| dc.date.accessioned | 2019-03-27T15:58:59Z | |
| dc.date.accessioned | 2022-10-18T22:15:22Z | |
| dc.date.available | 2019-03-27T15:58:59Z | |
| dc.date.available | 2022-10-18T22:15:22Z | |
| dc.date.created | 2019-03-27T15:58:59Z | |
| dc.date.issued | 2016 | |
| dc.identifier | http://hdl.handle.net/10533/234674 | |
| dc.identifier | 1140624 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4466031 | |
| dc.description.abstract | Two-pore domain potassium (K2P) channels trigger the background K+
currents in mammalian cells. K2P channels are separated into six subfamilies
based on their structural and functional properties. The acid-sensitive TASK-1
and TASK-3 channels belong t | |
| dc.language | eng | |
| dc.relation | 3° | |
| dc.relation | info:eu-repo/grantAgreement/Fondecyt/1140624 | |
| dc.relation | Latin American Federation of Biophysical Societies (LAFeBS) | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.title | Structure-based study of TASK channels blockers | |
| dc.type | Ponencia | |
