Relevant bibliographies by topics / Kca1.1

Academic literature on the topic 'Kca1.1'

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Published: 11 March 2023

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Journal articles on the topic "Kca1.1"

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Takai, Jun, Alexandra Santu, Haifeng Zheng, Sang Don Koh, Masanori Ohta, Linda M. Filimban, Vincent Lemaître, Ryutaro Teraoka, Hanjoong Jo, and Hiroto Miura. "Laminar shear stress upregulates endothelial Ca2+-activated K+ channels KCa2.3 and KCa3.1 via a Ca2+/calmodulin-dependent protein kinase kinase/Akt/p300 cascade." American Journal of Physiology-Heart and Circulatory Physiology 305, no. 4 (August 15, 2013): H484—H493. http://dx.doi.org/10.1152/ajpheart.00642.2012.

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In endothelial cells (ECs), Ca2+-activated K+ channels KCa2.3 and KCa3.1 play a crucial role in the regulation of arterial tone via producing NO and endothelium-derived hyperpolarizing factors. Since a rise in intracellular Ca2+ levels and activation of p300 histone acetyltransferase are early EC responses to laminar shear stress (LS) for the transcriptional activation of genes, we examined the role of Ca2+/calmodulin-dependent kinase kinase (CaMKK), the most upstream element of a Ca2+/calmodulin-kinase cascade, and p300 in LS-dependent regulation of KCa2.3 and KCa3.1 in ECs. Exposure to LS (15 dyn/cm2) for 24 h markedly increased KCa2.3 and KCa3.1 mRNA expression in cultured human coronary artery ECs (3.2 ± 0.4 and 45 ± 10 fold increase, respectively; P < 0.05 vs. static condition; n = 8–30), whereas oscillatory shear (OS; ± 5 dyn/cm2 × 1 Hz) moderately increased KCa3.1 but did not affect KCa2.3. Expression of KCa2.1 and KCa2.2 was suppressed under both LS and OS conditions, whereas KCa1.1 was slightly elevated in LS and unchanged in OS. Inhibition of CaMKK attenuated LS-induced increases in the expression and channel activity of KCa2.3 and KCa3.1, and in phosphorylation of Akt (Ser473) and p300 (Ser1834). Inhibition of Akt abolished the upregulation of these channels by diminishing p300 phosphorylation. Consistently, disruption of the interaction of p300 with transcription factors eliminated the induction of these channels. Thus a CaMKK/Akt/p300 cascade plays an important role in LS-dependent induction of KCa2.3 and KCa3.1 expression, thereby regulating EC function and adaptation to hemodynamic changes.
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Zhang, Jin, Susan T. Halm, and Dan R. Halm. "Role of the BK channel (KCa1.1) during activation of electrogenic K+ secretion in guinea pig distal colon." American Journal of Physiology-Gastrointestinal and Liver Physiology 303, no. 12 (December 15, 2012): G1322—G1334. http://dx.doi.org/10.1152/ajpgi.00325.2012.

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Secretagogues acting at a variety of receptor types activate electrogenic K+ secretion in guinea pig distal colon, often accompanied by Cl− secretion. Distinct blockers of KCa1.1 (BK, Kcnma1), iberiotoxin (IbTx), and paxilline inhibited the negative short-circuit current ( Isc) associated with K+ secretion. Mucosal addition of IbTx inhibited epinephrine-activated Isc (epi Isc) and transepithelial conductance (epi Gt) consistent with K+ secretion occurring via apical membrane KCa1.1. The concentration dependence of IbTx inhibition of epi Isc yielded an IC50 of 193 nM, with a maximal inhibition of 51%. Similarly, IbTx inhibited epi Gt with an IC50 of 220 nM and maximal inhibition of 48%. Mucosally added paxilline (10 μM) inhibited epi Isc and epi Gt by ∼50%. IbTx and paxilline also inhibited Isc activated by mucosal ATP, supporting apical KCa1.1 as a requirement for this K+ secretagogue. Responses to IbTx and paxilline indicated that a component of K+ secretion occurred during activation of Cl− secretion by prostaglandin-E2 and cholinergic stimulation. Analysis of KCa1.1α mRNA expression in distal colonic epithelial cells indicated the presence of the ZERO splice variant and three splice variants for the COOH terminus. The presence of the regulatory β-subunits KCaβ1 and KCaβ4 also was demonstrated. Immunolocalization supported the presence of KCa1.1α in apical and basolateral membranes of surface and crypt cells. Together these results support a cellular mechanism for electrogenic K+ secretion involving apical membrane KCa1.1 during activation by several secretagogue types, but the observed K+ secretion likely required the activity of additional K+ channel types in the apical membrane.
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Srivastava, Shekhar, Papiya Choudhury, Zhai Li, GongXin Liu, Vivek Nadkarni, Kyung Ko, William A. Coetzee, and Edward Y. Skolnik. "Phosphatidylinositol 3-Phosphate Indirectly Activates KCa3.1 via 14 Amino Acids in the Carboxy Terminus of KCa3.1." Molecular Biology of the Cell 17, no. 1 (January 2006): 146–54. http://dx.doi.org/10.1091/mbc.e05-08-0763.

