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Academic literature on the topic '(Na+,K+)-dependent ATPase'

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Published: 4 June 2021
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Journal articles on the topic "(Na+,K+)-dependent ATPase"

1

Aizman, R. I., G. Celsi, L. Grahnquist, Z. M. Wang, Y. Finkel, and A. Aperia. "Ontogeny of K+ transport in rat distal colon." American Journal of Physiology-Gastrointestinal and Liver Physiology 271, no. 2 (August 1, 1996): G268—G274. http://dx.doi.org/10.1152/ajpgi.1996.271.2.g268.

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Infants need to retain more K+ than adults to avoid growth retardation. Since the K+ requirements are different in infants (I) and in adults (A), the mechanisms regulating K+ homeostasis should also be different. The colon plays an important role for the regulation of K+ homeostasis. Colonic K+ transport is bidirectional. In this study we have examined the development of colonic K+ transport with special reference to the contribution of different K(+)-transporting pathways. The net colonic K+ uptake, as determined by in vivo perfusion studies and by 86Rb uptake, was significantly higher in I than in A rats. In both I and A colon, approximately 80% of total 86Rb uptake was dependent on vanadate-sensitive P-type adenosinetriphosphatases (ATPases), but the contribution of these different ATPases changes during development. The activity of colonic Na(+)-K(+)-ATPase, measured as ouabain-sensitive Na(+)-dependent ATP hydrolysis and as 86Rb uptake, was lower in I than in A rats. In contrast, the activity of K(+)-ATPases located in apical membrane and measured as ouabain insensitive and SCH-28080 sensitive, as ouabain-sensitive Na(+)-independent ATP hydrolysis, and as 86Rb uptake was significantly higher in I than in A rats. The ratio between apically located K(+)-ATPases and basolateral Na(+)-K(+)-ATPase activities was almost 3.2-fold higher in I than in A colon. We identified with Northern blot the expression of the colonic H(+)-K(+)-ATPase and the Na(+)-K(+)-ATPase alpha-subunits. The alpha-mRNA expression of both ATPases was significantly higher in I than in A rats. The pH and K+ sensitivity of the ouabain-insensitive, SCH-28080-sensitive K(+)-ATPase was the same in I and A colons. In conclusion, the relative activity of apical K+ absorbing ATPases is higher in the I than in the A colon, which should aid infants in retaining K+.
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2

Benders, A. A., J. A. Timmermans, A. Oosterhof, H. J. Ter Laak, T. H. M. S. M. van Kuppevelt, R. A. Wevers, and J. H. Veerkamp. "Deficiency of Na+/K+-ATPase and sarcoplasmic reticulum Ca2+-ATPase in skeletal muscle and cultured muscle cells of myotonic dystrophy patients." Biochemical Journal 293, no. 1 (July 1, 1993): 269–74. http://dx.doi.org/10.1042/bj2930269.

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Since defective regulation of ion transport could initiate or contribute to the abnormal cellular function in myotonic dystrophy (MyD), Na+/K(+)-ATPase and sarcoplasmic reticulum (SR) Ca(2+)-ATPase were examined in skeletal muscle and cultured skeletal muscle cells of controls and MyD patients. Na+/K(+)-ATPase was investigated by measuring ouabain binding and the activities of Na+/K(+)-ATPase and K(+)-dependent 3-O-methylfluorescein phosphate (3-O-MFPase). SR Ca(2+)-ATPase was analysed by e.l.i.s.a., Ca(2+)-dependent phosphorylation and its activities with ATP and 3-O-methylfluorescein phosphatase (3-O-MFP). In MyD muscle the K(+)-dependent 3-O-MFPase activity and the activity and concentration of SR Ca(2+)-ATPase were decreased by 40%. In cultured muscle cells from MyD patients the activities as well as the concentration of both Na+/K(+)-ATPase and SR Ca(2+)-ATPase were reduced by about 30-40%. The ouabain-binding constant and the molecular activities, i.e. catalytic-centre activities with ATP or 3-O-MFP, of Na+/K(+)-ATPase and SR Ca(2+)-ATPase were similar in muscle as well as in cultured cells from both controls and MyD patients. Thus the decreased activity of both ATPases in MyD muscle is caused by a reduction in the number of their molecules. To check whether the deficiency of ATP-dependent ion pumps is a general feature of the pathology of MyD, we examined erythrocytes from the same patients. In these cells the Ca2+ uptake rate and the Ca(2+)-ATPase activity were lower than in controls, but the Ca(2+)-ATPase concentration was normal. Thus the reduced Ca(2+)-ATPase activity is caused by a decrease in the molecular activity of the ion pump. The Na+/K(+)-ATPase activity is also lower in erythrocytes of MyD patients. It is concluded that the observed alterations in ion pumps may contribute to the pathological phenomena in the muscle and other tissues in patients with MyD.
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3

Mathews, P. M., D. Claeys, F. Jaisser, K. Geering, J. D. Horisberger, J. P. Kraehenbuhl, and B. C. Rossier. "Primary structure and functional expression of the mouse and frog alpha-subunit of the gastric H(+)-K(+)-ATPase." American Journal of Physiology-Cell Physiology 268, no. 5 (May 1, 1995): C1207—C1214. http://dx.doi.org/10.1152/ajpcell.1995.268.5.c1207.

