Calcium Binding And Voltage Gating In Cx46 Hemichannels

The opening of connexin (Cx) hemichannels in the membrane is tightly regulated by calcium (Ca2+) and membrane voltage. Electrophysiological and atomic force microscopy experiments indicate that Ca2+ stabilizes the hemichannel closed state. However, struc

Detalles Bibliográficos
Autores: Pinto, Bernardo I, Pupo, Amaury, Garcia, Isaac E, Mena-Ulecia, Karel, Martinez, Agustin D, Latorre, Ramon, Gonzalez, Carlos
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2015
País:Chile
Idioma:inglés
OAI Identifier:oai:repositorio.anid.cl:10533/231953
Acceso en línea:https://hdl.handle.net/10533/231953
Access Level:acceso abierto
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spelling Gonzalez, CarlosLatorre, RamonMartinez, Agustin DMena-Ulecia, KarelGarcia, Isaac EPupo, AmauryPinto, Bernardo I201710.1038/s41598-017-15975-5https://hdl.handle.net/10533/231953http://purl.org/coar/access_right/c_abf2Calcium Binding And Voltage Gating In Cx46 HemichannelsPinto, Bernardo IPupo, AmauryGarcia, Isaac EMena-Ulecia, KarelMartinez, Agustin DLatorre, RamonGonzalez, Carlos2018-12-07T13:32:39Z2022-07-07T21:31:45Z20152018-12-07T13:32:39Z2022-07-07T21:31:45Z2017The opening of connexin (Cx) hemichannels in the membrane is tightly regulated by calcium (Ca2+) and membrane voltage. Electrophysiological and atomic force microscopy experiments indicate that Ca2+ stabilizes the hemichannel closed state. However, strucRegularFONDECYTFONDECYT11502731150273virtual::33412-1WOS:000415692800023https://hdl.handle.net/10533/231953enghandle/10533/11155710.1038/s41598-017-15975-5handle/10533/111541handle/10533/108045https://www.nature.com/articles/s41598-017-15975-5Atribución-NoComercial-SinDerivadas 3.0 Chilehttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/info:eu-repo/semantics/openAccessCalcium Binding And Voltage Gating In Cx46 HemichannelsScientific ReportsArticuloinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttps://hdl.handle.net/10533/231953FONDECYThttp://purl.org/coar/resource_type/c_2df8fbb1e3aaab85-a139-46a6-9f6a-8827a29a3f15virtual::33412-1e3aaab85-a139-46a6-9f6a-8827a29a3f15virtual::33412-110533/231953oai:repositorio.anid.cl:10533/2319532023-07-24 15:43:39.337https://repositorio.anid.clRepositorio ANIDaletelier@anid.cl
dc.title.none.fl_str_mv Calcium Binding And Voltage Gating In Cx46 Hemichannels
dc.title.journal.none.fl_str_mv Scientific Reports
title Calcium Binding And Voltage Gating In Cx46 Hemichannels
spellingShingle Calcium Binding And Voltage Gating In Cx46 Hemichannels
Pinto, Bernardo I
title_short Calcium Binding And Voltage Gating In Cx46 Hemichannels
title_full Calcium Binding And Voltage Gating In Cx46 Hemichannels
title_fullStr Calcium Binding And Voltage Gating In Cx46 Hemichannels
title_full_unstemmed Calcium Binding And Voltage Gating In Cx46 Hemichannels
title_sort Calcium Binding And Voltage Gating In Cx46 Hemichannels
dc.creator.none.fl_str_mv Pinto, Bernardo I
Pupo, Amaury
Garcia, Isaac E
Mena-Ulecia, Karel
Martinez, Agustin D
Latorre, Ramon
Gonzalez, Carlos
author Pinto, Bernardo I
author_facet Pinto, Bernardo I
Pupo, Amaury
Garcia, Isaac E
Mena-Ulecia, Karel
Martinez, Agustin D
Latorre, Ramon
Gonzalez, Carlos
author_role author
author2 Pupo, Amaury
Garcia, Isaac E
Mena-Ulecia, Karel
Martinez, Agustin D
Latorre, Ramon
Gonzalez, Carlos
author2_role author
author
author
author
author
author
description The opening of connexin (Cx) hemichannels in the membrane is tightly regulated by calcium (Ca2+) and membrane voltage. Electrophysiological and atomic force microscopy experiments indicate that Ca2+ stabilizes the hemichannel closed state. However, struc
publishDate 2015
dc.date.annoconcurso.none.fl_str_mv 2015
dc.date.issued.none.fl_str_mv 2017
dc.date.accessioned.none.fl_str_mv 2018-12-07T13:32:39Z
2022-07-07T21:31:45Z
dc.date.available.none.fl_str_mv 2018-12-07T13:32:39Z
2022-07-07T21:31:45Z
dc.type.none.fl_str_mv Articulo
dc.type.driver.none.fl_str_mv info:eu-repo/semantics/article
dc.type.openaire.none.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.folio.none.fl_str_mv 1150273
1150273
dc.identifier.idwos.none.fl_str_mv WOS:000415692800023
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/10533/231953
identifier_str_mv 1150273
WOS:000415692800023
url https://hdl.handle.net/10533/231953
dc.language.iso.none.fl_str_mv eng
language eng
dc.relation.contest.none.fl_str_mv handle/10533/111557
dc.relation.doi.none.fl_str_mv 10.1038/s41598-017-15975-5
dc.relation.instrument.none.fl_str_mv handle/10533/111541
dc.relation.program.none.fl_str_mv handle/10533/108045
dc.relation.uri.none.fl_str_mv https://www.nature.com/articles/s41598-017-15975-5
dc.rights.none.fl_str_mv Atribución-NoComercial-SinDerivadas 3.0 Chile
http://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rights.driver.none.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv Atribución-NoComercial-SinDerivadas 3.0 Chile
http://creativecommons.org/licenses/by-nc-nd/3.0/cl/
eu_rights_str_mv openAccess
repository.name.fl_str_mv Repositorio ANID
repository.mail.fl_str_mv aletelier@anid.cl
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