Gotowe bibliografie tematyczne / KCNQ channels

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Gotowa bibliografia na temat „KCNQ channels”

Autor: Grafiati

Data publikacji: 5 czerwca 2025

Data aktualizacji: 2 sierpnia 2025

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Artykuły w czasopismach na temat "KCNQ channels"

Pattnaik, Bikash R., and Bret A. Hughes. "Effects of KCNQ channel modulators on the M-type potassium current in primate retinal pigment epithelium." American Journal of Physiology-Cell Physiology 302, no. 5 (2012): C821—C833. http://dx.doi.org/10.1152/ajpcell.00269.2011.

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Recently, we demonstrated the expression of KCNQ1, KCNQ4, and KCNQ5 transcripts in monkey retinal pigment epithelium (RPE) and showed that the M-type current in RPE cells is blocked by the specific KCNQ channel blocker XE991. Using patch-clamp electrophysiology, we investigated the pharmacological sensitivity of the M-type current in isolated monkey RPE cells to elucidate the subunit composition of the channel. Most RPE cells exhibited an M-type current with a voltage for half-maximal activation of approximately −35 mV. The M-type current activation followed a double-exponential time course an

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Gamper, Nikita, Yang Li, and Mark S. Shapiro. "Structural Requirements for Differential Sensitivity of KCNQ K+ Channels to Modulation by Ca2+/Calmodulin." Molecular Biology of the Cell 16, no. 8 (2005): 3538–51. http://dx.doi.org/10.1091/mbc.e04-09-0849.

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Calmodulin modulation of ion channels has emerged as a prominent theme in biology. The sensitivity of KCNQ1–5 K+ channels to modulation by Ca2+/calmodulin (CaM) was studied using patch-clamp, Ca2+ imaging, and biochemical and pharmacological approaches. Coexpression of CaM in Chinese hamster ovary (CHO) cells strongly reduced currents of KCNQ2, KCNQ4, and KCNQ5, but not KCNQ1 or KCNQ3. In simultaneous current recording/Ca2+ imaging experiments, CaM conferred Ca2+ sensitivity to KCNQ4 and KCNQ5, but not to KCNQ1, KCNQ3, or KCNQ1/KCNE1 channels. A chimera constructed from the carboxy terminus of

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Brueggemann, Lioubov I., Jennifer M. Haick, Samantha Neuburg та ін. "KCNQ (Kv7) potassium channel activators as bronchodilators: combination with a β2-adrenergic agonist enhances relaxation of rat airways". American Journal of Physiology-Lung Cellular and Molecular Physiology 306, № 6 (2014): L476—L486. http://dx.doi.org/10.1152/ajplung.00253.2013.

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KCNQ (Kv7 family) potassium (K+) channels were recently found in airway smooth muscle cells (ASMCs) from rodent and human bronchioles. In the present study, we evaluated expression of KCNQ channels and their role in constriction/relaxation of rat airways. Real-time RT-PCR analysis revealed expression of KCNQ4 > KCNQ5 > KCNQ1 > KCNQ2 > KCNQ3, and patch-clamp electrophysiology detected KCNQ currents in rat ASMCs. In precision-cut lung slices, the KCNQ channel activator retigabine induced a concentration-dependent relaxation of small bronchioles preconstricted with methacholine (MeCh;

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Zhang, Xiaoming, Dongli Yang, and Bret A. Hughes. "KCNQ5/Kv7.5 potassium channel expression and subcellular localization in primate retinal pigment epithelium and neural retina." American Journal of Physiology-Cell Physiology 301, no. 5 (2011): C1017—C1026. http://dx.doi.org/10.1152/ajpcell.00185.2011.

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Previous studies identified in retinal pigment epithelial (RPE) cells an M-type K+ current, which in many other cell types is mediated by channels encoded by KCNQ genes. The aim of this study was to assess the expression of KCNQ genes in the monkey RPE and neural retina. Application of the specific KCNQ channel blocker XE991 eliminated the M-type current in freshly isolated monkey RPE cells, indicating that KCNQ subunits contribute to the underlying channels. RT-PCR analysis revealed the expression of KCNQ1, KCNQ4, and KCNQ5 transcripts in the RPE and all five KCNQ transcripts in the neural re

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Wang, Alice W., Michael C. Yau, Caroline K. Wang, et al. "Four drug-sensitive subunits are required for maximal effect of a voltage sensor–targeted KCNQ opener." Journal of General Physiology 150, no. 10 (2018): 1432–43. http://dx.doi.org/10.1085/jgp.201812014.