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KCa3.1 is an intermediate conductance Ca2+-activated K+ channel that is expressed predominantly in hematopoietic cells, smooth muscle cells, and epithelia where it functions to regulate membrane potential, Ca2+ influx, cell volume, and chloride secretion. We recently found that the KCa3.1 channel also specifically requires phosphatidylinositol-3 phosphate [PI(3)P] for channel activity and is inhibited by myotubularin-related protein 6 (MTMR6), a PI(3)P phosphatase. We now show that PI(3)P indirectly activates KCa3.1. Unlike KCa3.1 channels, the related KCa2.1, KCa2.2, or KCa2.3 channels do not require PI(3)P for activity, suggesting that the KCa3.1 channel has evolved a unique means of regulation that is critical for its biological function. By making chimeric channels between KCa3.1 and KCa2.3, we identified a stretch of 14 amino acids in the carboxy-terminal calmodulin binding domain of KCa3.1 that is sufficient to confer regulation of KCa2.3 by PI(3)P. However, mutation of a single potential phosphorylation site in these 14 amino acids did not affect channel activity. These data together suggest that PI(3)P and these 14 amino acids regulate KCa3.1 channel activity by recruiting an as yet to be defined regulatory subunit that is required for Ca2+ gating of KCa3.1.
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Nakamoto, Tetsuji, Victor G. Romanenko, Atsushi Takahashi, Ted Begenisich, and James E. Melvin. "Apical maxi-K (KCa1.1) channels mediate K+ secretion by the mouse submandibular exocrine gland." American Journal of Physiology-Cell Physiology 294, no. 3 (March 2008): C810—C819. http://dx.doi.org/10.1152/ajpcell.00511.2007.

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The exocrine salivary glands of mammals secrete K+ by an unknown pathway that has been associated with HCO3− efflux. However, the present studies found that K+ secretion in the mouse submandibular gland did not require HCO3−, demonstrating that neither K+/HCO3− cotransport nor K+/H+ exchange mechanisms were involved. Because HCO3− did not appear to participate in this process, we tested whether a K channel is required. Indeed, K+ secretion was inhibited >75% in mice with a null mutation in the maxi-K, Ca2+-activated K channel (KCa1.1) but was unchanged in mice lacking the intermediate-conductance IKCa1 channel (KCa3.1). Moreover, paxilline, a specific maxi-K channel blocker, dramatically reduced the K+ concentration in submandibular saliva. The K+ concentration of saliva is well known to be flow rate dependent, the K+ concentration increasing as the flow decreases. The flow rate dependence of K+ secretion was nearly eliminated in K Ca 1.1 null mice, suggesting an important role for KCa1.1 channels in this process as well. Importantly, a maxi-K-like current had not been previously detected in duct cells, the theoretical site of K+ secretion, but we found that KCa1.1 channels localized to the apical membranes of both striated and excretory duct cells, but not granular duct cells, using immunohistochemistry. Consistent with this latter observation, maxi-K currents were not detected in granular duct cells. Taken together, these results demonstrate that the secretion of K+ requires and is likely mediated by KCa1.1 potassium channels localized to the apical membranes of striated and excretory duct cells in the mouse submandibular exocrine gland.
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Stoneking, Colin J., Oshini Shivakumar, David Nicholson Thomas, William H. Colledge, and Michael J. Mason. "Voltage dependence of the Ca2+-activated K+channel KCa3.1 in human erythroleukemia cells." American Journal of Physiology-Cell Physiology 304, no. 9 (May 1, 2013): C858—C872. http://dx.doi.org/10.1152/ajpcell.00368.2012.

