:pubmed |
| pubmed-article:11738048 | pubmed:author | pubmed-author:BubunenkoMM | lld:pubmed |
| pubmed-article:11738048 | pubmed:author | pubmed-author:RoutzahnK MKM | lld:pubmed |
| pubmed-article:11738048 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11738048 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:11738048 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11738048 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11738048 | pubmed:pagination | 1225-36 | lld:pubmed |
| pubmed-article:11738048 | pubmed:dateRevised | 2005-12-26 | lld:pubmed |
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| pubmed-article:11738048 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11738048 | pubmed:articleTitle | Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage. | lld:pubmed |
| pubmed-article:11738048 | pubmed:affiliation | Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA. | lld:pubmed |
| pubmed-article:11738048 | pubmed:publicationType | Journal Article | lld:pubmed |
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