| pubmed-article:8126718 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8126718 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:8126718 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
| pubmed-article:8126718 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8126718 | lifeskim:mentions | umls-concept:C0332462 | lld:lifeskim |
| pubmed-article:8126718 | lifeskim:mentions | umls-concept:C0205214 | lld:lifeskim |
| pubmed-article:8126718 | lifeskim:mentions | umls-concept:C1550535 | lld:lifeskim |
| pubmed-article:8126718 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8126718 | pubmed:dateCreated | 1994-4-8 | lld:pubmed |
| pubmed-article:8126718 | pubmed:abstractText | A systematic screening of sequence databases with a motif hitherto found only in animal and poxvirus proteins has revealed a trail leading back to prokaryotes. Fortuitously, an X-ray structure is available for one of the identified sequences and shows the fundamental fold to be a set of circularly arranged beta sheets. This structure may be very widely distributed throughout the biological world in sialidases and some other enzymes. In bacteria, a mobile noncatalytic domain is often associated with these same enzymes. | lld:pubmed |
| pubmed-article:8126718 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8126718 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8126718 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8126718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8126718 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8126718 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8126718 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8126718 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:8126718 | pubmed:author | pubmed-author:DoolittleR... | lld:pubmed |
| pubmed-article:8126718 | pubmed:author | pubmed-author:BorgTT | lld:pubmed |
| pubmed-article:8126718 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8126718 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:8126718 | pubmed:volume | 236 | lld:pubmed |
| pubmed-article:8126718 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8126718 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8126718 | pubmed:pagination | 1277-82 | lld:pubmed |
| pubmed-article:8126718 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:8126718 | pubmed:meshHeading | pubmed-meshheading:8126718-... | lld:pubmed |
| pubmed-article:8126718 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:8126718 | pubmed:articleTitle | Drosophila kelch motif is derived from a common enzyme fold. | lld:pubmed |
| pubmed-article:8126718 | pubmed:affiliation | European Molecular Biological Laboratory, Heidelberg, Germany. | lld:pubmed |
| pubmed-article:8126718 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8126718 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8126718 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8126718 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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