| pubmed-article:11914486 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11914486 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:11914486 | lifeskim:mentions | umls-concept:C0002003 | lld:lifeskim |
| pubmed-article:11914486 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:11914486 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:11914486 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11914486 | lifeskim:mentions | umls-concept:C0149322 | lld:lifeskim |
| pubmed-article:11914486 | pubmed:issue | Pt 4 | lld:pubmed |
| pubmed-article:11914486 | pubmed:dateCreated | 2002-3-26 | lld:pubmed |
| pubmed-article:11914486 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914486 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914486 | pubmed:abstractText | The crystal structure of the complex of human recombinant aldose reductase (AR) with zenarestat, one of its potent inhibitors, has been solved at 2.5 A resolution. Zenarestat fits neatly in the hydrophobic active site and induces unique and dramatic conformational changes. For example, the benzene ring of zenarestat occupies a gap in the side chains of Leu300 and Trp111 that interact directly and forms a CH-pi interaction in the native holoenzyme. As a result, the benzene ring of the inhibitor and these side chains form a CH-pi-pi interaction. Such structural information is key to understanding the mode of action of this class of inhibitors and for rational design of better therapeutics. | lld:pubmed |
| pubmed-article:11914486 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11914486 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914486 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11914486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11914486 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11914486 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11914486 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:11914486 | pubmed:author | pubmed-author:KinoshitaTaka... | lld:pubmed |
| pubmed-article:11914486 | pubmed:author | pubmed-author:GotoToshioT | lld:pubmed |
| pubmed-article:11914486 | pubmed:author | pubmed-author:FujiiTakashiT | lld:pubmed |
| pubmed-article:11914486 | pubmed:author | pubmed-author:MiyakeHiroshi... | lld:pubmed |
| pubmed-article:11914486 | pubmed:author | pubmed-author:TakakuraShoji... | lld:pubmed |
| pubmed-article:11914486 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11914486 | pubmed:volume | 58 | lld:pubmed |
| pubmed-article:11914486 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11914486 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11914486 | pubmed:pagination | 622-6 | lld:pubmed |
| pubmed-article:11914486 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
| pubmed-article:11914486 | pubmed:meshHeading | pubmed-meshheading:11914486... | lld:pubmed |
| pubmed-article:11914486 | pubmed:meshHeading | pubmed-meshheading:11914486... | lld:pubmed |
| pubmed-article:11914486 | pubmed:meshHeading | pubmed-meshheading:11914486... | lld:pubmed |
| pubmed-article:11914486 | pubmed:meshHeading | pubmed-meshheading:11914486... | lld:pubmed |
| pubmed-article:11914486 | pubmed:meshHeading | pubmed-meshheading:11914486... | lld:pubmed |
| pubmed-article:11914486 | pubmed:meshHeading | pubmed-meshheading:11914486... | lld:pubmed |
| pubmed-article:11914486 | pubmed:meshHeading | pubmed-meshheading:11914486... | lld:pubmed |
| pubmed-article:11914486 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11914486 | pubmed:articleTitle | The structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat. | lld:pubmed |
| pubmed-article:11914486 | pubmed:affiliation | Exploratory Research Laboratories, Fujisawa Pharmaceutical Co. Ltd, 5-2-3, Tokodai, Tsukuba, Ibaraki 300-2698, Japan. takayoshi_kinoshita@po.fujisawa.co.jp | lld:pubmed |
| pubmed-article:11914486 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11914486 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11914486 | lld:pubmed |