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KCNQ2-5 (Kv7.2–Kv7.5) channels are strongly influenced by an emerging class of small-molecule channel activators. Retigabine is the prototypical KCNQ activator that is thought to bind within the pore. It requires the presence of a Trp side chain that is conserved among retigabine-sensitive channels but absent in the retigabine-insensitive KCNQ1 subtype. Recent work has demonstrated that certain KCNQ openers are insensitive to mutations of this conserved Trp, and that their effects are instead abolished or attenuated by mutations in the voltage-sensing domain (VSD). In this study, we investigat

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Pablo, Juan Lorenzo, and Geoffrey S. Pitt. "FGF14 is a regulator of KCNQ2/3 channels." Proceedings of the National Academy of Sciences 114, no. 1 (2016): 154–59. http://dx.doi.org/10.1073/pnas.1610158114.

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KCNQ2/3 (Kv7.2/7.3) channels and voltage-gated sodium channels (VGSCs) are enriched in the axon initial segment (AIS) where they bind to ankyrin-G and coregulate membrane potential in central nervous system neurons. The molecular mechanisms supporting coordinated regulation of KCNQ and VGSCs and the cellular mechanisms governing KCNQ trafficking to the AIS are incompletely understood. Here, we show that fibroblast growth factor 14 (FGF14), previously described as a VGSC regulator, also affects KCNQ function and localization. FGF14 knockdown leads to a reduction of KCNQ2 in the AIS and a reduct

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Li, Yang, Paul Langlais, Nikita Gamper, Feng Liu, and Mark S. Shapiro. "Dual Phosphorylations Underlie Modulation of Unitary KCNQ K+Channels by Src Tyrosine Kinase." Journal of Biological Chemistry 279, no. 44 (2004): 45399–407. http://dx.doi.org/10.1074/jbc.m408410200.

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Src tyrosine kinase suppresses KCNQ (M-type) K+channels in a subunit-specific manner representing a mode of modulation distinct from that involving G protein-coupled receptors. We probed the molecular and biophysical mechanisms of this modulation using mutagenesis, biochemistry, and both whole-cell and single channel modes of patch clamp recording. Immunoprecipitation assays showed that Src associates with KCNQ2–5 subunits but phosphorylates only KCNQ3–5. Using KCNQ3 as a background, we found that mutation of a tyrosine in the amino terminus (Tyr-67) or one in the carboxyl terminus (Tyr-349) a

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Zhang, Fan, Yani Liu, Dandan Zhang, Xizhenzi Fan, Decheng Shao, and Han Li. "Suppression of KCNQ/M Potassium Channel in Dorsal Root Ganglia Neurons Contributes to the Development of Osteoarthritic Pain." Pharmacology 103, no. 5-6 (2019): 257–62. http://dx.doi.org/10.1159/000496422.

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Osteoarthritic pain has a strong impact on patients’ quality of life. Understanding the pathogenic mechanisms underlying osteoarthritic pain will likely lead to the development of more effective treatments. In the present study of osteoarthritic model rats, we observed a reduction of M-current density and a remarkable decrease in the levels of KCNQ2 and KCNQ3 proteins and mRNAs in dorsal root ganglia (DRG) neurons, which were associated with hyperalgesic behaviors. The activation of KCNQ/M channels with flupirtine significantly increased the mechanical threshold and prolonged the withdrawal la

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Schuetz, Friderike, Sharad Kumar, Philip Poronnik, and David J. Adams. "Regulation of the voltage-gated K+ channels KCNQ2/3 and KCNQ3/5 by serum- and glucocorticoid-regulated kinase-1." American Journal of Physiology-Cell Physiology 295, no. 1 (2008): C73—C80. http://dx.doi.org/10.1152/ajpcell.00146.2008.

