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dc.creatorGonzález-Díaz, Wendy
dc.creatorValdebenito, Braulio
dc.creatorCaballero, Julio
dc.creatorRiadi, Gonzalo
dc.creatorRiedelsberger, Janin
dc.creatorMartínez, Gonzalo
dc.creatorRamírez, David
dc.creatorZúñiga, Leandro
dc.creatorSepulveda, Francisco V
dc.creatorDreyer, Ingo
dc.creatorJanta, Michael
dc.creatorBecker, Dirk
dc.date.accessioned2018-11-29T15:36:01Z
dc.date.available2018-11-29T15:36:01Z
dc.date.issued2015
dc.identifier.urihttp://hdl.handle.net/10533/228052
dc.description.abstractTwo-pore domain potassium (K-2P) channels are membrane proteins widely identified in mammals, plants, and other organisms. A functional channel is a dimer with each subunit comprising two pore-forming loops and four transmembrane domains. The genome of t
dc.language.isoeng
dc.relation.urihttps://link.springer.com/content/pdf/10.1007%2Fs00424-014-1638-4.pdf
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 Chile
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.titleK2p channels in plants and animals
dc.typeArticulo
dc.description.conicytinstrumentRegular
dc.identifier.folio1140624
dc.description.conicytprogramFONDECYT
dc.relation.contesthandle/10533/111556
dc.rights.driverinfo:eu-repo/semantics/openAccess
dc.title.journalPflügers Archiv - European Journal of Physiology
dc.type.driverinfo:eu-repo/semantics/article
dc.relation.instrumenthandle/10533/111541
dc.relation.programhandle/10533/108045
dc.description.shortconicytprogramFONDECYT
dc.date.annoconcurso2014
dc.type.openaireinfo:eu-repo/semantics/publishedVersion


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