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Molecular aspects of the voltage sensor of ionic channels: structure, kinetics and evolution

Abstract

Electrical signaling constitutes one of the primary means of communication in the nervous system and other excitable tissues with the voltage-gated ion channels being responsible for initiating and propagating electrical impulses. Voltage-gated ion channels are also involved in different mechanisms related to body homeostasis such as intracellular regulation of calcium and hydrogen ion concentrations. Due to those reasons, the physical properties of these channels and its interaction with chemical agents have been extensively studied during the last decades. The voltage-gated ion channels exist in three functional states depending on transmembrane voltage: closed, open or inactivated. The improvement of molecular biology, electrophysiology and crystallography techniques jumped up the ion channel studies to a molecular level. However, structure/functional states studies are scarce in the literature and low disseminated in Brazil. Taking advantage from my experience obtained in the Department of Physiology of University of Wisconsin, we intent to open a new research line in the Departamento de Biofísica of Unifesp, focusing our studies on ion channel structure/function relationship. The research topics associated with this proposal have specific interest on the activity of the voltage sensor of voltage-gated ion channels and comprise: i) the coupling between the voltage sensor and pore of potassium channels; ii) the functional characterization of negative charged residues of the voltage sensor of domain IV to the inactivation of sodium channels and; iii) the co-evolution analysis of voltage-gated proton channels. (AU)

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Scientific publications (5)
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
RIBEIRO-SILVA, LUISA; QUEIROZ, FERNANDA OLIVEIRA; BRITO DA SILVA, ANNIELLE MENDES; HIRATA, APARECIDA EMIKO; ARCISIO-MIRANDA, MANOEL. Voltage-Gated Proton Channel in Human Glioblastoma Multiforme Cells. ACS Chemical Neuroscience, v. 7, n. 7, p. 864-869, . (10/52077-9, 13/26005-9)
PANINKA, ROLF MATIAS; CARLOS-LIMA, ESTEVAO; LINDSEY, SUSAN C.; KUNII, ILDA S.; DIAS-DA-SILVA, MAGNUS R.; ARCISIO-MIRANDA, MANOEL. DOWN-REGULATION OF Kir2.6 CHANNEL BY C-TERMINI MUTATION D252N AND ITS ASSOCIATION WITH THE SUSCEPTIBILITY TO THYROTOXIC PERIODIC PARALYSIS. Neuroscience, v. 346, p. 197-202, . (10/52077-9, 11/20747-8)
DOS SANTOS CABRERA, MARCIA PEREZ; BALDISSERA, GISELE; SILVA-GONCALVES, LAIZ DA COSTA; DE SOUZA, BIBIANA MONSON; RISKE, KARIN A.; PALMA, MARIO SERGIO; RUGGIERO, JOSE ROBERTO; ARCISIO-MIRANDA, MANOEL. Combining Experimental Evidence and Molecular Dynamic Simulations To Understand the Mechanism of Action of the Antimicrobial Octapeptide Jelleine-I. BIOCHEMISTRY, v. 53, n. 29, p. 4857-4868, . (11/51684-1, 06/57122-7, 10/11823-0, 10/52077-9, 12/24259-0)
PANINKA, ROLF M.; MAZZOTTI, DIEGO R.; KIZYS, MARINA M. L.; VIDI, ANGELA C.; RODRIGUES, HELIO; SILVA, SILAS P.; KUNII, ILDA S.; FURUZAWA, GILBERTO K.; ARCISIO-MIRANDA, MANOEL; DIAS-DA-SILVA, MAGNUS R.. Whole genome and exome sequencing realignment supports the assignment of KCNJ12, KCNJ17, and KCNJ18 paralogous genes in thyrotoxic periodic paralysis locus: functional characterization of two polymorphic Kir2.6 isoforms. Molecular Genetics and Genomics, v. 291, n. 4, p. 1535-1544, . (10/52077-9, 11/20747-8)
DOS SANTOS CABRERA, MARCIA PEREZ; ARCISIO-MIRANDA, MANOEL; GORJAO, RENATA; LEITE, NATALIA BUENO; DE SOUZA, BIBIANA MONSON; CURI, RUI; PROCOPIO, JOAQUIM; RUGGIERO NETO, JOAO; PALMA, MARIO SERGIO. Influence of the Bilayer Composition on the Binding and Membrane Disrupting Effect of Polybia-MP1, an Antimicrobial Mastoparan Peptide with Leukemic T-Lymphocyte Cell Selectivity. BIOCHEMISTRY, v. 51, n. 24, p. 4898-4908, . (10/11823-0, 06/57122-7, 10/52077-9)

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