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The H(+)-K(+)-ATPase of the gastric parietal cells is responsible for the acidification of the stomach lumen. This heterodimeric protein belongs to the family of cation-translocating P-type ATPases, which includes the closely related Na(+)-ATPase. We have cloned the alpha-subunit cDNA of the Xenopus and murine gastric H(+)-K(+)-ATPase (alpha H-K). We have expressed Xenopus and murine alpha H-K along with the previously cloned gastric H(+)-K(+)-ATPase beta-subunit of rabbit (beta H-K) in Xenopus oocytes by cRNA injection. An antibody directed against the beta H-K coimmunoprecipitates under nondenaturing conditions the alpha H-K of both species, demonstrating assembly of the alpha/beta complex. Additionally, we demonstrate the presence of K(+)-transporting H(+)-K(+)-ATPase in the plasma membrane of oocytes by 86Rb- uptake. The H(+)-K(+)-ATPase-mediated K+ uptake was inhibited by the gastric H(+)-K(+)-ATPase inhibitor Sch-28080, but not by ouabain, and shows K(+)-dependent activation (K1/2 approximately 2 mM). Furthermore, H(+)-K(+)-ATPase-expressing oocytes show a Sch-28080 inhibitable proton extrusion. Our data indicate that the expressed H(+)-K(+)-ATPase behaves functionally in oocytes as in the gastric gland.
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4

Missiaen, L., F. Wuytack, H. De Smedt, M. Vrolix, and R. Casteels. "AlF4- reversibly inhibits ‘P’-type cation-transport ATPases, possibly by interacting with the phosphate-binding site of the ATPase." Biochemical Journal 253, no. 3 (August 1, 1988): 827–33. http://dx.doi.org/10.1042/bj2530827.

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The only known cellular action of AlF4- is to stimulate the G-proteins. The aim of the present work is to demonstrate that AlF4- also inhibits ‘P’-type cation-transport ATPases. NaF plus AlCl3 completely and reversibly inhibits the activity of the purified (Na+ + K+)-ATPase (Na+- and K+-activated ATPase) and of the purified plasmalemmal (Ca2+ + Mg2+)-ATPase (Ca2+-stimulated and Mg2+-dependent ATPase). It partially inhibits the activity of the sarcoplasmic-reticulum (Ca2+ + Mg2+)-ATPase, whereas it does not affect the mitochondrial H+-transporting ATPase. The inhibitory substances are neither F- nor Al3+ but rather fluoroaluminate complexes. Because AlF4- still inhibits the ATPase in the presence of guanosine 5′-[beta-thio]diphosphate, and because guanosine 5′-[beta gamma-imido]triphosphate does not inhibit the ATPase, it is unlikely that the inhibition could be due to the activation of an unknown G-protein. The time course of inhibition and the concentrations of NaF and AlCl3 required for this inhibition differ for the different ATPases. AlF4- inhibits the (Na+ + K+)-ATPase and the plasmalemmal (Ca2+ + Mg2+)-ATPase noncompetitively with respect to ATP and to their respective cationic substrates, Na+ and Ca2+. AlF4- probably binds to the phosphate-binding site of the ATPase, as the Ki for inhibition of the (Na+ + K+)-ATPase and of the plasmalemmal (Ca2+ + Mg2+)-ATPase is shifted in the presence of respectively 5 and 50 mM-Pi to higher concentrations of NaF. Moreover, AlF4- inhibits the K+-activated p-nitrophenylphosphatase of the (Na+ + K+)-ATPase competitively with respect to p-nitrophenyl phosphate. This AlF4- –induced inhibition of ‘P’-type cation-transport ATPases warns us against explaining all the effects of AlF4- on intact cells by an activation of G-proteins.
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5

Asano, Shinji, Satomi Hoshina, Yumi Nakaie, Toshiyuki Watanabe, Michihiko Sato, Yuichi Suzuki, and Noriaki Takeguchi. "Functional expression of putative H+-K+-ATPase from guinea pig distal colon." American Journal of Physiology-Cell Physiology 275, no. 3 (September 1, 1998): C669—C674. http://dx.doi.org/10.1152/ajpcell.1998.275.3.c669.

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A guinea pig cDNA encoding the putative colonic H+-K+-ATPase α-subunit (T. Watanabe, M. Sato, K. Kaneko, T. Suzuki, T. Yoshida, and Y. Suzuki; GenBank accession no. D21854 ) was functionally expressed in HEK-293, a human kidney cell line. The cDNA for the putative colonic H+-K+-ATPase was cotransfected with cDNA for either rabbit gastric H+-K+-ATPase or TorpedoNa+-K+-ATPase β-subunit. In both expressions, Na+-independent, K+-dependent ATPase (K+-ATPase) activity was detected in the membrane fraction of the cells, with a Michaelis-Menten constant for K+ of 0.68 mM. The expressed K+-ATPase activity was inhibited by ouabain, with its IC50 value being 52 μM. However, the activity was resistant to Sch-28080, an inhibitor specific for gastric H+-K+-ATPase. The ATPase was not functionally expressed in the absence of the β-subunits. Therefore, it is concluded that the cDNA encodes the catalytic subunit (α-subunit) of the colonic H+-K+-ATPase. Although the β-subunit of the colonic H+-K+-ATPase has not been identified yet, both gastric H+-K+-ATPase and Na+-K+-ATPase β-subunits were found to act as a surrogate for the colonic β-subunit for the functional expression of the ATPase. The present colonic H+-K+-ATPase first expressed in mammalian cells showed the highest ouabain sensitivity in expressed colonic H+-K+-ATPases so far reported (rat colonic in Xenopus oocytes had an IC 50 = 0.4–1 mM; rat colonic in Sf9 cells had no ouabain sensitivity).
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6

Kraut, J. A., F. Starr, G. Sachs, and M. Reuben. "Expression of gastric and colonic H(+)-K(+)-ATPase in the rat kidney." American Journal of Physiology-Renal Physiology 268, no. 4 (April 1, 1995): F581—F587. http://dx.doi.org/10.1152/ajprenal.1995.268.4.f581.

