| Title : Synthesis of alpha-oxycarbanilinophosphonates and their anticholinesterase activities: the most potent derivative is bound to the peripheral site of acetylcholinesterase - Kaboudin_2013_J.Enzyme.Inhib.Med.Chem_28_576 |
| Author(s) : Kaboudin B , Emadi S , Faghihi MR , Fallahi M , Sheikh-Hasani V |
| Ref : J Enzyme Inhib Med Chem , 28 :576 , 2013 |
| Abstract : |
| PubMedSearch : Kaboudin_2013_J.Enzyme.Inhib.Med.Chem_28_576 |
| PubMedID: 22397393 |
| Title : Synthesis of alpha-oxycarbanilinophosphonates and their anticholinesterase activities: the most potent derivative is bound to the peripheral site of acetylcholinesterase - Kaboudin_2013_J.Enzyme.Inhib.Med.Chem_28_576 |
| Author(s) : Kaboudin B , Emadi S , Faghihi MR , Fallahi M , Sheikh-Hasani V |
| Ref : J Enzyme Inhib Med Chem , 28 :576 , 2013 |
| Abstract : |
| PubMedSearch : Kaboudin_2013_J.Enzyme.Inhib.Med.Chem_28_576 |
| PubMedID: 22397393 |
| Title : Synthesis of alpha-oxycarbanilinophosphonates and their anticholinesterase activities: the most potent derivative is bound to the peripheral site of acetylcholinesterase - Kaboudin_2013_J.Enzyme.Inhib.Med.Chem_28_576 |
| Author(s) : Kaboudin B , Emadi S , Faghihi MR , Fallahi M , Sheikh-Hasani V |
| Ref : J Enzyme Inhib Med Chem , 28 :576 , 2013 |
| Abstract : |
| PubMedSearch : Kaboudin_2013_J.Enzyme.Inhib.Med.Chem_28_576 |
| PubMedID: 22397393 |