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  1. Article ; Online: Influences: The Cell Physiology Laboratory in Montemar, Chile.

    Bezanilla, Francisco

    The Journal of general physiology

    2018  Volume 150, Issue 11, Page(s) 1464–1468

    MeSH term(s) Animals ; Chile ; Decapodiformes/physiology ; Electrophysiology/history ; History, 20th Century ; Laboratories/history ; Neurophysiology/history
    Language English
    Publishing date 2018-10-19
    Publishing country United States
    Document type Historical Article ; Journal Article
    ZDB-ID 3118-5
    ISSN 1540-7748 ; 0022-1295
    ISSN (online) 1540-7748
    ISSN 0022-1295
    DOI 10.1085/jgp.201812157
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.150: Show issues Location:
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  2. Article ; Online: Gating currents.

    Bezanilla, Francisco

    The Journal of general physiology

    2018  Volume 150, Issue 7, Page(s) 911–932

    Abstract: Many membrane proteins sense the voltage across the membrane where they are inserted, and their function is affected by voltage changes. The voltage sensor consists of charges or dipoles that move in response to changes in the electric field, and their ... ...

    Abstract Many membrane proteins sense the voltage across the membrane where they are inserted, and their function is affected by voltage changes. The voltage sensor consists of charges or dipoles that move in response to changes in the electric field, and their movement produces an electric current that has been called gating current. In the case of voltage-gated ion channels, the kinetic and steady-state properties of the gating charges provide information of conformational changes between closed states that are not visible when observing ionic currents only. In this
    MeSH term(s) Animals ; Humans ; Ion Channel Gating ; Membrane Potentials ; Patch-Clamp Techniques/methods ; Potassium Channels, Voltage-Gated/metabolism ; Voltage-Gated Sodium Channels/metabolism
    Chemical Substances Potassium Channels, Voltage-Gated ; Voltage-Gated Sodium Channels
    Language English
    Publishing date 2018-06-25
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 3118-5
    ISSN 1540-7748 ; 0022-1295
    ISSN (online) 1540-7748
    ISSN 0022-1295
    DOI 10.1085/jgp.201812090
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  3. Article: A Mechanistic Reinterpretation of Fast Inactivation in Voltage-Gated Na

    Liu, Yichen / Bassetto, Carlos A Z / Pinto, Bernardo I / Bezanilla, Francisco

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Fast Inactivation in voltage-gated ... ...

    Abstract Fast Inactivation in voltage-gated Na
    Language English
    Publishing date 2023-04-28
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.04.27.538555
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: A Mechanistic Reinterpretation of Fast Inactivation in Voltage-Gated Na+ Channels.

    Liu, Yichen / Bassetto, Carlos A Z / Pinto, Bernardo I / Bezanilla, Francisco

    Research square

    2023  

    Abstract: The hinged-lid model is long accepted as the canonical model for fast inactivation in Nav channels. It predicts that the hydrophobic IFM motif acts intracellularly as the gating particle that binds and occludes the pore during fast inactivation. However, ...

    Abstract The hinged-lid model is long accepted as the canonical model for fast inactivation in Nav channels. It predicts that the hydrophobic IFM motif acts intracellularly as the gating particle that binds and occludes the pore during fast inactivation. However, the observation in recent high-resolution structures that the bound IFM motif locates far from the pore, contradicts this preconception. Here, we provide a mechanistic reinterpretation of fast inactivation based on structural analysis and ionic/gating current measurements. We demonstrate that in Nav1.4 the final inactivation gate is comprised of two hydrophobic rings at the bottom of S6 helices. These rings function
    Language English
    Publishing date 2023-05-22
    Publishing country United States
    Document type Preprint
    DOI 10.21203/rs.3.rs-2924505/v1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: A mechanistic reinterpretation of fast inactivation in voltage-gated Na

    Liu, Yichen / Bassetto, Carlos A Z / Pinto, Bernardo I / Bezanilla, Francisco

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 5072

    Abstract: The hinged-lid model was long accepted as the canonical model for fast inactivation in Nav channels. It predicts that the hydrophobic IFM motif acts intracellularly as the gating particle that binds and occludes the pore during fast inactivation. However, ...