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Enzymatic and microperfusion studies have indicated that an ATP-dependent H+/K+ exchange process is present in the collecting duct of the mammalian kidney. Immunochemical staining has also provided evidence for expression of a gastric-type H(+)-K+ adenosine triphosphatase (H(+)-K(+)-ATPase). Rat kidney mRNA was probed with use of the polymerase chain reaction (PCR) to determine the presence of an H(+)-K(+)-ATPase. cDNA made with mRNA isolated from the kidneys of rats maintained on a low-K diet was used as template in PCR reactions with primers encompassing the cDNA sequence of the alpha-subunit of the gastric H(+)-K(+)-ATPase and the 5' and 3' ends of the colonic H(+)-K(+)-ATPase. The resulting products, 300–700 bp in size, hybridized with probes directed against either the gastric or colonic sequences of the H(+)-K(+)-ATPase. Sequencing of the individual PCR products showed identity with the appropriate regions of the alpha-subunits of the gastric H(+)-K(+)-ATPase and colonic H(+)-K(+)-ATPase. These data indicate that the rat kidney expresses mRNAs encoding both gastric and colonic H(+)-K(+)-ATPases.
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7

Crambert, Gilles, Ciming Li, Dirk Claeys, and Käthi Geering. "FXYD3 (Mat-8), a New Regulator of Na,K-ATPase." Molecular Biology of the Cell 16, no. 5 (May 2005): 2363–71. http://dx.doi.org/10.1091/mbc.e04-10-0878.

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Four of the seven members of the FXYD protein family have been identified as specific regulators of Na,K-ATPase. In this study, we show that FXYD3, also known as Mat-8, is able to associate with and to modify the transport properties of Na,K-ATPase. In addition to this shared function, FXYD3 displays some uncommon characteristics. First, in contrast to other FXYD proteins, which were shown to be type I membrane proteins, FXYD3 may have a second transmembrane-like domain because of the presence of a noncleavable signal peptide. Second, FXYD3 can associate with Na,K- as well as H,K-ATPases when expressed in Xenopus oocytes. However, in situ (stomach), FXYD3 is associated only with Na,K-ATPase because its expression is restricted to mucous cells in which H,K-ATPase is absent. Coexpressed in Xenopus oocytes, FXYD3 modulates the glycosylation processing of the β subunit of X,K-ATPase dependent on the presence of the signal peptide. Finally, FXYD3 decreases both the apparent affinity for Na+ and K+ of Na,K-ATPase.
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8

Ono, S., J. Guntupalli, and T. D. DuBose. "Role of H(+)-K(+)-ATPase in pHi regulation in inner medullary collecting duct cells in culture." American Journal of Physiology-Renal Physiology 270, no. 5 (May 1, 1996): F852—F861. http://dx.doi.org/10.1152/ajprenal.1996.270.5.f852.

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Studies in inner medullary collecting duct (IMCD) cells in primary culture have proposed two mechanisms for Na(+)-independent hydrogen ion transport: an H(+)-adenosinetriphosphatase (H(+)-ATPase) and an H(+)-K(+)-ATPase. In the present study, we have employed two sources of IMCD cells, cells in primary culture derived from the terminal papilla of the Munich-Wistar rat (IMCDp) and an established murine cell line (mIMCD-3), to define the predominant mechanism(s) of Na(+)-independent intracellular pH (pHi) recovery in the IMCD. In confluent monolayers of IMCDp and mIMCD-3 cells, pHi was measured using the pH-sensitive dye 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein (BCECF) following addition and withdrawal of NH4Cl. Removal of K+ completely abolished Na(+)-independent pHi recovery in both IMCDp (delta pHi/min = 0.039 +/- 0.006 to 0.005 +/- 0.003; P < 0.001) and in mIMCD-3 (delta pHi/min = 0.055 +/- 0.009 to -0.003 +/- 0.002; P < 0.001) cells, respectively. In mIMCD-3 cells, K(+)-dependent pHi recovery was abolished by either of two specific inhibitors of the H(+)-K(+)-ATPase, Sch-28080 (5 or 10 microM) or A-80915A (10 microM). In contrast, bafilomycin A1 (2.5 and 10 nM), an inhibitor of the H(+)-ATPase, failed to attenuate K(+)-dependent pHi recovery. Moreover, sequence verified mouse gastric and colonic alpha-H(+)-K(+)-ATPase probes hybridized to total RNA from mIMCD-3 cells. Based on these findings, we conclude that Na(+)-independent pHi recovery from an acid load in both IMCDp and mIMCD-3 cells in critically dependent on extracellular K(+)-That K(+)-dependent pHi recovery was inhibited by both Sch-28080 and A-80915A but not by bafilomycin A1 suggests that the predominant mechanism by which Na(+)-independent pHi recovery is accomplished in IMCD is through the H(+)-K(+)-ATPase. Expression of both gastric and colonic alpha-H(+)-K(+)-ATPase mRNA in mIMCD-3 cells suggests that one or both of these H(+)-K(+)-ATPases may be responsible for proton secretion in the IMCD.
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9

Vujisic, Ljubica, Danijela Krstic, and Jovan Vucetic. "Chemical aspect of the influence of cobalt ions on atpase activity." Journal of the Serbian Chemical Society 65, no. 7 (2000): 507–15. http://dx.doi.org/10.2298/jsc0007507v.

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The influence of Co 2+ ions on the activities of Na+/K+-ATPase and Mg2+ -ATPase, enzymes from rat brain synaptic plasma membrane, was studied. The aim of this study was to investigate the inhibition of both ATPases activities byexposure tocobalt ions as a function of experimentally added CoSO4. The "free" Co2+ concentrations in the reaction mixturewere also calculated and discussed. CoSO4 induced a dose-dependent inhibition of both enzymes. The IC50 values of Co 2+, as calculated from the experimental curves, were 168 mM for Na+/K+-ATPase and 262 mMfor Mg 2+-ATPase, and for the recalculated free Co 2+ concentration 75.4 mM for Na+/K+-ATPase and 136 mM for Mg 2+-ATPase. The obtained linear Dixon's plot for Na+/K+-ATPase implies equilibium binding of cobalt with inhibitory sites on the enzyme. The kinetic parameters for both enzymes in presence and absence of CoSO4 were calculated from the experimental data. The results of the kinetic analysis show that inhibition of Na+/K+-ATPase induced by CoSO4 is non-competitive, and for Mg 2+-ATPase that there are two sites of different sensitivities or two different enzymes.
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10

Reinhardt, J., M. Kosch, M. Lerner, H. Bertram, D. Lemke, and H. Oberleithner. "Stimulation of protein kinase C pathway mediates endocytosis of human nongastric H+-K+-ATPase, ATP1AL1." American Journal of Physiology-Renal Physiology 283, no. 2 (August 1, 2002): F335—F343. http://dx.doi.org/10.1152/ajprenal.00226.2001.