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We have isolated a K+-selective, Ca2+-dependent whole cell current and single-channel correlate in the human erythroleukemia (HEL) cell line. The whole cell current was inhibited by the intermediate-conductance KCa3.1 inhibitors clotrimazole, TRAM-34, and charybdotoxin, unaffected by the small-conductance KCa2 family inhibitor apamin and the large-conductance KCa1.1 inhibitors paxilline and iberiotoxin, and augmented by NS309. The single-channel correlate of the whole cell current was blocked by TRAM-34 and clotrimazole, insensitive to paxilline, and augmented by NS309 and had a single-channel conductance in physiological K+gradients of ∼9 pS. RT-PCR revealed that the KCa3.1 gene, but not the KCa1.1 gene, was expressed in HEL cells. The KCa3.1 current, isolated in HEL cells under whole cell patch-clamp conditions, displayed an activated current component during depolarizing voltage steps from hyperpolarized holding potentials and tail currents upon repolarization, consistent with voltage-dependent modulation. This activated current increased with increasing voltage steps above −40 mV and was sensitive to inhibition by clotrimazole, TRAM-34, and charybdotoxin and insensitive to apamin, paxilline, and iberiotoxin. In single-channel experiments, depolarization resulted in an increase in open channel probability ( Po) of KCa3.1, with no increase in channel number. The voltage modulation of Powas an increasing monotonic function of voltage. In the absence of elevated Ca2+, voltage was ineffective at inducing channel activity in whole cell and single-channel experiments. These data indicate that KCa3.1 in HEL cells displays a unique form of voltage dependence modulating Po.
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Ohya, Susumu, Junko Kajikuri, Kyoko Endo, Hiroaki Kito, and Miki Matsui. "KCa1.1 K+ Channel Inhibition Overcomes Resistance to Antiandrogens and Doxorubicin in a Human Prostate Cancer LNCaP Spheroid Model." International Journal of Molecular Sciences 22, no. 24 (December 17, 2021): 13553. http://dx.doi.org/10.3390/ijms222413553.

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Several types of K+ channels play crucial roles in tumorigenicity, stemness, invasiveness, and drug resistance in cancer. Spheroid formation of human prostate cancer (PC) LNCaP cells with ultra-low attachment surface cultureware induced the up-regulation of cancer stem cell markers, such as NANOG, and decreased the protein degradation of the Ca2+-activated K+ channel KCa1.1 by down-regulating the E3 ubiquitin ligase, FBXW7, compared with LNCaP monolayers. Accordingly, KCa1.1 activator-induced hyperpolarizing responses were larger in isolated cells from LNCaP spheroids. The pharmacological inhibition of KCa1.1 overcame the resistance of LNCaP spheroids to antiandrogens and doxorubicin (DOX). The protein expression of androgen receptors (AR) was significantly decreased by LNCaP spheroid formation and reversed by KCa1.1 inhibition. The pharmacological and genetic inhibition of MDM2, which may be related to AR protein degradation in PC stem cells, revealed that MDM2 was responsible for the acquisition of antiandrogen resistance in LNCaP spheroids, which was overcome by KCa1.1 inhibition. Furthermore, a member of the multidrug resistance-associated protein subfamily of ABC transporters, MRP5 was responsible for the acquisition of DOX resistance in LNCaP spheroids, which was also overcome by KCa1.1 inhibition. Collectively, the present results suggest the potential of KCa1.1 in LNCaP spheroids, which mimic PC stem cells, as a therapeutic target for overcoming antiandrogen- and DOX-resistance in PC cells.
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Rehak, Renata, Theodore M. Bartoletti, Jordan D. T. Engbers, Geza Berecki, Ray W. Turner, and Gerald W. Zamponi. "Low Voltage Activation of KCa1.1 Current by Cav3-KCa1.1 Complexes." PLoS ONE 8, no. 4 (April 23, 2013): e61844. http://dx.doi.org/10.1371/journal.pone.0061844.

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Sones, WR, N. Leblanc, and IA Greenwood. "Inhibition of vascular calcium-gated chloride currents by blockers of KCa1.1, but not by modulators of KCa2.1 or KCa2.3 channels." British Journal of Pharmacology 158, no. 2 (July 23, 2009): 521–31. http://dx.doi.org/10.1111/j.1476-5381.2009.00332.x.