    Abstract The hinged-lid model was long accepted as the canonical model for fast inactivation in Nav channels. It predicts that the hydrophobic IFM motif acts intracellularly as the gating particle that binds and occludes the pore during fast inactivation. However, the observation in recent high-resolution structures that the bound IFM motif is located far from the pore, contradicts this preconception. Here, we provide a mechanistic reinterpretation of fast inactivation based on structural analysis and ionic/gating current measurements. We demonstrate that in Nav1.4 the final inactivation gate is comprised of two hydrophobic rings at the bottom of S6 helices. These rings function in series and close downstream of IFM binding. Reducing the volume of the sidechain in both rings leads to a partially conductive, leaky inactivated state and decreases the selectivity for Na
    MeSH term(s) Ear Auricle ; Electric Conductivity ; Ion Transport ; Ions
    Chemical Substances Ions
    Language English
    Publishing date 2023-08-21
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-40514-4
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  6. Article ; Online: Ion channel thermodynamics studied with temperature jumps measured at the cell membrane.

    Bassetto, Carlos A Z / Pinto, Bernardo I / Latorre, Ramon / Bezanilla, Francisco

    Biophysical journal

    2023  Volume 122, Issue 4, Page(s) 661–671

    Abstract: Perturbing the temperature of a system modifies its energy landscape, thus providing a ubiquitous tool to understand biological processes. Here, we developed a framework to generate sudden temperature jumps (Tjumps) and sustained temperature steps ( ... ...

    Abstract Perturbing the temperature of a system modifies its energy landscape, thus providing a ubiquitous tool to understand biological processes. Here, we developed a framework to generate sudden temperature jumps (Tjumps) and sustained temperature steps (Tsteps) to study the temperature dependence of membrane proteins under voltage clamp while measuring the membrane temperature. Utilizing the melanin under the Xenopus laevis oocytes membrane as a photothermal transducer, we achieved short Tjumps up to 9°C in less than 1.5 ms and constant Tsteps for durations up to 150 ms. We followed the temperature at the membrane with sub-ms time resolution by measuring the time course of membrane capacitance, which is linearly related to temperature. We applied Tjumps in Kir1.1 isoform b, which reveals a highly temperature-sensitive blockage relief, and characterized the effects of Tsteps on the temperature-sensitive channels TRPM8 and TRPV1. These newly developed approaches provide a general tool to study membrane protein thermodynamics.
    MeSH term(s) Animals ; Temperature ; Membrane Potentials ; Ion Channels/metabolism ; Cell Membrane/metabolism ; Thermodynamics ; Xenopus laevis/metabolism ; Oocytes/metabolism
    Chemical Substances Ion Channels
    Language English
    Publishing date 2023-01-18
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2023.01.015
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 235: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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    Zs.MO 2: Show issues

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  7. Article: Optocapacitance: physical basis and its application.

    Pinto, Bernardo I / Bassetto, Carlos A Z / Bezanilla, Francisco

    Biophysical reviews

    2022  Volume 14, Issue 2, Page(s) 569–577

    Abstract: The observation that membrane capacitance increases with temperature has led to the development of new methods of neuronal stimulation using light. The optocapacitive effect refers to a light-induced change in capacitance produced by the heating of the ... ...

    Abstract The observation that membrane capacitance increases with temperature has led to the development of new methods of neuronal stimulation using light. The optocapacitive effect refers to a light-induced change in capacitance produced by the heating of the membrane through a photothermal effect. This change in capacitance manifests as a current, named optocapacitive current that depolarizes cells and therefore can be used to stimulate excitable tissues. Here, we discuss how optocapacitance arises from basic membrane properties, the characteristics of the optocapacitive current, its use for neuronal stimulation, and the challenges for its application in vivo.
    Language English
    Publishing date 2022-04-13
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 2486483-3
    ISSN 1867-2469 ; 1867-2450
    ISSN (online) 1867-2469
    ISSN 1867-2450
    DOI 10.1007/s12551-022-00943-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Noncanonical electromechanical coupling paths in cardiac hERG potassium channel.

