| Literature DB >> 16250659 |
Helmer Søhoel1, Tommy Liljefors, Steven V Ley, Steven F Oliver, Alessandra Antonello, Martin D Smith, Carl Erik Olsen, John T Isaacs, S Brøgger Christensen.
Abstract
Analysis of molecular interaction fields based on the published crystal structure of thapsigargin bound to the sarco/endoplasmatic reticulum Ca(2+)-ATPase and analysis of the volume and shape of the ligand binding site and of the SERCA-thapsigargin interactions have enabled design of two new compounds inhibiting SERCA in the subpicomolar range. The two inhibitors were synthesized using (S)-carvone as starting material and found to be 3 and 10 times more potent than thapsigargin.Entities:
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Year: 2005 PMID： 16250659 DOI： 10.1021/jm058036v
Source DB: PubMed Journal: J Med Chem ISSN： 0022-2623 Impact factor: 7.446