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Xin, Wenkuan, Qiuping Cheng, Rupal P. Soder, Eric S. Rovner, and Georgi V. Petkov. "Constitutively active phosphodiesterase activity regulates urinary bladder smooth muscle function: critical role of KCa1.1 channel." American Journal of Physiology-Renal Physiology 303, no. 9 (November 1, 2012): F1300—F1306. http://dx.doi.org/10.1152/ajprenal.00351.2012.

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Pharmacological blockade of cyclic nucleotide phosphodiesterase (PDE) can relax human urinary bladder smooth muscle (UBSM); however, the underlying cellular mechanism is unknown. In this study, we investigated the effects of PDE pharmacological blockade on human UBSM excitability, spontaneous and nerve-evoked contractility, and determined the underlying cellular mechanism mediating these effects. Patch-clamp electrophysiological experiments showed that 3-isobutyl-1-methylxanthine (10 μM), a nonselective PDE inhibitor, caused ∼3.6-fold increase in the transient KCa1.1 channel current frequency and ∼2.5-fold increase in the spontaneous transient hyperpolarization frequency in UBSM-isolated cells. PDE blockade also caused ∼5.6-mV hyperpolarization of the UBSM cell membrane potential. Blocking the KCa1.1 channels with paxilline abolished the spontaneous transient hyperpolarization and the hyperpolarization effect of PDE blockade on the UBSM cell membrane potential. Live cell Ca2+-imaging experiments showed that PDE blockade significantly decreased the global intracellular Ca2+ levels. Attenuation of PDE activity significantly reduced spontaneous phasic contraction amplitude, muscle force integral, duration, frequency, and muscle tone of human UBSM isolated strips. Blockade of PDE also significantly reduced the contraction amplitude, muscle force integral, and duration of the nerve-evoked contractions induced by 20-Hz electrical field stimulation. Pharmacological inhibition of KCa1.1 channels abolished the relaxation effects of PDE blockade on both spontaneous and nerve-evoked contractions in human UBSM-isolated strips. Our data provide strong evidence that in human UBSM PDE is constitutively active, thus maintaining spontaneous UBSM contractility. PDE blockade causes relaxation of human UBSM by increasing transient KCa1.1 channel current activity, hyperpolarizing cell membrane potential, and decreasing the global intracellular Ca2+.
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Li, Bai-Yan, Patricia Glazebrook, Diana L. Kunze, and John H. Schild. "KCa1.1 channel contributes to cell excitability in unmyelinated but not myelinated rat vagal afferents." American Journal of Physiology-Cell Physiology 300, no. 6 (June 2011): C1393—C1403. http://dx.doi.org/10.1152/ajpcell.00278.2010.

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High conductance calcium-activated potassium (BKCa) channels can modulate cell excitability and neurotransmitter release at synaptic and afferent terminals. BKCa channels are present in primary afferents of most, if not, all internal organs and are an intriguing target for pharmacological manipulation of visceral sensation. Our laboratory has a long-standing interest in the neurophysiological differences between myelinated and unmyelinated visceral afferent function. Here, we seek to determine whether there is a differential distribution of BKCa channels in myelinated and unmyelinated vagal afferents. Immunocytochemistry studies with double staining for the BK-type KCa1.1 channel protein and isolectin B4 (IB4), a reliable marker of unmyelinated peripheral afferents, reveal a pattern of IB4 labeling that strongly correlates with the expression of the KCa1.1 channel protein. Measures of cell size and immunostaining intensity for KCa1.1 and IB4 cluster into two statistically distinct ( P < 0.05) populations of cells. Smaller diameter neurons most often presented with strong IB4 labeling and are presumed to be unmyelinated ( n = 1,390) vagal afferents. Larger diameter neurons most often lacked or exhibited a very weak IB4 labeling and are presumed to be myelinated ( n = 58) vagal afferents. Complimentary electrophysiological studies reveal that the BKCa channel blockers charybdotoxin (ChTX) and iberiotoxin (IbTX) bring about a comparable elevation in excitability and action potential widening in unmyelinated neurons but had no effect on the excitability of myelinated vagal afferents. This study is the first to demonstrate using combined immunohistochemical and electrophysiological techniques that KCa1.1 channels are uniquely expressed in unmyelinated C-type vagal afferents and do not contribute to the dynamic discharge characteristics of myelinated A-type vagal afferents. This unique functional distribution of BK-type KCa channels may provide an opportunity for afferent selective pharmacological intervention across a wide range of visceral pathophysiologies, particularly those with a reflexogenic etiology and pain.
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Dissertations / Theses on the topic "Kca1.1"

