Author

Bernardo I. Pinto

University of ChicagoORCID 0000-0003-0200-1069Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:deep learning· 2 Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Assay:structural biology· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Assay:electrophysiology· 1

Frequent Co-Authors

Francisco BezanillaiD· 3 shared Benoı̂t RouxiD· 2 shared Eduardo PerozoiD· 2 shared Richa AgrawaliD· 2 shared Trayder ThomasiD· 2 shared Carlos A Z BassettoiD· 1 shared Lydia BlachowicziD· 1 shared Ramón LatorreiD· 1 shared

Activity by Year

2025-2026 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersBiophysics

Francisco BezanillaORCID

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4 papers

Recent·Most cited

Mechanistical and structural basis of Kv channel inhibition by 4 aminopyridine

Bernardo I. Pinto, Richa Agrawal, Trayder Thomas, Eduardo Perozo, Benoı̂t Roux, Francisco Bezanilla

This study determines the structure of Kv channels bound to 4AP, showing it binds the closed state and enters via membrane-facing fenestrations, explaining its inhibitory mechanism.

bioRxiv · Sep 15, 2026 · PreprintBiophysics

Structure of the ILT Mutant Shaker K+ Channel and the Mechanism of Voltage Activation

Richa Agrawal, Ramon Mendoza Uriarte, Bernardo I. Pinto, Trayder Thomas, Lydia Blachowicz, Young Hoon Koh, Francisco Bezanilla, Eduardo Perozo, Benoı̂t Roux

The paper determines the cryo-EM structure of a Shaker K+ channel mutant and shows that voltage sensing domain activation induces a dynamic shift in the linker population equilibrium rather than directly pulling the gate open.

bioRxiv · Nov 13, 2025 · PreprintBiophysics

Structural Basis for Voltage Gating and Dalfampridine Binding in the Shaker Potassium Channel Revealed by Closed-State Model

Bernardo I. Pinto

The paper presents a structural model of the closed Shaker potassium channel, revealing how voltage sensor movement drives pore opening and identifies a binding site for dalfampridine.

Biophysical Journal · Jun 24, 2025Peer-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