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The voltage-gated KCNQ2/3 and KCNQ3/5 K+ channels regulate neuronal excitability. We recently showed that KCNQ2/3 and KCNQ3/5 channels are regulated by the ubiquitin ligase Nedd4-2. Serum- and glucocorticoid-regulated kinase-1 (SGK-1) plays an important role in regulation of epithelial ion transport. SGK-1 phosphorylation of Nedd4-2 decreases the ability of Nedd4-2 to ubiquitinate the epithelial Na+ channel, which increases the abundance of channel protein in the cell membrane. In this study, we investigated the mechanism(s) of SGK-1 regulation of M-type KCNQ channels expressed in Xenopus oocy

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Lagrange, Andre. "Retigabine: Bending Potassium Channels to Our Will." Epilepsy Currents 5, no. 5 (2005): 166–68. http://dx.doi.org/10.1111/j.1535-7511.2005.00052.x.

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The New Anticonvulsant Retigabine Favors Voltage-dependent Opening of the Kv7.2 (KCNQ2) Channel by Binding to Its Activation Gate Wuttke TV, Seebohm G, Bail S, Maljevic S, Lerche H Mol Pharmacol 2005;67:1009–1017 Retigabine (RTG) is an anticonvulsant drug with a novel mechanism of action. It activates neuronal KCNQ-type K+ channels by inducing a large hyperpolarizing shift of steady-state activation. To identify the structural determinants of KCNQ channel activation by RTG, we constructed a set of chimeras by using the neuronal KV7.2 ( KCNQ2) channel, which is activated by RTG, and the cardiac

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Rozprawy doktorskie na temat "KCNQ channels"

Kim, Robin Yongkyu. "Mechanistic insights into retigabine modulation of neuronal KCNQ channels." Thesis, University of British Columbia, 2017. http://hdl.handle.net/2429/62625.

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The full abstract for this thesis is available in the body of the thesis, and will be available when the embargo expires.<br>Medicine, Faculty of<br>Anesthesiology, Pharmacology and Therapeutics, Department of<br>Graduate

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Mruk, Karen. "Small Molecule Investigation of KCNQ Potassium Channels: A Dissertation." eScholarship@UMMS, 2012. https://escholarship.umassmed.edu/gsbs_diss/621.

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Voltage-gated K+ channels associate with multiple regulatory proteins to form complexes with diverse gating properties and pharmacological sensitivities. Small molecules which activate or inhibit channel function are valuable tools for dissecting the assembly and function of these macromolecular complexes. My thesis focuses on the discovery and use of small molecules to probe the structure and function of the KCNQ family of voltage-gated K+ channels. One protein that obligatorily assembles with KCNQ channels to mediate proper assembly, trafficking, and gating is the calcium sensor, calmodulin.

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Gage, Steven D. "Structural and Functional Studies of the KCNQ1-KCNE K⁺ Channel Complex: A Dissertation." eScholarship@UMMS, 2008. https://escholarship.umassmed.edu/gsbs_diss/409.

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KCNQ1 is a homotetrameric voltage-gated potassium channel expressed in cardiomyocytes and epithelial tissues. However, currents arising from KCNQ1 have never been physiologically observed. KCNQ1 is able to provide the diverse potassium conductances required by these distinct cell types through coassembly with and modulation by type I transmembrane β-subunits of the KCNE gene family. KCNQ1-KCNE K+ channels play important physiological roles. In cardiac tissues the association of KCNQ1 with KCNE1 gives rise to IKs, the slow delayed outwardly rectifying potassium current. IKs is in part responsib

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Cerina, Manuela [Verfasser], and Thomas [Akademischer Betreuer] Budde. "The role of KCNQ channels in the thalamus / Manuela Cerina ; Betreuer: Thomas Budde." Münster : Universitäts- und Landesbibliothek Münster, 2013. http://d-nb.info/1141577968/34.

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Brennan, Sean. "KV7 potassium channels : a focus on human intra-pulmonary arteries." Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/kv7-potassium-channels-a-focus-on-human-intrapulmonary-arteries(46f5ff0e-1674-4ab1-916d-2f43e3c585e5).html.