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The human nongastric H+-K+-ATPase, ATP1AL1, shown to reabsorb K+ in exchange for H+ or Na+, is localized in the luminal plasma membrane of renal epithelial cells. It is presumed that renal H+-K+-ATPases can be regulated by endocytosis. However, little is known about the molecular mechanisms that control plasma membrane expression of renal H+-K+-ATPases. In our study, activation of protein kinase C (PKC) using phorbol esters (phorbol 12-myristate 13-acetate) leads to clathrin-dependent internalization and intracellular accumulation of the ion pump in stably transfected Madin-Darby canine kidney cells. Functional inactivation of the H+-K+-ATPase by PKC activation is shown by intracellular pH measurements. Proton extrusion capacity of ATP1AL1-transfected cells is drastically reduced after phorbol 12-myristate 13-acetate incubation and can be prevented with the PKC blocker bisindolylmaleimide. Ion pump internalization and inactivation are specifically mediated by the PKC pathway, whereas activation of the protein kinase A pathway has no influence. Our results show that the nongastric H+-K+-ATPase is a specific target for the PKC pathway. Therefore, PKC-mediated phosphorylation is a potential regulatory mechanism for apical nongastric H+-K+-ATPase plasma membrane expression.
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Dissertations / Theses on the topic "(Na+,K+)-dependent ATPase"

1

Hao, Jingping. "The electrical properties of Bufo marinus Na⁺, K⁺-ATPase." Ohio : Ohio University, 2009. http://www.ohiolink.edu/etd/view.cgi?ohiou1258151062.

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2

Cheng, Sam Xian Jun. "Functional significance of phosphorylation of rat renal Na+,K+-ATPase by PKA and PKC /." Stockholm, 1998. http://diss.kib.ki.se/1998/91-628-2971-8.

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3

Nguyen, Khoa Thuy Diem. "Energy metabolism in the brain and rapid distribution of glutamate transporter GLAST in astrocytes." Thesis, The University of Sydney, 2008. http://hdl.handle.net/2123/3996.

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Glutamate transporters play a role in removing extracellular excitatory neurotransmitter, L-glutamate into the cells. The rate of the uptake depends on the density of the transporters at the membrane. Some studies claimed that glutamate transporters could transit between the cytoplasm and the membrane on a time-scale of minutes. The present study examined the distribution of glutamate transporter GLAST predominantly expressed in rat cortical cultured astrocytes between the membrane and the cytoplasm by using deconvolution microscopy and then analyzing the images. The regulation of the distribution of GLAST was studied in the presence of glutamate transporter substrate (D-aspartate), purinergic receptor activators (α,β-methylene ATP, adenosine), neuroleptic drugs (clozapine, haloperidol), ammonia (hyperammonia) and Na+/K+-ATPase inhibitors (ouabain, digoxin and FCCP). It was demonstrated that the translocation of GLAST towards the plasma membrane was induced by D-aspartate, α,β-methylene ATP, adenosine, clozapine and ammonia (at 100 μM and very high concentrations of 10 mM). However, the inhibition of Na+/K+-ATPase activity had an opposite effect, resulting in redistribution of GLAST away from the membrane. It has previously been claimed that the membrane-cytoplasm trafficking of GLAST was regulated by phosphorylation catalysed by protein kinase C delta (PKC-delta). Involvement of this mechanism has, however, been put to doubt when rottlerin, a PKC-delta inhibitor, used to test the hypothesis showed to inhibit Na+/K+-ATPase-mediated uptake of Rb+, suggesting that rottlerin influenced the activity of Na+/K+-ATPase. As Na+/K+-ATPase converts ATP to energy and pumps Na+, K+ ions, thus helping to maintain normal electrochemical and ionic gradients across the cell membrane. Its inhibition also reduced D-aspartate transport and could impact on the cytoplasm-to-membrane traffic of GLAST molecules. Furthermore, rottlerin decreased the activity of Na+/K+-ATPase by acting as a mitochondrial inhibitor. The present study has focused on the inhibition of Na+/K+-ATPase activity by rottlerin, ouabain and digoxin in homogenates prepared from rat kidney and cultured astrocytes. The activity of Na+/K+-ATPase was measured by the absorption of inorganic phosphate product generated from the hydrolysis of ATP and the fluorescent transition of the dye RH421 induced by the movement of Na+/K+-ATPase. This approach has a potential to test whether the rottlerin effect on Na+/K+-ATPase is a direct inhibition of the enzyme activity. Rottlerin has been found to block the activity of Na+/K+-ATPase in a dose-dependent manner in both rat kidney and astrocyte homogenates. Therefore, rottlerin inhibited the activity of Na+/K+-ATPase directly in a cell-free preparation, thus strongly indicating that the effect was direct on the enzyme. In parallel experiments, ouabain and digoxin produced similar inhibitions of Na+/K+-ATPase activity in rat kidney while digoxin blocked the activity of Na+/K+-ATPase to a greater extent than ouabain in rat cortical cultured astrocytes. In a separate set of experiments, Na+/K+-ATPase in the astrocytic membrane was found to be unsaturated in E1(Na+)3 conformation in the presence of Na+ ions and this could explain the differences between the effects of digoxin and ouabain on the activity of Na+/K+-ATPase in rat astrocytes. In addition, it was found that at low concentrations of rottlerin, the activity of Na+/K+-ATPase was increased rather than inhibited. This effect was further investigated by studying rottlerin interactions with membrane lipids. The activity of Na+/K+-ATPase has been reported to be regulated by membrane lipids. The enzyme activity can be enhanced by increasing fluidity of the lipid membrane. I have, therefore, proposed that rottlerin binds to the membrane lipids and the effects of rottlerin on Na+/K+-ATPase are mediated by changes in the properties (fluidity) of the membrane. The hypothesis was tested by comparing rottlerin and a detergent, DOC (sodium deoxycholate), for their binding to the lipids by using a DMPC (1,2-Dimyristoyl-sn-Glycero-3-Phosphocholine) monolayer technique. DOC has been shown to both increase and inhibit activity of Na+/K+-ATPase in a manner similar to that displayed by rottlerin. The effects of rottlerin and DOC on the DMPC monolayers were studied by measuring the surface pressure of DMPC monolayers and surface area per DMPC molecule. I established that both rottlerin and DOC decreased the surface pressure of DMPC monolayers and increased the surface area per DMPC molecule. This indicates that both rottlerin and DOC penetrated into the DMPC monolayers. If rottlerin can interact with the lipids, changes in fluidity of the lipid membrane cannot be ruled out and should be considered as a possible factor contributing to the effects of rottlerin on the activity of Na+/K+-ATPase. Overall, the study demonstrates that rottlerin is not only a PKC-delta inhibitor but can have additional effects, both on the enzyme activities (Na+/K+-ATPase) and/or on lipid-containing biological structures such as membranes. The findings have implication not only for studies where rottlerin was used as a supposedly specific PKC-delta inhibitor but also for mechanisms of its toxicity.
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4