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Rappert, Denis [Verfasser], and Ralf [Akademischer Betreuer] Köhler. "Die Rolle der Ca2+-aktivierten K+-Kanäle KCa3.1 und KCa2.3 bei retinalen Angiogeneseprozessen / Denis Rappert. Betreuer: Ralf Köhler." Marburg : Philipps-Universität Marburg, 2011. http://d-nb.info/1013288335/34.

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Huang, Chunling. "Targeting KCa3.1 in diabetic tubulointerstitial fibrosis." Thesis, The University of Sydney, 2014. http://hdl.handle.net/2123/12155.

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KCa3.1, a potassium channel protein, mediates cellular signaling processes associated with dysfunction of vasculature. However, the role of KCa3.1 in diabetic nephropathy has not been studied. In this thesis, human proximal tubular cells and fibroblasts as well as two diabetic mouse models: KCa3.1-/- and eNOS-/- treated with KCa3.1 inhibitor TRAM34, were used to determine the therapeutic effect of KCa3.1 in diabetic tubulointerstitial fibrosis. Our results show that blockade of KCa3.1 by gene knockout or by concurrent exposure to the inhibitor TRAM34 reversed the diabetic-induced upregulation of inflammation and fibrotic responses through a TGF-β1/Smad dependent signaling pathway. We also demonstrated a key role of KCa3.1 in mediating TGF-β1 induced MCP-1 expression in renal proximal tubular cells via Smad3, p38 and ERK1/2 MAPK signaling pathways. In addition, our studies also demonstrate that blocking the KCa3.1 channel inhibits the NF-κB pathway, resulting in downregulation of the inflammatory marker CCL20. Our preliminary studies have further shown that blockade of KCa3.1 is likely to exert its anti-fibrotic effects through normalization of the autophagocytic pathways, and by inhibition of fibroblast activation. Collectively, the data shown in the thesis uniquely demonstrates that blockade of KCa3.1 is able to prevent the development of diabetic nephropathy.
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Hellwig, Nicole. "Funktionelle Bedeutung des thrombozytären Kalzium abhängigen Kaliumkanals KCa3.1." Diss., lmu, 2012. http://nbn-resolving.de/urn:nbn:de:bvb:19-143388.

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Roach, Katy Morgan. "The role of the K⁺ channel KCa3.1 in idiopathic pulmonary fibrosis." Thesis, University of Leicester, 2013. http://hdl.handle.net/2381/27825.

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Idiopathic pulmonary fibrosis (IPF) is a common disease with a median survival of only 3 years. There is no effective treatment. IPF is characterized by myofibroblast accumulation and progressive lung scarring. The Ca²⁺-activated K⁺ channel KCa3.1 modulates the activity of several structural and inflammatory cells which play important roles in model diseases characterized by tissue remodelling and fibrosis. We hypothesise that KCa3.1-dependent cell processes are a common denominator in IPF. KCa3.1 expression and function were examined in human myofibroblasts derived from IPF and non-fibrotic (NFC) donors. Myofibroblasts grown in vitro were characterised by western blot, immunofluorescence, RT-PCR and patch clamp electrophysiology to determine KCa3.1 channel expression. Wound healing, collagen secretion and contraction assays were performed using the pro-fibrotic mediators TGFβ1 and bFGF and two specific KCa3.1 blockers (TRAM-34, ICA-17043 [Senicapoc]). Both NFC and IPF myofibroblasts expressed KCa3.1 channel mRNA and protein. Using the KCa3.1 channel opener 1-EBIO, KCa3.1 ion currents were elicited in 59% of NFC and 77% of IPF myofibroblasts tested (P=0.0411). These currents were blocked by TRAM-34 (200 nM). The 1-EBIO-induced currents were significantly larger in IPF cells compared to NFC cells (P=0.0078). TGFβ1 and bFGF increased KCa3.1 channel expression. TRAM-34 and ICA-17043 dose-dependently attenuated wound healing, TGFβ1-dependent collagen secretion and bFGF- and TGFβ1-dependent contraction. We show for the first time that human lung myofibroblasts express the KCa3.1 K⁺ channel. KCa3.1 channel block attenuates pro-fibrotic myofibroblast function. These findings raise the possibility that blocking the KCa3.1 channel will inhibit pathological myofibroblast function in IPF, and thus offer a novel approach to IPF therapy.
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Hellwig, Nicole [Verfasser], and Florian [Akademischer Betreuer] Krötz. "Funktionelle Bedeutung des thrombozytären Kalzium abhängigen Kaliumkanals KCa3.1 / Nicole Hellwig. Betreuer: Florian Krötz." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2012. http://d-nb.info/1023660660/34.

