pubmed-article:15070344 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15070344 | lifeskim:mentions | umls-concept:C0030054 | lld:lifeskim |
pubmed-article:15070344 | lifeskim:mentions | umls-concept:C0599874 | lld:lifeskim |
pubmed-article:15070344 | lifeskim:mentions | umls-concept:C1417196 | lld:lifeskim |
pubmed-article:15070344 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
pubmed-article:15070344 | lifeskim:mentions | umls-concept:C0244104 | lld:lifeskim |
pubmed-article:15070344 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
pubmed-article:15070344 | lifeskim:mentions | umls-concept:C1707520 | lld:lifeskim |
pubmed-article:15070344 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:15070344 | lifeskim:mentions | umls-concept:C2346592 | lld:lifeskim |
pubmed-article:15070344 | pubmed:issue | 14 | lld:pubmed |
pubmed-article:15070344 | pubmed:dateCreated | 2004-4-8 | lld:pubmed |
pubmed-article:15070344 | pubmed:abstractText | (4-Hydroxyphenyl)pyruvate dioxygenase (HPPD) is an unusual alpha-keto acid-dependent non-heme iron dioxygenase as it incorporates both atoms of dioxygen into a single substrate, paralleling the extradiol dioxygenases. CD/MCD studies of the catalytically active ferrous site and its interaction with substrate reveal a geometic and electronic structure and mechanistic approach to oxygen activation which bridges those of the alpha-KG-dependent and the extradiol dioxygenases. | lld:pubmed |
pubmed-article:15070344 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15070344 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15070344 | pubmed:language | eng | lld:pubmed |
pubmed-article:15070344 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15070344 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15070344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15070344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:15070344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15070344 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15070344 | pubmed:month | Apr | lld:pubmed |
pubmed-article:15070344 | pubmed:issn | 0002-7863 | lld:pubmed |
pubmed-article:15070344 | pubmed:author | pubmed-author:SolomonEdward... | lld:pubmed |
pubmed-article:15070344 | pubmed:author | pubmed-author:MoranGraham... | lld:pubmed |
pubmed-article:15070344 | pubmed:author | pubmed-author:KavanaMichael... | lld:pubmed |
pubmed-article:15070344 | pubmed:author | pubmed-author:NeidigMichael... | lld:pubmed |
pubmed-article:15070344 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15070344 | pubmed:day | 14 | lld:pubmed |
pubmed-article:15070344 | pubmed:volume | 126 | lld:pubmed |
pubmed-article:15070344 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15070344 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15070344 | pubmed:pagination | 4486-7 | lld:pubmed |
pubmed-article:15070344 | pubmed:dateRevised | 2008-1-17 | lld:pubmed |
pubmed-article:15070344 | pubmed:meshHeading | pubmed-meshheading:15070344... | lld:pubmed |
pubmed-article:15070344 | pubmed:meshHeading | pubmed-meshheading:15070344... | lld:pubmed |
pubmed-article:15070344 | pubmed:meshHeading | pubmed-meshheading:15070344... | lld:pubmed |
pubmed-article:15070344 | pubmed:meshHeading | pubmed-meshheading:15070344... | lld:pubmed |
pubmed-article:15070344 | pubmed:meshHeading | pubmed-meshheading:15070344... | lld:pubmed |
pubmed-article:15070344 | pubmed:meshHeading | pubmed-meshheading:15070344... | lld:pubmed |
pubmed-article:15070344 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15070344 | pubmed:articleTitle | CD and MCD studies of the non-heme ferrous active site in (4-hydroxyphenyl)pyruvate dioxygenase: correlation between oxygen activation in the extradiol and alpha-KG-dependent dioxygenases. | lld:pubmed |
pubmed-article:15070344 | pubmed:affiliation | Department of Chemistry, Stanford University, Stanford, California 94305, USA. | lld:pubmed |
pubmed-article:15070344 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15070344 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:15070344 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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