Nguyen, Khoa Thuy Diem. "Energy metabolism in the brain and rapid distribution of glutamate transporter GLAST in astrocytes." University of Sydney, 2008. http://hdl.handle.net/2123/3996.

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Doctor of Philosophy (Medicine)
Glutamate transporters play a role in removing extracellular excitatory neurotransmitter, L-glutamate into the cells. The rate of the uptake depends on the density of the transporters at the membrane. Some studies claimed that glutamate transporters could transit between the cytoplasm and the membrane on a time-scale of minutes. The present study examined the distribution of glutamate transporter GLAST predominantly expressed in rat cortical cultured astrocytes between the membrane and the cytoplasm by using deconvolution microscopy and then analyzing the images. The regulation of the distribution of GLAST was studied in the presence of glutamate transporter substrate (D-aspartate), purinergic receptor activators (α,β-methylene ATP, adenosine), neuroleptic drugs (clozapine, haloperidol), ammonia (hyperammonia) and Na+/K+-ATPase inhibitors (ouabain, digoxin and FCCP). It was demonstrated that the translocation of GLAST towards the plasma membrane was induced by D-aspartate, α,β-methylene ATP, adenosine, clozapine and ammonia (at 100 μM and very high concentrations of 10 mM). However, the inhibition of Na+/K+-ATPase activity had an opposite effect, resulting in redistribution of GLAST away from the membrane. It has previously been claimed that the membrane-cytoplasm trafficking of GLAST was regulated by phosphorylation catalysed by protein kinase C delta (PKC-delta). Involvement of this mechanism has, however, been put to doubt when rottlerin, a PKC-delta inhibitor, used to test the hypothesis showed to inhibit Na+/K+-ATPase-mediated uptake of Rb+, suggesting that rottlerin influenced the activity of Na+/K+-ATPase. As Na+/K+-ATPase converts ATP to energy and pumps Na+, K+ ions, thus helping to maintain normal electrochemical and ionic gradients across the cell membrane. Its inhibition also reduced D-aspartate transport and could impact on the cytoplasm-to-membrane traffic of GLAST molecules. Furthermore, rottlerin decreased the activity of Na+/K+-ATPase by acting as a mitochondrial inhibitor. The present study has focused on the inhibition of Na+/K+-ATPase activity by rottlerin, ouabain and digoxin in homogenates prepared from rat kidney and cultured astrocytes. The activity of Na+/K+-ATPase was measured by the absorption of inorganic phosphate product generated from the hydrolysis of ATP and the fluorescent transition of the dye RH421 induced by the movement of Na+/K+-ATPase. This approach has a potential to test whether the rottlerin effect on Na+/K+-ATPase is a direct inhibition of the enzyme activity. Rottlerin has been found to block the activity of Na+/K+-ATPase in a dose-dependent manner in both rat kidney and astrocyte homogenates. Therefore, rottlerin inhibited the activity of Na+/K+-ATPase directly in a cell-free preparation, thus strongly indicating that the effect was direct on the enzyme. In parallel experiments, ouabain and digoxin produced similar inhibitions of Na+/K+-ATPase activity in rat kidney while digoxin blocked the activity of Na+/K+-ATPase to a greater extent than ouabain in rat cortical cultured astrocytes. In a separate set of experiments, Na+/K+-ATPase in the astrocytic membrane was found to be unsaturated in E1(Na+)3 conformation in the presence of Na+ ions and this could explain the differences between the effects of digoxin and ouabain on the activity of Na+/K+-ATPase in rat astrocytes. In addition, it was found that at low concentrations of rottlerin, the activity of Na+/K+-ATPase was increased rather than inhibited. This effect was further investigated by studying rottlerin interactions with membrane lipids. The activity of Na+/K+-ATPase has been reported to be regulated by membrane lipids. The enzyme activity can be enhanced by increasing fluidity of the lipid membrane. I have, therefore, proposed that rottlerin binds to the membrane lipids and the effects of rottlerin on Na+/K+-ATPase are mediated by changes in the properties (fluidity) of the membrane. The hypothesis was tested by comparing rottlerin and a detergent, DOC (sodium deoxycholate), for their binding to the lipids by using a DMPC (1,2-Dimyristoyl-sn-Glycero-3-Phosphocholine) monolayer technique. DOC has been shown to both increase and inhibit activity of Na+/K+-ATPase in a manner similar to that displayed by rottlerin. The effects of rottlerin and DOC on the DMPC monolayers were studied by measuring the surface pressure of DMPC monolayers and surface area per DMPC molecule. I established that both rottlerin and DOC decreased the surface pressure of DMPC monolayers and increased the surface area per DMPC molecule. This indicates that both rottlerin and DOC penetrated into the DMPC monolayers. If rottlerin can interact with the lipids, changes in fluidity of the lipid membrane cannot be ruled out and should be considered as a possible factor contributing to the effects of rottlerin on the activity of Na+/K+-ATPase. Overall, the study demonstrates that rottlerin is not only a PKC-delta inhibitor but can have additional effects, both on the enzyme activities (Na+/K+-ATPase) and/or on lipid-containing biological structures such as membranes. The findings have implication not only for studies where rottlerin was used as a supposedly specific PKC-delta inhibitor but also for mechanisms of its toxicity.
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Kuznetsova, Irina [Verfasser]. "Inhibition of the influenza A virus-induced, tubulin-dependent apical mislocalization of the Na+,K+-ATPase in infected cells: Improving vectorial water transport and pulmonary edema clearance / Irina Kuznetsova." Gieߟen : Universitätsbibliothek, 2020. http://d-nb.info/1216143633/34.