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Pulmonary arterial hypertension (PAH) is a disease in which pulmonary vascular resistance increases. The cell membrane of pulmonary artery smooth muscle cells (PASMC) in PAH patients is depolarised, resulting in disrupted Ca2+ signalling leading to smooth muscle constriction and PASMC proliferation and migration. In rat pulmonary artery (PA) smooth muscle the KV7 K+ channels, encoded by the KCNQ genes, have been proposed to contribute to the resting K+ current, promoting low resting tone by maintaining a negative membrane potential and low intracellular Ca2+. KV7 channel activating drugs have

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Delank, Anna-Katharina [Verfasser], and Sven [Akademischer Betreuer] Meuth. "The role of KCNQ-channels in the pathophysiology of multiple sclerosis / Anna-Katharina Delank ; Betreuer: Sven Meuth." Münster : Universitäts- und Landesbibliothek Münster, 2021. http://d-nb.info/1229512187/34.

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Piccinin, Sonia. "The role of group I mGluRs and KCNQ/M channels in synaptic and non-synaptic neuronal activity in hippocampal slices." Thesis, University of Bristol, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.486110.

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The overall aim of this work was to establish the role of group I mGluR and KCNQ/M channels in aspects of the neurophysiology of area CA1 of the rat hippocampus. Specifically we studied the role of these putative drug targets in a form of epileptiform activity and in the slow fEPSP recorded using extracellular methods. First, we have described here the extracellular recording of an excitatory slow fEPSP which is predominantly mediated by acetylcholine, as evidenced by the increase in physostigmine and inhibition in the presence of atropine. This type of response is significantly enhanced by tw

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Prole, David L. "Intrinsic functional properties of neuronal KCNQ2/KCNQ3 potassium channels : insights into channel structure." Thesis, University of Bristol, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.400272.

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Morin, Trevor J. "Chemical-Biological Investigation of KCNQ1/KCNE K⁺ Channel Complexes: A Dissertation." eScholarship@UMMS, 2008. https://escholarship.umassmed.edu/gsbs_diss/398.

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KCNE β-subunits modulate KCNQ1 (Q1) voltage-gate K+channels providing the current diversity required for Q1 channels to function in a wide variety of cell types and tissues. In the present thesis, the stoichiometry of KCNE1 (E1) β-subunits in functioning Q1 channels is investigated, along with the formation of heteromeric channel complexes, complexes containing 2 different KCNE β-subunits. The chemical approaches used to answer these questions were then expanded to generate a novel labeling reagent. To determine the stoichiometry of the Q1/E1 complex, I devised an iterative subunit counting ap

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Shimizu, Atsuya, Ryoko Niwa, Zhibo Lu, Haruo Honjo, and Kaichiro Kamiya. "Effects of Dronedarone on HERG and KCNQ1/KCNE1 Channels." Research Institute of Environmental Medicine, Nagoya University, 2003. http://hdl.handle.net/2237/7585.

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Książki na temat "KCNQ channels"

Chan, Priscilla Jay. Functional and Biochemical Characterization of KCNQ1/KCNE1 Subunit Interactions in the Cardiac IKs Potassium Channel. [publisher not identified], 2011.

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Części książek na temat "KCNQ channels"

Tzingounis, Anastasios V., and H. Peter Larsson. "KCNQ Channels." In Textbook of Ion Channels Volume II. CRC Press, 2023. http://dx.doi.org/10.1201/9781003096276-6.

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Abbott, Geoffrey W. "KCNE Regulation of KCNQ Channels." In Studies of Epithelial Transporters and Ion Channels. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-55454-5_25.

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Gurney, Alison M., Shreena Joshi, and Boris Manoury. "KCNQ Potassium Channels: New Targets for Pulmonary Vasodilator Drugs?" In Advances in Experimental Medicine and Biology. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-500-2_26.

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Byron, Kenneth L., Lioubov I. Brueggemann, Priyanka P. Kakad, and Jennifer M. Haick. "Kv7 (KCNQ) Potassium Channels and L-type Calcium Channels in the Regulation of Airway Diameter." In Calcium Signaling In Airway Smooth Muscle Cells. Springer International Publishing, 2013. http://dx.doi.org/10.1007/978-3-319-01312-1_2.