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Ongerth, Tanja. "Untersuchung erkrankungsmodifizierender und antiepileptogener Effekte eines Blockers des Kaliumkanals KCa3.1 in chronischen Epilepsiemodellen." Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-167686.

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Rieke, Marius Andreas [Verfasser], and Albrecht [Akademischer Betreuer] Schwab. "Die Rolle mitochondrialer KCa3.1-Kanäle in Lungenkrebszellen / Marius Andreas Rieke ; Betreuer: Albrecht Schwab." Münster : Universitäts- und Landesbibliothek Münster, 2020. http://d-nb.info/1216947740/34.

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Radtke, Josephine [Verfasser]. "Vasodilatation und Blutdrucksenkung durch Aktivierung des Kaliumkanals KCa3.1 mit SKA-31 ist unabhängig von Connexin40 / Josephine Radtke." Lübeck : Zentrale Hochschulbibliothek Lübeck, 2014. http://d-nb.info/1058582437/34.

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Schultz, Tim [Verfasser], and Ralf PD Dr [Akademischer Betreuer] Köhler. "Untersuchung zur pharmakologischen Aktivierung arterieller KCa3.1-Kanäle durch SKA-31 / Tim Schultz. Betreuer: Ralf PD Dr. Köhler." Marburg : Philipps-Universität Marburg, 2011. http://d-nb.info/1013255151/34.

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Ongerth, Tanja [Verfasser], and Heidrun [Akademischer Betreuer] Potschka. "Untersuchung erkrankungsmodifizierender und antiepileptogener Effekte eines Blockers des Kaliumkanals KCa3.1 in chronischen Epilepsiemodellen / Tanja Ongerth. Betreuer: Heidrun Potschka." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2014. http://d-nb.info/1049153200/34.

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Book chapters on the topic "Kca1.1"

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Devor, Daniel C., Claudia A. Bertuccio, and Kirk L. Hamilton. "KCa3.1 in Epithelia." In Ion Channels and Transporters of Epithelia in Health and Disease, 659–705. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-3366-2_20.

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Devor, Daniel C., Patrick H. Thibodeau, and Kirk L. Hamilton. "KCa3.1 in Epithelia." In Studies of Epithelial Transporters and Ion Channels, 893–948. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-55454-5_22.

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Villars, P., K. Cenzual, J. Daams, R. Gladyshevskii, O. Shcherban, V. Dubenskyy, N. Melnichenko-Koblyuk, et al. "KCa10[VO4]7." In Landolt-Börnstein - Group III Condensed Matter, 625. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-44752-8_525.

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Villars, P., K. Cenzual, J. Daams, R. Gladyshevskii, O. Shcherban, V. Dubenskyy, N. Melnichenko-Koblyuk, et al. "KCa12[SiO4]4[SO4]2O2F." In Structure Types. Part 5: Space Groups (173) P63 - (166) R-3m, 877. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-46933-9_738.

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Banderali, Umberto, Line Garneau, Manuel Simoes, Hélène Klein, and Rémy Sauvé. "The KCa3.1 Channel in Endothelial Cells as New Target for an EDHF-Based Control of Vascular Tone: From Structure to Regulation and Pharmacological Properties." In Signal Transduction in the Cardiovascular System in Health and Disease, 357–74. Boston, MA: Springer US, 2008. http://dx.doi.org/10.1007/978-0-387-09552-3_19.

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Anukam, Kingsley C. "Probiotic Research Studies That Led to the Discovery of Lactobacillus pentosus KCA1." In Microbiomes and Emerging Applications, 121–35. Boca Raton: CRC Press, 2022. http://dx.doi.org/10.1201/9781003180241-7.