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Schneeberger, Anne. "Ionenbindung an die Na, K-ATPase." [S.l. : s.n.], 2000. http://deposit.ddb.de/cgi-bin/dokserv?idn=959955968.

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Liang, Man. "Na/K ATPase : signaling versus pumping." Toledo, Ohio : University of Toledo, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1173803261.

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Thesis (Ph.D.)--University of Toledo, 2006.
"In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Sciences." Major advisor: Zi-Jian Xie. Includes abstract. Document formatted into pages: iii, 156 p. Title from title page of PDF document. Bibliography: pages 64-67, 97-100, 116-117, 125-155.
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Tian, Jiang. "Na/K-ATPase : a signaling receptor." Connect to Online Resource-OhioLINK, 2006. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=mco1175177603.

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Thesis (Ph.D.)--University of Toledo, 2006.
"In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Sciences." Major advisor: Zi-Jian Xie. Includes abstract. Title from title page of PDF document. Bibliography: pages 64-70, 104-108, 121-158.
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Aizman, Oleg. "Novel aspects of Na⁺,K⁺-ATPase /." Stockholm, 2002. http://diss.kib.ki.se/2002/91-7349-311-2.

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Carradus, Maria. "Structural studies of Na'+K'+-ATPase." Thesis, Imperial College London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342323.

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Books on the topic "(Na+,K+)-dependent ATPase"

1

Chakraborti, Sajal, and Naranjan S. Dhalla, eds. Regulation of Membrane Na+-K+ ATPase. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-24750-2.

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Horisberger, Jean-Daniel. The Na,K-ATPase: Structure-function relationship. Austin: R.G. Landes, 1994.

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International Conference on the Na/K-ATPase and Related ATPases (9th 1999 Sapporo, Japan). Na/K-ATPase and related ATPases: Proceedings of the 9th International Conference on the Na/K-ATPase and Related ATPases, Sapporo, Japan, 18-23 August 1999. Edited by Kaya Shunji and Taniguchi Kazuya 1966-. Amsterdam: Elsevier, 2000.

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J, Shearer M., and Seghatchian M. J, eds. Vitamin K and vitamin K-dependent proteins: Analytical, physiological, and clinical aspects. Boca Raton, Fla: CRC Press, 1993.

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Garetz, Susan Lynn. Variation in expression of Na+K+ATPase ł and ø subunit mRNAs in rat tissues and nervous system cell lines. [New Haven: s.n.], 1989.

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International, Conference on Na K.-ATPase. The sodium pump: Proceedings of the Fourth International Conference on Na, K-ATPase held at the Physiological Laboratory, Cambridge, in August 1984. Cambridge: Company of Biologists, 1985.

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Ian, Glynn, Ellory J. C, and Company of Biologists, eds. The sodium pump: Proceedings of the Fourth International Conference on Na, K-ATPase, held at the Physiological Laboratory, Cambridge, in August 1984. Cambridge, U.K: Company of Biologists, 1985.

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Yasunobu, Suketa, and Excerpta Medica (Firm), eds. Control and diseases of sodium dependent transport proteins and ion channels: Proceedings of the First International Conference held in Shizuoka, Japan, 24-28th August 1999. Amsterdam: Elsevier, 2000.

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Dhalla, Naranjan S., and Sajal Chakraborti. Regulation of Membrane Na+-K+ ATPase. Springer, 2015.

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Chakraborti, Sajal, and Naranjan S. Dhalla. Regulation of Membrane Na+-K+ ATPase. Springer, 2015.

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Book chapters on the topic "(Na+,K+)-dependent ATPase"

1

Spieker, C., K. H. Rahn, and W. Zidek. "Age-dependent secretion of a Na+ K+ ATPase inhibitor in spontaneously hypertensive rats." In Arteriosklerotische Gefäßerkrankungen, 410–16. Wiesbaden: Vieweg+Teubner Verlag, 1992. http://dx.doi.org/10.1007/978-3-663-19646-4_47.

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Obradovic, Milan, Julijana Stanimirovic, Anastasija Panic, Bozidarka Zaric, and Esma R. Isenovic. "Na+/K+-ATPase." In Encyclopedia of Signaling Molecules, 3338–43. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101543.

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Obradovic, Milan, Julijana Stanimirovic, Anastasija Panic, Bozidarka Zaric, and Esma R. Isenovic. "Na +/K+-ATPase." In Encyclopedia of Signaling Molecules, 1–6. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101543-1.

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Scheiner-Bobis, G. "Na+/K+-ATPase." In Encyclopedia of Molecular Pharmacology, 1–10. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-21573-6_267-1.

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Scheiner-Bobis, G. "Na+/K+-ATPase." In Encyclopedia of Molecular Pharmacology, 1062–71. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-57401-7_267.

