| dc.date.accessioned | 2019-03-27T15:59:01Z | |
| dc.date.accessioned | 2022-10-18T22:15:30Z | |
| dc.date.available | 2019-03-27T15:59:01Z | |
| dc.date.available | 2022-10-18T22:15:30Z | |
| dc.date.created | 2019-03-27T15:59:01Z | |
| dc.date.issued | 2018 | |
| dc.identifier | http://hdl.handle.net/10533/234692 | |
| dc.identifier | 1140624 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4466049 | |
| dc.description.abstract | Two-‐pore
domain
potassium
(K2P)
channels
underlie
the
background
K+
currents
in
mammalian
cells.
They
can
be
segregated
into
six
subfamilies
based
on
their
structure
and
functional
properties.
The
acid-‐
sensitive
TASK-‐1
and
TASK-‐3
channels
belong | |
| dc.language | eng | |
| dc.relation | 3° | |
| dc.relation | info:eu-repo/grantAgreement/Fondecyt/1140624 | |
| dc.relation | Protein Biophysics at the End of the World | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.title | Understanding the structural mechanism of selective blockers of pH-gated K2P channels | |
| dc.type | Ponencia | |
