| pubmed-article:15959931 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15959931 | lifeskim:mentions | umls-concept:C0002062 | lld:lifeskim |
| pubmed-article:15959931 | lifeskim:mentions | umls-concept:C0001044 | lld:lifeskim |
| pubmed-article:15959931 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:15959931 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:15959931 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15959931 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:15959931 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:15959931 | pubmed:dateCreated | 2005-6-15 | lld:pubmed |
| pubmed-article:15959931 | pubmed:abstractText | Acetylcholinesterase plays a crucial role in the metabolism of neurotransmitter, acetylcholine. Inhibition of Torpedo californica acetylcholinesterase by triterpenoidal alkaloids buxamine-B (1) and buxamine-C (2) has been studied by enzyme kinetics and molecular docking experiments. Buxamine-C (2) has been found to be 20-fold potent than buxamine-B (1) (Ki = 5.5 and 110 microM, respectively). The ligand docking experiments predicted that the cyclopentanophenanthrene skeleton of both inhibitors properly fits into the aromatic gorge of the enzyme. The C-3 and C-20 amino groups of both alkaloids mimic the well-known bis-quaternary ammonium inhibitors such as decamethonium and interact with Trp84 and Trp279 residues of the enzyme, respectively. The C-3 amino group in buxamine-C (2) appears to be better positioned at the bottom of the aromatic gorge and thus seems to be crucial for the inhibitory activity of such inhibitors. | lld:pubmed |
| pubmed-article:15959931 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15959931 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15959931 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15959931 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15959931 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15959931 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15959931 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15959931 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15959931 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15959931 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:15959931 | pubmed:author | pubmed-author:Atta-ur-Rahma... | lld:pubmed |
| pubmed-article:15959931 | pubmed:author | pubmed-author:KhalidAsaadA | lld:pubmed |
| pubmed-article:15959931 | pubmed:author | pubmed-author:ChoudharyM... | lld:pubmed |
| pubmed-article:15959931 | pubmed:author | pubmed-author:AzimM... | lld:pubmed |
| pubmed-article:15959931 | pubmed:author | pubmed-author:ParveenShehna... | lld:pubmed |
| pubmed-article:15959931 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15959931 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:15959931 | pubmed:volume | 331 | lld:pubmed |
| pubmed-article:15959931 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15959931 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15959931 | pubmed:pagination | 1528-32 | lld:pubmed |
| pubmed-article:15959931 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15959931 | pubmed:meshHeading | pubmed-meshheading:15959931... | lld:pubmed |
| pubmed-article:15959931 | pubmed:meshHeading | pubmed-meshheading:15959931... | lld:pubmed |
| pubmed-article:15959931 | pubmed:meshHeading | pubmed-meshheading:15959931... | lld:pubmed |
| pubmed-article:15959931 | pubmed:meshHeading | pubmed-meshheading:15959931... | lld:pubmed |
| pubmed-article:15959931 | pubmed:meshHeading | pubmed-meshheading:15959931... | lld:pubmed |
| pubmed-article:15959931 | pubmed:meshHeading | pubmed-meshheading:15959931... | lld:pubmed |
| pubmed-article:15959931 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15959931 | pubmed:articleTitle | Structural basis of acetylcholinesterase inhibition by triterpenoidal alkaloids. | lld:pubmed |
| pubmed-article:15959931 | pubmed:affiliation | Dr. Panjwani Center for Molecular Medicine and Drug Research, International Center for Chemical Sciences, University of Karachi, Pakistan. | lld:pubmed |
| pubmed-article:15959931 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15959931 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