    Bassetto, Carlos A Z / Costa, Flavio / Guardiani, Carlo / Bezanilla, Francisco / Giacomello, Alberto

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 1110

    Abstract: Voltage-gated potassium channels are involved in many physiological processes such as nerve impulse transmission, the heartbeat, and muscle contraction. However, for many of them the molecular determinants of the gating mechanism remain elusive. Here, ... ...

    Abstract Voltage-gated potassium channels are involved in many physiological processes such as nerve impulse transmission, the heartbeat, and muscle contraction. However, for many of them the molecular determinants of the gating mechanism remain elusive. Here, using a combination of theoretical and experimental approaches, we address this problem focusing on the cardiac hERG potassium channel. Network analysis of molecular dynamics trajectories reveals the presence of a kinematic chain of residues that couples the voltage sensor domain to the pore domain and involves the S4/S1 and S1/S5 subunit interfaces. Mutagenesis experiments confirm the role of these residues and interfaces in the activation and inactivation mechanisms. Our findings demonstrate the presence of an electromechanical transduction path crucial for the non-domain-swapped hERG channel gating that resembles the noncanonical path identified in domain-swapped K
    MeSH term(s) Heart Rate ; Muscle Contraction ; Mutagenesis ; Potassium Channels, Voltage-Gated ; Synaptic Transmission
    Chemical Substances Potassium Channels, Voltage-Gated ; KCNH2 protein, human
    Language English
    Publishing date 2023-02-27
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-36730-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Methodological improvements for fluorescence recordings in

    Lee, Elizabeth E L / Bezanilla, Francisco

    The Journal of general physiology

    2019  Volume 151, Issue 2, Page(s) 264–272

    Abstract: ... Xenopus ... ...

    Abstract Xenopus laevis
    MeSH term(s) Animals ; Female ; Fluorescence ; Melanins/metabolism ; Oocytes/drug effects ; Oocytes/metabolism ; Oocytes/radiation effects ; Patch-Clamp Techniques/methods ; Phenylurea Compounds/pharmacology ; Protein Kinase Inhibitors/pharmacology ; Pyrimidines/pharmacology ; Ultraviolet Rays ; Xenopus
    Chemical Substances HG-9-91-01 ; Melanins ; Phenylurea Compounds ; Protein Kinase Inhibitors ; Pyrimidines
    Language English
    Publishing date 2019-01-03
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 3118-5
    ISSN 1540-7748 ; 0022-1295
    ISSN (online) 1540-7748
    ISSN 0022-1295
    DOI 10.1085/jgp.201812189
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Photolipid excitation triggers depolarizing optocapacitive currents and action potentials.

    Bassetto, Carlos A Z / Pfeffermann, Juergen / Yadav, Rohit / Strassgschwandtner, Simon / Glasnov, Toma / Bezanilla, Francisco / Pohl, Peter

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 1139

    Abstract: Optically-induced changes in membrane capacitance may regulate neuronal activity without requiring genetic modifications. Previously, they mainly relied on sudden temperature jumps due to light absorption by membrane-associated nanomaterials or water. ... ...

    Abstract Optically-induced changes in membrane capacitance may regulate neuronal activity without requiring genetic modifications. Previously, they mainly relied on sudden temperature jumps due to light absorption by membrane-associated nanomaterials or water. Yet, nanomaterial targeting or the required high infrared light intensities obstruct broad applicability. Now, we propose a very versatile approach: photolipids (azobenzene-containing diacylglycerols) mediate light-triggered cellular de- or hyperpolarization. As planar bilayer experiments show, the respective currents emerge from millisecond-timescale changes in bilayer capacitance. UV light changes photolipid conformation, which awards embedding plasma membranes with increased capacitance and evokes depolarizing currents. They open voltage-gated sodium channels in cells, generating action potentials. Blue light reduces the area per photolipid, decreasing membrane capacitance and eliciting hyperpolarization. If present, mechanosensitive channels respond to the increased mechanical membrane tension, generating large depolarizing currents that elicit action potentials. Membrane self-insertion of administered photolipids and focused illumination allows cell excitation with high spatiotemporal control.
    MeSH term(s) Action Potentials ; Membrane Potentials ; Cell Membrane ; Neurons/physiology ; Ultraviolet Rays
    Language English
    Publishing date 2024-02-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-45403-y
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