Author

Ramón Latorre

University of ValparaísoORCID 0000-0002-6044-5795Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Assay:electrophysiology· 2 Approach:statistical model· 2 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

Antonio Peña-PichicoiiD· 1 shared Bernardo I. PintoiD· 1 shared Carlos A Z BassettoiD· 1 shared Eduardo PerozoiD· 1 shared Felipe EcheverríaiD· 1 shared Fernando Danilo González-NiloiD· 1 shared Francisco BezanillaiD· 1 shared Gustavo F. ContrerasiD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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1 shared paperBiophysics

Antonio Peña-PichicoiORCID

Mutual co-authors in cluster

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3 papers

Recent·Most cited

Tuning the gate and the gear: The LRRC26 (γ1) subunit modulates intrinsic gating and voltage-sensor coupling of the BK channel

Felipe Echeverría, Antonio Peña-Pichicoi, Miguel Fernandez, Willy R. Carrasquel-Ursulaez, Juan Pablo Castillo, Osvaldo Diez Alvarez, Ramón Latorre

This study shows that the γ1 subunit of BK channels increases the equilibrium constant for channel opening by destabilizing the closed state and enhancing voltage-sensor-pore coupling.

Proceedings of the National Academy of Sciences · Feb 17, 2026Peer-reviewedBiophysics

The BK channel-NS1619 agonist complex reveals molecular insights on allosteric activation gating

Naileth González-Sanabria, Gustavo F. Contreras, Maximiliano Rojas, Yorley Duarte, Fernando Danilo González-Nilo, Eduardo Perozo, Ramón Latorre

The paper identifies how NS1619 binds to BK channels and stabilizes their open conformation through structural and dynamic analysis.

Proceedings of the National Academy of Sciences · Jan 27, 2026Peer-reviewedBiophysics

Turning a Kv channel into hot and cold receptor by perturbing its electromechanical coupling.

Bernardo I. Pinto, Carlos A Z Bassetto, Ramón Latorre, Francisco Bezanilla

This study shows that a single mutation can drastically alter the temperature response of Kv channels by modifying their electromechanical coupling.

Nature Communications · Apr 9, 2025Peer-reviewedBiophysics