Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Carlos A. Villalba-Galea"'
Publikováno v:
Frontiers in Pharmacology, Vol 11 (2020)
An ever-growing body of evidence has shown that voltage-gated ion channels are likely molecular systems that display hysteresis in their activity. This phenomenon manifests in the form of dynamic changes in both their voltage dependence of activity a
Externí odkaz:
https://doaj.org/article/30262a4ee9b7468cb85deddc29a11ae7
Autor:
Carlos A. Villalba-Galea
Publikováno v:
Frontiers in Pharmacology, Vol 11 (2020)
The activity of KV7 channels critically contributes to the regulation of cellular electrical excitability in many cell types. In the central nervous system, the heteromeric KV7.2/KV7.3 channel is thought to be the chief molecular entity giving rise t
Externí odkaz:
https://doaj.org/article/101e789dc08b497cabbe06e6493ac043
Autor:
Christian R. Halaszovich, Michael G. Leitner, Angeliki Mavrantoni, Audrey Le, Ludivine Frezza, Anja Feuer, Daniela N. Schreiber, Carlos A. Villalba-Galea, Dominik Oliver
Publikováno v:
Journal of Lipid Research, Vol 53, Iss 11, Pp 2266-2274 (2012)
In voltage-sensitive phosphatases (VSPs), a transmembrane voltage sensor domain (VSD) controls an intracellular phosphoinositide phosphatase domain, thereby enabling immediate initiation of intracellular signals by membrane depolarization. The existe
Externí odkaz:
https://doaj.org/article/b8403ec3445b4b2ca548629ef0b4fadb
Autor:
Carlos A. Villalba-Galea
Publikováno v:
Journal of General Physiology. 155
This letter proposes an alternative explanation to the work published by Cowgill and Chanda on the nature of hysteresis in the voltage-gated, potassium-selective channel Shaker.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::38fd2631d4c365f9b67f7d0fdcc028ea
https://doi.org/10.1085/jgp.202313371
https://doi.org/10.1085/jgp.202313371
Autor:
Concepción Pérez, Clara Herrera-Arozamena, Olaia Martí-Marí, María Isabel Rodríguez-Franco, Mario de la Fuente Revenga, Carlos A. Villalba-Galea, Martín Estrada-Valencia
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
By linking two N-methyl-N-carbocyclic quaternary ammonium groups to an azobenzene scaffold in meta- or para-positions we generated a series of photoswitchable neuromuscular ligands for which we coined the term “azocuroniums”. These compounds swit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cf3cdf80ed4edae8f488ee4d249b1d8
http://hdl.handle.net/10261/217685
http://hdl.handle.net/10261/217685
Autor:
Helen H. Robinson, Carlos A. Villalba-Galea, Hannah E. Small, Linda M. Boland, Aaron Corbin-Leftwich
Publikováno v:
The Journal of General Physiology
Voltage-gated Na+ and K+ channels are known to underlie the temporal characteristics of action potentials. Corbin-Leftwich et al. establish reliable action potential recordings from Xenopus oocytes coexpressing these channels and show how different K
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dec3c6161ce5001c82454c4b6e6dc9a6
https://doi.org/10.1085/jgp.201812146
https://doi.org/10.1085/jgp.201812146
Autor:
Scott K. Adney, Mayra Delgado-Ramírez, Jorge Arreola, Aldo A. Rodríguez-Menchaca, Iván A. Aréchiga-Figueroa, Carlos A. Villalba-Galea, José J. De Jesús-Pérez, Diomedes E. Logothetis
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
Scientific Reports
Scientific Reports
Phosphatidylinositol 4,5-bisphosphate (PIP2) is a membrane phospholipid that regulates the function of multiple ion channels, including some members of the voltage-gated potassium (Kv) channel superfamily. The PIP2 sensitivity of Kv channels is well
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::997056efc903ea1b0588c609bcfcd9d5
http://link.springer.com/article/10.1038/s41598-018-20280-w
http://link.springer.com/article/10.1038/s41598-018-20280-w
Autor:
María Isabel Rodríguez-Franco, Carlos A. Villalba-Galea, Martín Estrada-Valencia, Clara Herrera-Arozamena
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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Muscular nicotinic acetylcholine receptors (nAChR) are ligand-gated ion channels located in the plasma membrane of the post-junctional motor endplate in skeletal muscles. These receptors are responsible for triggering the electrical signal that leads
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98dfb50af3cdf1218f5e4035420191bd
http://hdl.handle.net/10261/206136
http://hdl.handle.net/10261/206136
Autor:
Aaron Corbin-Leftwich, Junghoon Ha, Audrey Le, Sayeed M. Mossadeq, Carlos A. Villalba-Galea, Iwona Ruchala
Publikováno v:
The Journal of General Physiology
Researchers studied the mechanism by which the anticonvulsant Retigabine enhances the activity of K+ channels and found that the drug stabilizes on open state at resting membrane potentials.
The anticonvulsant Retigabine is a KV7 channel agonist
The anticonvulsant Retigabine is a KV7 channel agonist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61f03fff99267d43f1535aea65022831
http://europepmc.org/articles/PMC4772374
http://europepmc.org/articles/PMC4772374
Autor:
Qufei Li, Eduardo Perozo, Klaus Schulten, David Medovoy, Sherry Wanderling, Raymond E. Hulse, Anthony A. Kossiakoff, Carlos A. Villalba-Galea, Abhishek Singharoy, Ryan McGreevy, Benoît Roux, Marcin Paduch
Publikováno v:
Nature Structural & Molecular Biology. 21:244-252
The transduction of transmembrane electric fields into protein motion plays an essential role in the generation and propagation of cellular signals. Voltage-sensing domains (VSD) carry out these functions through reorientations of S4 helix with discr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e53146d8e8a36f182eadde586370a8ec
https://doi.org/10.1038/nsmb.2768
https://doi.org/10.1038/nsmb.2768