| pubmed-article:2509184 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2509184 | lifeskim:mentions | umls-concept:C0043335 | lld:lifeskim |
| pubmed-article:2509184 | lifeskim:mentions | umls-concept:C0311400 | lld:lifeskim |
| pubmed-article:2509184 | lifeskim:mentions | umls-concept:C0743223 | lld:lifeskim |
| pubmed-article:2509184 | pubmed:issue | 2-4 | lld:pubmed |
| pubmed-article:2509184 | pubmed:dateCreated | 1989-12-19 | lld:pubmed |
| pubmed-article:2509184 | pubmed:abstractText | UDPGT isoenzymes are products of multiple gene families as demonstrated by sequence analysis of purified proteins and by molecular cloning experiments. These isoenzymes are relatively specific for endogenous substrates but have broad substrate specificities for xenobiotic substrates. They are important metabolic enzymes capable of converting exogenous and endogenous substances to more hydrophilic metabolites. Each species has its own pattern of UDPGTs and it is not possible at this time to extrapolate information directly from one species to another. | lld:pubmed |
| pubmed-article:2509184 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509184 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2509184 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509184 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2509184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509184 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2509184 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2509184 | pubmed:issn | 0360-2532 | lld:pubmed |
| pubmed-article:2509184 | pubmed:author | pubmed-author:TephlyT RTR | lld:pubmed |
| pubmed-article:2509184 | pubmed:author | pubmed-author:GreenM DMD | lld:pubmed |
| pubmed-article:2509184 | pubmed:author | pubmed-author:TownsendMM | lld:pubmed |
| pubmed-article:2509184 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2509184 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:2509184 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2509184 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2509184 | pubmed:pagination | 689-95 | lld:pubmed |
| pubmed-article:2509184 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2509184 | pubmed:meshHeading | pubmed-meshheading:2509184-... | lld:pubmed |
| pubmed-article:2509184 | pubmed:meshHeading | pubmed-meshheading:2509184-... | lld:pubmed |
| pubmed-article:2509184 | pubmed:meshHeading | pubmed-meshheading:2509184-... | lld:pubmed |
| pubmed-article:2509184 | pubmed:meshHeading | pubmed-meshheading:2509184-... | lld:pubmed |
| pubmed-article:2509184 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2509184 | pubmed:articleTitle | UDP-glucuronosyltransferases in the metabolic disposition of xenobiotics. | lld:pubmed |
| pubmed-article:2509184 | pubmed:affiliation | Department of Pharmacology, University of Iowa, Iowa City 52242. | lld:pubmed |
| pubmed-article:2509184 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2509184 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2509184 | pubmed:publicationType | Review | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2509184 | lld:pubmed |
