| pubmed-article:11709175 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11709175 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:11709175 | lifeskim:mentions | umls-concept:C0038790 | lld:lifeskim |
| pubmed-article:11709175 | lifeskim:mentions | umls-concept:C0039949 | lld:lifeskim |
| pubmed-article:11709175 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:11709175 | lifeskim:mentions | umls-concept:C2697616 | lld:lifeskim |
| pubmed-article:11709175 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
| pubmed-article:11709175 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:11709175 | pubmed:dateCreated | 2001-11-15 | lld:pubmed |
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| pubmed-article:11709175 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11709175 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11709175 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11709175 | pubmed:abstractText | Rhodanese domains are structural modules occurring in the three major evolutionary phyla. They are found as single-domain proteins, as tandemly repeated modules in which the C-terminal domain only bears the properly structured active site, or as members of multidomain proteins. Although in vitro assays show sulfurtransferase or phosphatase activity associated with rhodanese or rhodanese-like domains, specific biological roles for most members of this homology superfamily have not been established. | lld:pubmed |
| pubmed-article:11709175 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11709175 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11709175 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11709175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11709175 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11709175 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11709175 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:11709175 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:11709175 | pubmed:author | pubmed-author:BolognesiMM | lld:pubmed |
| pubmed-article:11709175 | pubmed:author | pubmed-author:LarsonT JTJ | lld:pubmed |
| pubmed-article:11709175 | pubmed:author | pubmed-author:DonahueJ LJL | lld:pubmed |
| pubmed-article:11709175 | pubmed:author | pubmed-author:BordoDD | lld:pubmed |
| pubmed-article:11709175 | pubmed:author | pubmed-author:SpallarossaAA | lld:pubmed |
| pubmed-article:11709175 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11709175 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:11709175 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11709175 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11709175 | pubmed:pagination | 1117-25 | lld:pubmed |
| pubmed-article:11709175 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11709175 | pubmed:meshHeading | pubmed-meshheading:11709175... | lld:pubmed |
| pubmed-article:11709175 | pubmed:meshHeading | pubmed-meshheading:11709175... | lld:pubmed |
| pubmed-article:11709175 | pubmed:meshHeading | pubmed-meshheading:11709175... | lld:pubmed |
| pubmed-article:11709175 | pubmed:meshHeading | pubmed-meshheading:11709175... | lld:pubmed |
| pubmed-article:11709175 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11709175 | pubmed:articleTitle | Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily. | lld:pubmed |
| pubmed-article:11709175 | pubmed:affiliation | Department of Pharmaceutical Sciences, University of Genova, Viale Benedetto XV, 3, 16132, Genova, Italy. | lld:pubmed |
| pubmed-article:11709175 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11709175 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:947935 | entrezgene:pubmed | pubmed-article:11709175 | lld:entrezgene |
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