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"BK Channels (KCa1.1)." In Encyclopedia of Computational Neuroscience, 417. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4614-6675-8_100077.

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"Kca1-1." In Encyclopedia of Signaling Molecules, 2763. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_105406.

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Garneau, Line, Hélène Klein, Lucie Parent, and Rémy Sauvé. "Toward the Rational Design of Constitutively Active KCa3.1 Mutant Channels." In Methods in Enzymology, 437–57. Elsevier, 2010. http://dx.doi.org/10.1016/b978-0-12-381296-4.00024-5.

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Conference papers on the topic "Kca1.1"

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SINGH, SHAILENDRA R., GLEN CRUSE, S. MARK DUFFY, Ruth Saunders, CAMILLE DOE, CHRIS BRIGHTLING, and PETER BRADDING. "Functional KCa3.1 K+ Channels Are Pivotal For Human Fibrocyte Migration." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2705.

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Roach, K. M., and P. Bradding. "KCa3.1 channel inhibition prevents fibrotic responses in a human lung explant model." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa929.

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Roach, Katy M., Malcolm C. Shepherd, Sumir R. Sabir, Heike Wulff, William Coward, Carol Feghali-Bostwick, S. M. Duffy, C. McSharry, and Peter Bradding. "The K+ Channel KCa3.1 As A Novel Target For Idiopathic Pulmonary Fibrosis." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1952.

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Naveed, Shams-un-nisa, Debbie Clements, Simon Johnson, Katy Roach, and Peter Bradding. "KCa3.1 ion channel is expressed by component cells of lymphangioleiomyomatosis (LAM) nodules." In ERS International Congress 2019 abstracts. European Respiratory Society, 2019. http://dx.doi.org/10.1183/13993003.congress-2019.pa3686.

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Fraser, Paul, Anas Bani Khalaf, Giovanni Mann, Matthew Smith, and Geraldine Clough. "10 Evidence that altered redox status results in KCa3.1 channel reduced endothelial cell surface expression." In Abstracts from the Fellowship of Postgraduate Medicine Centenary Conference 2018: Transforming Health and Health Care. The Fellowship of Postgraduate Medicine, 2018. http://dx.doi.org/10.1136/postgradmedj-2018-fpm.21.

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Šutovská, M., J. Mažerik, and S. Fraňová. "KCa3.1 inhibition possesses complex anti-asthmatic effect in a guinea pig model of chronic asthma." In ERS International Congress 2022 abstracts. European Respiratory Society, 2022. http://dx.doi.org/10.1183/13993003.congress-2022.4632.

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Naveed, S., D. Clements, SR Johnson, and P. Bradding. "S65 The calcium-activated K+ channel KCa3.1 is expressed by component cells of lymphangioleiomyomatosis (LAM) nodules." In British Thoracic Society Winter Meeting 2018, QEII Centre, Broad Sanctuary, Westminster, London SW1P 3EE, 5 to 7 December 2018, Programme and Abstracts. BMJ Publishing Group Ltd and British Thoracic Society, 2018. http://dx.doi.org/10.1136/thorax-2018-212555.71.

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Organ, Louise, Emmanuel Koumoundouros, Barbara Bacci, Wayne Kimpton, Chrishan Samuel, Glen Westall, Ian Glaspole, Ken Snibson, and Jade Jaffar. "LATE-BREAKING ABSTRACT: KCa3.1 ion channel-blockade reduces pulmonary fibrotic responses via the inhibition of fibroblast proliferation." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa4044.

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Perera, K. Udari Eshani, Louise Organ, Habtamu Biyazen Derseh, Sasika Nimanthi Dewage, Andrew Stent, and Ken Snibson. "Effect of in vivo blockade of the KCa3.1 ion channel on type II alveolar epithelial cell turnover in pulmonary fibrosis." In ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa3715.

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Van Der Velden, Joanne L., Donna Barker, Garry Barcham, Emmanuel Koumoundouros, Heike Wulff, Neil Castle, Peter Bradding, and Ken Snibson. "Kca3.1 Blockade Improves Lung Function And Retards Allergen-Induced Increases In Mast Cell Density In A Sheep Model Of Chronic Asthma." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a3602.

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