Pub. Date : 2020 Dec 31
PMID : 33382027
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The crystal structure of galantamine bound human acetylcholinesterase (hAChE) has been reported; however, the inhibition mechanism of hAChE by galantamine is not well understood. | Galantamine | acetylcholinesterase (Cartwright blood group) | Homo sapiens |
| 2 | The crystal structure of galantamine bound human acetylcholinesterase (hAChE) has been reported; however, the inhibition mechanism of hAChE by galantamine is not well understood. | Galantamine | acetylcholinesterase (Cartwright blood group) | Homo sapiens |
| 3 | The crystal structure of galantamine bound human acetylcholinesterase (hAChE) has been reported; however, the inhibition mechanism of hAChE by galantamine is not well understood. | Galantamine | acetylcholinesterase (Cartwright blood group) | Homo sapiens |
| 4 | The crystal structure of galantamine bound human acetylcholinesterase (hAChE) has been reported; however, the inhibition mechanism of hAChE by galantamine is not well understood. | Galantamine | acetylcholinesterase (Cartwright blood group) | Homo sapiens |
| 5 | A Well-tempered metadynamics (WTMtD) simulation study has been performed with the crystal structure of galantamine bound hAChE. | Galantamine | acetylcholinesterase (Cartwright blood group) | Homo sapiens |
| 6 | Such proton transfer process is lowered in the presence of galantamine due to the separation of catalytic triad inside the gorge of AChE as observed with WTMtD. | Galantamine | acetylcholinesterase (Cartwright blood group) | Homo sapiens |
| 7 | A docking study has been performed to examine the ACh"s binding with the catalytic triad of galantamine bound hAChE. | Galantamine | acetylcholinesterase (Cartwright blood group) | Homo sapiens |