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Lee, Chin Ok, and David C. Gadsby. "PKA Activation in Cardiac Myocytes Affects the Voltage Dependence of Na-K ATPase Pump and Na-Ca Exchange Currents Differently." In The Primo Vascular System, 271–83. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4614-0601-3_37.

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Delamere, Nicholas A., and Shigeo Tamiya. "Lens Na+, K+-ATPase." In Ocular Transporters In Ophthalmic Diseases And Drug Delivery, 111–23. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-375-2_6.

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de Pont, Jan Joep H. H. M., Jan B. Koenderink, Herman G. P. Swarts, and Peter H. G. M. Willems. "Structure-Activity Relationships of Na,K-ATPase and H,K-ATPase." In Mechanisms and Consequences of Proton Transport, 71–82. Boston, MA: Springer US, 2002. http://dx.doi.org/10.1007/978-1-4615-0971-4_7.

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Sachs, George, and Björn Wallmark. "The gastric H, K ATPase." In Proton Pump Inhibitors, 23–45. Basel: Birkhäuser Basel, 1999. http://dx.doi.org/10.1007/978-3-0348-8795-3_2.

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Chakraborti, Sajal, Sayed Modinur Rahaman, Md Nur Alam, Amritlal Mandal, Biswarup Ghosh, Kuntal Dey, and Tapati Chakraborti. "Na+/K+-ATPase: A Perspective." In Regulation of Membrane Na+-K+ ATPase, 3–30. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24750-2_1.

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Conference papers on the topic "(Na+,K+)-dependent ATPase"

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Grzesik, Benno, Ramona Ruhl, Nieves Gabrielli, Werner Seeger, Wolfgang Kummer, Uwe Pfeil, and Istvan Vadasz. "Intermedin Enhances Alveolar Edema Clearance By Promoting Na,K-ATPase Exocytosis In A Protein Kinase A-Dependent But CAMP-Independent Manner." 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.a3521.

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Gusarova, GA, LA Dada, A. Briva, H. Trejo, and JI Sznajder. "Hypoxia Leads to Ca2+/Calmodulin-Dependent Kinase Kinase β (CaMKKβ) Activation/AMPK Phosphorylation, Na,K-ATPase Endocytosis and Impaired Alveolar Epithelial Reabsorbtion." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a1927.

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Hack, N., J. M. Wilkinson, and N. Crawford. "A MONOCLONAL ANTIBODY (PL/IM 430) THAT BLOCKS THE ACTIVE TRANSL0CATI0N OF Ca2+ INTO HUMAN PLATELET INTRACELLULAR MEMBRANE (ER) VESICLES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644678.

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In earlier studies [1] we identified a number of important biological properties associated with highly purified human platelet intracellular membrane (ER), isolated by continuous flow electrophoresis. These included a high affinity Ca2+Mg2+ ATPase and protein phosghorylation both of which are involved inthe active uptake of Ca into ER vesicles. The stored Ca2+ could be released with inositol(1,4,5)trisphosphate, (IP ), (approx. 50% release in 30 s 1/2 max. for release - 0.253 μM IP3,) [2]. To probe the structure-function relationship of proteins in these ER vesicles, a panel of monoclonal antibodies (Mabs) has been raised, using the ER membrane preparation as immunogen. Four of these Mabs recognise a single 100 kDa polypeptide by immunoblotting. This protein is present in platelet membranes and can also be identified in cultured human monocyte, macrophage and endothelial cell lines. None of the M^bs showed any significant effect upon the ER membrane Ca2+ Mg2+ ATPase activity but one, PL/IM 430 (of IgGl subclass), inhibited the Ca2+sequestration by the vesicles significantly (approx. 70% inhibition at 10 μM IgG). This inhibition was independent of the ATP concentration over a range2of 0-2 mM ATP, but was2dose-dependent for external free Ca 2between 30-300 nM Ca2+, giving maximum inhibition at 300 nM Ca with 10 pM IgG2+ Binding of the antibody substantially lowers the Vmax for Ca2+for Ca2+ uptake but is without effect upon the Km. PL/IM 430 therefore appears to recognise a 100 kDa polypeptide closely involved with Ca2+ trnslocation but at a site which i, s without effect upon the Ca2+Mg− ATPase associated with the Ca pump.We are grateful to the Wellcome Trust and the British Heart Foundation for financial support for these studies.[1] Hack, N., Croset, M. and Crawford, N. (1986) Biochem. J. 233, 661-668.[2] Authi, K. S. and Crawford, N. (1985) Biochem. J. Z3O, 247-253
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Fujimoto, T., B. Djuricic, K. Tanoue, Y. Fukushima, and H. Yamazaki. "CHANGES IN ENZYMATIC ACTIVITIES IN BRAIN CAPILLARY ENDOTHELIAL CELLS INJURED BY PLATELET AGGREGATION IN VIVO." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643368.

