Relevant bibliographies by topics / Adenosine triphosphatase

Academic literature on the topic 'Adenosine triphosphatase'

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Published: 4 June 2021
Last updated: 26 July 2024

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Journal articles on the topic "Adenosine triphosphatase"

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Dunn, P. P. J., A. R. Slabas, and A. L. Moore. "Characterization of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatases." Biochemical Journal 233, no. 3 (February 1, 1986): 839–44. http://dx.doi.org/10.1042/bj2330839.

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The catalytic properties of cuckoo-pint (Arum maculatum) mitochondrial adenosine triphosphatase have been analysed. The pH profile, effect of inhibitors, cold-stability and substrate specificity are characteristic of mitochondrial adenosine triphosphatases, although a high guanosine triphosphatase activity does appear to be restricted to plant mitochondrial adenosine triphosphatases. The kinetic properties of nucleoside 5′-triphosphate hydrolysis by membrane-bound and soluble enzymes have been studied by means of double-reciprocal plots. These plots were linear in the absence of an activating anion, which may indicate that the catalytic and/or regulatory mechanism of Arum maculatum adenosine triphosphatase is different from that of other enzyme preparations. It is suggested that the differences in subunit composition of plant and mammalian adenosine triphosphatases reported previously [Dunn, Slabas & Moore (1985) Biochem. J. 225, 821-824] are structurally, rather than functionally, significant.
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Kristjansson, Hordur, Martha H. Sadler, and Lawrence I. Hochstein. "Halobacterial adenosine triphosphatases and the adenosine triphosphatase fromHalobacterium saccharovorum." FEMS Microbiology Letters 39, no. 1-2 (July 1986): 151–57. http://dx.doi.org/10.1111/j.1574-6968.1986.tb01856.x.

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Weiler, Elmar, Farhad Khalil-Manesh, and Harvey C. Gonick. "Effects of Lead and a Low-Molecular-Weight Endogenous Plasma Inhibitor on the Kinetics of Sodium—Potassium-Activated Adenosine Triphosphatase and Potassium-Activated p-Nitrophenylphosphatase." Clinical Science 79, no. 2 (August 1, 1990): 185–92. http://dx.doi.org/10.1042/cs0790185.

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1. Lead, ouabain and an endogenous plasma inhibitor were all found to be potent inhibitors of purified hog cerebral cortex sodium—potassium-activated adenosine triphosphatase and potassium-stimulated p-nitrophenylphosphatase. 2. The kinetic characteristics of inhibition of both enzymes by lead and the endogenous plasma inhibitor differed in several respects. For sodium—potassium-activated adenosine triphosphatase, lead and the endogenous plasma inhibitor were non-competitive inhibitors with respect to potassium; lead was competitive with respect to sodium, whereas the endogenous plasma inhibitor had no effect; lead was competitive with respect to magnesium adenosine triphosphate, whereas the endogenous plasma inhibitor was uncompetitive. For potassium-activated p-nitrophenylphosphatase, both lead and the endogenous plasma inhibitor were competitive with respect to potassium; lead showed a mixed type of inhibition with respect to p-nitrophenylphosphate, whereas the endogenous plasma inhibitor was non-competitive. 3. Lead and the endogenous plasma inhibitor exhibited synergistic inhibitory activity on sodium—potassium-activated adenosine triphosphatase. 4. These results suggest that lead could play a contributory role in the pathogenesis of essential hypertension via an additive inhibition of vascular smooth muscle sodium—potassium-activated adenosine triphosphatase.
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Liu, Gang, Si Qi Li, Ping Ping Hu, and Xiao Yong Tong. "Altered sarco(endo)plasmic reticulum calcium adenosine triphosphatase 2a content: Targets for heart failure therapy." Diabetes and Vascular Disease Research 15, no. 4 (May 15, 2018): 322–35. http://dx.doi.org/10.1177/1479164118774313.

