Výsledky vyhledávání - "Covadonga Malo"

Akademický článek

Redox regulation of KV7 channels through EF3 hand of calmodulin

Autor: Eider Nuñez, Frederick Jones, Arantza Muguruza-Montero, Janire Urrutia, Alejandra Aguado, Covadonga Malo, Ganeko Bernardo-Seisdedos, Carmen Domene, Oscar Millet, Nikita Gamper, Alvaro Villarroel

Publikováno v: eLife, Vol 12 (2023)

Neuronal KV7 channels, important regulators of cell excitability, are among the most sensitive proteins to reactive oxygen species. The S2S3 linker of the voltage sensor was reported as a site-mediating redox modulation of the channels. Recent struct

Externí odkaz: https://doaj.org/article/0bd7d7f107f1445e8d187383cd53a107

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Akademický článek

An epilepsy-causing mutation leads to co-translational misfolding of the Kv7.2 channel

Autor: Janire Urrutia, Alejandra Aguado, Carolina Gomis-Perez, Arantza Muguruza-Montero, Oscar R. Ballesteros, Jiaren Zhang, Eider Nuñez, Covadonga Malo, Hee Jung Chung, Aritz Leonardo, Aitor Bergara, Alvaro Villarroel

Publikováno v: BMC Biology, Vol 19, Iss 1, Pp 1-18 (2021)

Abstract Background The amino acid sequence of proteins generally carries all the necessary information for acquisition of native conformations, but the vectorial nature of translation can additionally determine the folding outcome. Such consideratio

Externí odkaz: https://doaj.org/article/06cb6d34b83948ddbd9c631e4790026c

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Akademický článek

Differential Regulation of PI(4,5)P2 Sensitivity of Kv7.2 and Kv7.3 Channels by Calmodulin

Autor: Alvaro Villarroel, Carolina Gomis-Perez, Maria V. Soldovieri, Covadonga Malo, Paolo Ambrosino, Maurizio Taglialatela, Pilar Areso

Publikováno v: Frontiers in Molecular Neuroscience, Vol 10 (2017)

HIGHLIGHTS- Calmodulin-dependent Kv7.2 current density without the need of binding calcium.- Kv7.2 current density increase is accompanied with resistance to PI(4,5)P2 depletion.- Kv7.3 current density is insensitive to calmodulin elevation.- Kv7.3 i

Externí odkaz: https://doaj.org/article/f109c741dcd64703a5ee752807ae837a

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Akademický článek

Pivoting between calmodulin lobes triggered by calcium in the Kv7.2/calmodulin complex.

Autor: Alessandro Alaimo, Araitz Alberdi, Carolina Gomis-Perez, Juncal Fernández-Orth, Ganeko Bernardo-Seisdedos, Covadonga Malo, Oscar Millet, Pilar Areso, Alvaro Villarroel

Publikováno v: PLoS ONE, Vol 9, Iss 1, p e86711 (2014)

Kv7.2 (KCNQ2) is the principal molecular component of the slow voltage gated M-channel, which strongly influences neuronal excitability. Calmodulin (CaM) binds to two intracellular C-terminal segments of Kv7.2 channels, helices A and B, and it is req

Externí odkaz: https://doaj.org/article/dca1fc06521041f5b0972c7720bcbb4a

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Redox regulation of Kv7 channels through EF3 hand of calmodulin

Neuronal KV7 channels, important regulators of cell excitability, are among the most sensitive proteins to reactive oxygen species. The S2S3 linker of the voltage sensor was reported as a site mediating redox modulation of the channels. Recent struct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::73f95e271f8d9297df223174546de267
https://doi.org/10.1101/2022.09.11.507486

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An Epilepsy-Causing Mutation Leads to Co-Translational Misfolding of the Kv7.2 Channel

Autor: Aitor Bergara, A. Leonardo, Eider Nuñez, Hee Jung Chung, Carolina Gomis-Perez, Alejandra Aguado, Jiaren Zhang, Alvaro Villarroel, Oscar R Ballesteros, Covadonga Malo, Arantza Muguruza-Montero, Janire Urrutia

Publikováno v: Addi: Archivo Digital para la Docencia y la Investigación
Universidad del País Vasco
Addi. Archivo Digital para la Docencia y la Investigación
instname
Digital.CSIC. Repositorio Institucional del CSIC
BMC Biology
BMC Biology, Vol 19, Iss 1, Pp 1-18 (2021)

[Background]: The amino acid sequence of proteins generally carries all the necessary information for acquisition of native conformations, but the vectorial nature of translation can additionally determine the folding outcome. Such consideration is p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92515a87fa801b084a5d9447fa942e32
http://hdl.handle.net/10810/51822

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Additional file 1 of An epilepsy-causing mutation leads to co-translational misfolding of the Kv7.2 channel

Autor: Janire Urrutia, Aguado, Alejandra, Gomis-Perez, Carolina, Muguruza-Montero, Arantza, Ballesteros, Oscar R., Jiaren Zhang, Nuñez, Eider, Covadonga Malo, Chung, Hee Jung, Aritz Leonardo, Bergara, Aitor, Villarroel, Alvaro

Additional file 1: Figure S1. Relationship between normalized current densities from cells expressing Kv7.2 channels carrying the indicated mutations in the helix A. Figure S2. The W344R mutation reduced expression of CFP-Kv7.2 in cultured hippocampa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1c4e99a341636ebd97df886c280bd78

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An Epilepsy-Causing Mutation Leads to Co-Translational Misfolding

Autor: Hee Jung Chung, Arantza Muguruza-Montero, Carolina Gomis-Perez, Covadonga Malo, Alejandra Aguado, Jiaren Zhang, Alvaro Villarroel, Janire Urrutia, A. Leonardo, Aitor Bergara, Eider Nuñez, Oscar R Ballesteros

Protein folding to the native state is particularly relevant in human diseases where inherited mutations lead to structural instability, aggregation and degradation. In general, the amino acid sequence carries all the necessary information for the na

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b4228761feec9985cbe14600a59a31bb
https://doi.org/10.1101/2020.11.25.398222

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Homomeric Kv7.2 current suppression is a common feature in KCNQ2 epileptic encephalopathy

Autor: Alfons Macaya, Miquel Raspall-Chaure, Carolina Gomis-Perez, Eduardo López-Laso, Janire Urrutia, Alvaro Villarroel, Anna Marcé-Grau, Covadonga Malo, Ana Felipe-Rucián

Publikováno v: Epilepsia. 60:139-148

Objective To gain insight into the mechanisms underlying KCNQ2 encephalopathy by examining the electrophysiologic properties of mutant Kv7.2 channels in different multimeric configurations. Methods We analyzed the genotype-phenotype relationship in 4

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60cd1c0bdff1b4ed738b3fdeec0de36a
https://doi.org/10.1111/epi.14609

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