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We have reported cerebrovascular injuries induced by platelet aggregation in vivo. Appearance of vacuoles in endothelial cells and eventual deendothelialization are characteristic in large cerebral arteries (Stroke, 16:245, 1985). Minor changes are observed in brain capillaries, but disturbances of blood-brain barrier (BBB) are seen. To analyse changes in BBB, enzymatic activities in capillary endothelial cells before and after ADP-induced platelet aggregation in vivo were investigated.80 mg/kg of ADP was injected through a catheter into the right internal carotid artery of 32 rabbits. One hr later, right and left cortexes freed from pial membranes were homogenized and microvessels were isolated using discontinuous sucrose gradient ultracentrifugation. Purity of microvessel fraction was ascertained microscopically. The follwing enzymatic activities in these samples were measured.; cytochrome C oxydase (CCO), monoamine oxidase (MAO), p-nitrophenyl-phosphatase transferase (pNPPase, K-dependent component of Na, K-ATPase), gamma-glutamyl transferase (GT) and adenylate cyclase (AC). The enzymatic activities did not change after a vehicle-injection and did not show any differences between capillaries of both the cortexes before the ADP-injection. One hr after the ADP, GT and CCO activities decreased significantly in the capillaries of injection side. MAO activity also reduced without significance. The other enzymes did not show significant changes in their activities. Although pNPPase and AC which are associated with inner surface of plasma membrane were preserved well, activity of GT which is associated with outer portion of the membrane decreased significantly. It suggests superficial luminal injury and that plasma membrane might be affected from the side of vascular lumen. Reduced CCO activity suggests that disturbance in BBB is probably related to the increase in vesicular transportation and/or energy failure. Reduction of MAO activity indicates that damages to mitochondria exist in the capillaries. Cerebral blood vessels are prone to damage by released substances from activated platelet in vivo.
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Lestari, Silvia W., Aucky Hinting, Hamdani Lunardi, Debby Aditya, Dessy Noor Miati, and Meidika Dara Rizki. "Sperm Na+,K+-ATPase and dynein ATPase activity: A study of embryo development in in vitro fertilization (IVF)." In SECOND INTERNATIONAL CONFERENCE OF MATHEMATICS (SICME2019). Author(s), 2019. http://dx.doi.org/10.1063/1.5096752.

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Onken, Horst. "V-ATPase and Na+/K+-ATPase energize postprandial fluid absorption from the isolated midgut of female yellow fever mosquitoes (Aedes aegypti)." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.93236.

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Krastev, Dragomir, Shudong Li, Yilun Sun, Yves Pommier, Kristijan Ramadan, and Christopher J. Lord. "Abstract P057: The ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from chromatin." In Abstracts: AACR-NCI-EORTC Virtual International Conference on Molecular Targets and Cancer Therapeutics; October 7-10, 2021. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1535-7163.targ-21-p057.

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Yang, Liqun, Olga Lopina, Daniel McStay, A. A. Boldyrev, Alan J. Rogers, and Peter J. Quinn. "Time-resolved phosphorescence measurement of conformational transitions in cation transport Na+, K+-ATPase." In OE/LASE'93: Optics, Electro-Optics, & Laser Applications in Science& Engineering, edited by Laurence A. Nafie and Henry H. Mantsch. SPIE, 1993. http://dx.doi.org/10.1117/12.145246.

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Li, Zhiqin, Alisa Litan, Seung Joon Lee, Bruce Graves, Sonali P. Barwe, and Sigrid A. Langhans. "Abstract 707: Distinct roles of Na,K-ATPase function and expression in medulloblastoma." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-707.

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Lestari, Silvia W., Manggiasih D. Larasati, Asmarinah, and Indra G. Mansur. "Sperm Na+, K+-ATPase and Ca2+-ATPase activity: A preliminary study of comparison of swim up and density gradient centrifugation methods for sperm preparation." In 2ND BIOMEDICAL ENGINEERING’S RECENT PROGRESS IN BIOMATERIALS, DRUGS DEVELOPMENT, AND MEDICAL DEVICES: Proceedings of the International Symposium of Biomedical Engineering (ISBE) 2017. Author(s), 2018. http://dx.doi.org/10.1063/1.5023963.

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Reports on the topic "(Na+,K+)-dependent ATPase"

1

Colton, Joel S., Sara C. Gilman, and Carol A. Colton. Effect of the Thiol-Oxidizing Agent, Diamide, on Cerebral Cortical Na(+) -K(+) ATPase. Fort Belvoir, VA: Defense Technical Information Center, September 1988. http://dx.doi.org/10.21236/ada205311.

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Aubert, B. Measurement of Time-Dependent CP-Violating Asymmetries in B0 ->K*0 gamma (K*0->K0{sub S} pi0) Decays. Office of Scientific and Technical Information (OSTI), June 2004. http://dx.doi.org/10.2172/826956.

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Aubert, B. Measurements of Branching Fractions and Time-Dependent CP-Violating Asymmetries in B to eta' K Decays. Office of Scientific and Technical Information (OSTI), February 2005. http://dx.doi.org/10.2172/839753.

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Gronau, M. Interpreting the Time-Dependent CP Asymmetry in B{sup 0} {yields} {pi}{sup 0} K{sub S}. Office of Scientific and Technical Information (OSTI), November 2003. http://dx.doi.org/10.2172/826518.

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Ilic, J. Time-dependent Dalitz-Plot Analysis of the Charmless Decay B^0 -> K^0S Pi Pi- at BABAR. Office of Scientific and Technical Information (OSTI), October 2009. http://dx.doi.org/10.2172/968531.

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Palombo, F. Measurement of Time-Dependent CP-Violating Asymmetries in B{sup 0} Meson Decays to eta' K{sup 0}. Office of Scientific and Technical Information (OSTI), August 2004. http://dx.doi.org/10.2172/829746.

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Aubert, B. Ambiguity-Free Measurement of cos2beta: Time-Intergrated and Time-Dependent Angular Analyses of B to J/psi K pi. Office of Scientific and Technical Information (OSTI), November 2004. http://dx.doi.org/10.2172/839607.

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T'Jampens, Stephane. Study of CP Symmetry Violation in the Charmonium-K*(892) Channel By a Complete Time Dependent Angular Analysis (BaBar Experiment). Office of Scientific and Technical Information (OSTI), September 2006. http://dx.doi.org/10.2172/891862.

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Joseph Marion Tuggle IV. Radiative B Meson Decay as a Probe of Physics Beyond the Standard Model: Time-Dependent CP Violation in B0 → K0S π0 γ and the B → Φ K γ Branching Fraction. Office of Scientific and Technical Information (OSTI), January 2009. http://dx.doi.org/10.2172/946450.

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Biassoni, Pietro. Measurements of Time-Dependent CP-Asymmetry Parameters in B Meson Decays to η' K0 and of Branching Fractions of SU(3) Related Modes with BaBar Experiment at SLAC. Office of Scientific and Technical Information (OSTI), January 2009. http://dx.doi.org/10.2172/946451.

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