| pubmed-article:17428662 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17428662 | lifeskim:mentions | umls-concept:C0020205 | lld:lifeskim |
| pubmed-article:17428662 | lifeskim:mentions | umls-concept:C0040018 | lld:lifeskim |
| pubmed-article:17428662 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
| pubmed-article:17428662 | lifeskim:mentions | umls-concept:C1518610 | lld:lifeskim |
| pubmed-article:17428662 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:17428662 | pubmed:dateCreated | 2007-6-4 | lld:pubmed |
| pubmed-article:17428662 | pubmed:abstractText | Based on X-ray crystallographic data of complexes of chlorodysinosin A with the enzyme thrombin, a series of analogs were synthesized varying the nature of the P(1), P(2), and P(3) pharmacophoric sites and the central octahydroindole carboxyamide core. In general, introduction of a hydrophobic substituent on the d-leucine amide residue dramatically improved the inhibition of the enzyme. This is rationalized based on a better fit of the P(3) subunit in the hydrophobic S(3) enzyme site. Single digit nanomolar inhibition expressed as IC(50) was observed for several analogs. | lld:pubmed |
| pubmed-article:17428662 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17428662 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17428662 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17428662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17428662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17428662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17428662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17428662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17428662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17428662 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17428662 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:17428662 | pubmed:issn | 0960-894X | lld:pubmed |
| pubmed-article:17428662 | pubmed:author | pubmed-author:HanessianStep... | lld:pubmed |
| pubmed-article:17428662 | pubmed:author | pubmed-author:XueYafengY | lld:pubmed |
| pubmed-article:17428662 | pubmed:author | pubmed-author:Del... | lld:pubmed |
| pubmed-article:17428662 | pubmed:author | pubmed-author:ErsmarkKaroli... | lld:pubmed |
| pubmed-article:17428662 | pubmed:author | pubmed-author:FjellströmOla... | lld:pubmed |
| pubmed-article:17428662 | pubmed:author | pubmed-author:BlombergNikla... | lld:pubmed |
| pubmed-article:17428662 | pubmed:author | pubmed-author:WangXiaotianX | lld:pubmed |
| pubmed-article:17428662 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17428662 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:17428662 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:17428662 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17428662 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17428662 | pubmed:pagination | 3480-5 | lld:pubmed |
| pubmed-article:17428662 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:meshHeading | pubmed-meshheading:17428662... | lld:pubmed |
| pubmed-article:17428662 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17428662 | pubmed:articleTitle | Structure-based organic synthesis of unnatural aeruginosin hybrids as potent inhibitors of thrombin. | lld:pubmed |
| pubmed-article:17428662 | pubmed:affiliation | Department of Chemistry, Université de Montréal, PO Box 6128, Station, Centre-Ville, Montréal, QC, Canada H3C 3J7. Stephen.hanessian@umontreal.ca | lld:pubmed |
| pubmed-article:17428662 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17428662 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:17428662 | lld:chembl |