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Tiwari, Purushottam B., Pareesa Kamgar-Dayhoff, Prakriti Tiwari, Maria I. McKillop, and Tinatin I. Brelidze. "Use of Surface Plasmon Resonance Technique for Studies of Inter-domain Interactions in Ion Channels." In Methods in Molecular Biology. Springer US, 2024. http://dx.doi.org/10.1007/978-1-0716-3818-7_7.

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AbstractIon channels are transmembrane proteins essential for cellular functions and are important drug targets. Surface plasmon resonance (SPR) is a powerful technique for investigating protein–protein and protein–small molecule ligand interactions. SPR has been underutilized for studies of ion channels, even though it could provide a wealth of information on the mechanisms of ion channel regulation and aid in ion channel drug discovery. Here we provide a detailed description of the use of SPR technology for investigating inter-domain interactions in KCNH potassium-selective and voltage-gated

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Loussouarn, Gildas, Isabelle BarÃ³, and Denis Escande. "KCNQ1 K+ Channelâ€”Mediated Cardiac Channelopathies." In Ion Channels. Humana Press, 2006. http://dx.doi.org/10.1385/1-59745-095-2:167.

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Sanguinetti, Michael C., and Guiscard Seebohm. "Physiological Functions, Biophysical Properties, and Regulation of KCNQ1 (KV7.1) Potassium Channels." In Ion Channels in Biophysics and Physiology. Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-4254-8_15.

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"KCNQ Channels." In Handbook of Ion Channels. CRC Press, 2015. http://dx.doi.org/10.1201/b18027-28.

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Cooper, Edward C. "Potassium Channels (Including KCNQ) and Epilepsy." In Jasper's Basic Mechanisms of the Epilepsies. Oxford University Press, 2012. http://dx.doi.org/10.1093/med/9780199746545.003.0005.

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Wu, Zizhen, and Qing Yang. "KCNQ/Kv7 channels as therapeutic target to treat neuropathic pain." In The Neurobiology, Physiology, and Psychology of Pain. Elsevier, 2022. http://dx.doi.org/10.1016/b978-0-12-820589-1.00001-4.

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Streszczenia konferencji na temat "KCNQ channels"

Okhalnik, A. D., M. S. Gavrish, S. A. Tutukov, and V. S. Tarabykin. "ROLE OF KCNQ3 IN THE FORMATION OF THE CEREBRAL CORTEX AND THE CORPUS CALLOSUM." In XI МЕЖДУНАРОДНАЯ КОНФЕРЕНЦИЯ МОЛОДЫХ УЧЕНЫХ: БИОИНФОРМАТИКОВ, БИОТЕХНОЛОГОВ, БИОФИЗИКОВ, ВИРУСОЛОГОВ, МОЛЕКУЛЯРНЫХ БИОЛОГОВ И СПЕЦИАЛИСТОВ ФУНДАМЕНТАЛЬНОЙ МЕДИЦИНЫ. IPC NSU, 2024. https://doi.org/10.25205/978-5-4437-1691-6-264.

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Identification of genes involved in the control of the cerebral cortex development is an an important task. Together with colleagues, we assessed the contribution of the voltage-gated K+ channel subunit (Kcnq3) to the formation of the corpus callosum, as well as its role in the migration and determination of the cell fate of neuronal progenitors.

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TOYODA, FUTOSHI, WEI-GUANG DING, ZANKOV DIMITAR, and HIROSHI MATSUURA. "DIFFERENTIAL EFFECTS OF MEFENAMIC ACID ON CARDIAC IKs AND THE KCNQ1/KCNE1 CHANNELS." In Proceedings of the 31st International Congress on Electrocardiology. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812702234_0072.

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AIZAWA, YOSHIYASU, LONG-MEI WU, KAZUO UEDA, et al. "KCNQ1 MUTATION CAUSING DOMINANT-NEGATIVE SUPPRESSION DUE TO DEFECTIVE CHANNEL TRAFFICKING UNDERLIES CARDIAC ARREST IN A PATIENT WITH LONG QT SYNDROME." In Proceedings of the 31st International Congress on Electrocardiology. WORLD SCIENTIFIC, 2005. http://dx.doi.org/10.1142/9789812702234_0078.

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