| pubmed-article:12668014 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12668014 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:12668014 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:12668014 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:12668014 | lifeskim:mentions | umls-concept:C0064557 | lld:lifeskim |
| pubmed-article:12668014 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:12668014 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
| pubmed-article:12668014 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
| pubmed-article:12668014 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:12668014 | pubmed:dateCreated | 2003-4-1 | lld:pubmed |
| pubmed-article:12668014 | pubmed:abstractText | The program GRID was used to design potential inhibitors of human L-xylulose reductase based on a model of the holoenzyme in complex with n-butyric acid. The inclusion of phosphate or carboxylate functional groups in the ligand suggested an increase in the net binding energy of the complex up to 2.8- and 4.0-fold, respectively. This study may be useful in the development of potent and specific inhibitors of the enzyme. | lld:pubmed |
| pubmed-article:12668014 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12668014 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12668014 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12668014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12668014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12668014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12668014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12668014 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12668014 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12668014 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12668014 | pubmed:issn | 0960-894X | lld:pubmed |
| pubmed-article:12668014 | pubmed:author | pubmed-author:El-KabbaniOss... | lld:pubmed |
| pubmed-article:12668014 | pubmed:author | pubmed-author:HaraAkiraA | lld:pubmed |
| pubmed-article:12668014 | pubmed:author | pubmed-author:CarboneVincen... | lld:pubmed |
| pubmed-article:12668014 | pubmed:author | pubmed-author:IshikuraShuhe... | lld:pubmed |
| pubmed-article:12668014 | pubmed:author | pubmed-author:DarmaninConni... | lld:pubmed |
| pubmed-article:12668014 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12668014 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:12668014 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:12668014 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12668014 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12668014 | pubmed:pagination | 1469-74 | lld:pubmed |
| pubmed-article:12668014 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:meshHeading | pubmed-meshheading:12668014... | lld:pubmed |
| pubmed-article:12668014 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12668014 | pubmed:articleTitle | Structure-based design of inhibitors of human L-xylulose reductase modelled into the active site of the enzyme. | lld:pubmed |
| pubmed-article:12668014 | pubmed:affiliation | Department of Medicinal Chemistry, Victorian College of Pharmacy, Monash University, 381 Royal Parade, Parkville, Victoria 3052, Australia. | lld:pubmed |
| pubmed-article:12668014 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:12668014 | lld:chembl |