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Sarco(endo)plasmic reticulum calcium adenosine triphosphatase is responsible for transporting cytosolic calcium into the sarcoplasmic reticulum and endoplasmic reticulum to maintain calcium homeostasis. Sarco(endo)plasmic reticulum calcium adenosine triphosphatase is the dominant isoform expressed in cardiac tissue, which is regulated by endogenous protein inhibitors, post-translational modifications, hormones as well as microRNAs. Dysfunction of sarco(endo)plasmic reticulum calcium adenosine triphosphatase is associated with heart failure, which makes sarco(endo)plasmic reticulum calcium adenosine triphosphatase a promising target for heart failure therapy. This review summarizes current approaches to ameliorate sarco(endo)plasmic reticulum calcium adenosine triphosphatase function and focuses on phospholamban, an endogenous inhibitor of sarco(endo)plasmic reticulum calcium adenosine triphosphatase, pharmacological tools and gene therapies.
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Ogata, Yumi, and Ikuo Kimura. "Adenosine triphosphate suppresses urea-induced denaturation of shark myosin calcium adenosine triphosphatase." Fisheries Science 85, no. 1 (October 22, 2018): 227–35. http://dx.doi.org/10.1007/s12562-018-1264-8.

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Pearson, J. D., S. B. Coade, and N. J. Cusack. "Characterization of ectonucleotidases on vascular smooth-muscle cells." Biochemical Journal 230, no. 2 (September 1, 1985): 503–7. http://dx.doi.org/10.1042/bj2300503.

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We compared the properties of the ectonucleotidases (nucleoside triphosphatase, EC 3.6.1.15; nucleoside diphosphatase, EC 3.6.1.6; 5′-nucleotidase, EC 3.1.3.5) in intact pig aortic smooth-muscle cells in culture with the properties that we previously investigated for ectonucleotidases of aortic endothelial cells [Cusack, Pearson & Gordon (1983) Biochem. J. 214, 975-981]. In experiments with nucleotide phosphorothioate diastereoisomers, stereoselective catabolism of adenosine 5′-[β-thio]triphosphate, but not of adenosine 5′-[α-thio]triphosphate, by the triphosphatase and stereoselective catabolism of adenosine 5′-[α-thio]diphosphate by the diphosphatase were found, as occurs in endothelial cells. In contrast with endothelial ecto-5′-nucleotidase, the smooth-muscle-cell enzyme catabolized adenosine 5′-monophosphorothioate (AMPS) to adenosine: the affinity of the enzyme for AMPS was greater than for AMP, and Vmax for AMPS was about one-sixth that for AMP. In both cell types AMPS was an apparently competitive inhibitor of AMP catabolism by 5′-nucleotidase. The relative rates of catabolism of nucleotide enantiomers in which the natural D-ribofuranosyl moiety is replaced by an L-ribofuranosyl moiety were similar to those in endothelial cells. No ectopyrophosphatase activity was detected in smooth-muscle cells, in contrast with endothelial cells, where modest activity is present.
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Antonelli, M. L., V. Carunchio, and M. Luciani. "Microcalorimetric study of the system adenosine-5′-triphosphate—sodium, potassium adenosine-5′-triphosphatase." Analytica Chimica Acta 252, no. 1-2 (November 1991): 17–22. http://dx.doi.org/10.1016/0003-2670(91)87191-9.

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Dey, Sandip, Chiranjit Biswas, and Jayati Sengupta. "The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged Escherichia coli ribosomes." Journal of Cell Biology 217, no. 7 (June 21, 2018): 2519–29. http://dx.doi.org/10.1083/jcb.201711131.

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The ribosome-associated GTPase HflX acts as an antiassociation factor upon binding to the 50S ribosomal subunit during heat stress in Escherichia coli. Although HflX is recognized as a guanosine triphosphatase, several studies have shown that the N-terminal domain 1 of HflX is capable of hydrolyzing adenosine triphosphate (ATP), but the functional role of its adenosine triphosphatase (ATPase) activity remains unknown. We demonstrate that E. coli HflX possesses ATP-dependent RNA helicase activity and is capable of unwinding large subunit ribosomal RNA. A cryo–electron microscopy structure of the 50S–HflX complex in the presence of nonhydrolyzable analogues of ATP and guanosine triphosphate hints at a mode of action for the RNA helicase and suggests the linker helical domain may have a determinant role in RNA unwinding. Heat stress results in inactivation of the ribosome, and we show that HflX can restore heat-damaged ribosomes and improve cell survival.
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Vivien, Benoît, Yves Lecarpentier, Bruno Riou, and Catherine Coirault. "Halothane and Isoflurane Do Not Directly Interact with Cardiac Cross-bridge Function." Anesthesiology 102, no. 2 (February 1, 2005): 364–70. http://dx.doi.org/10.1097/00000542-200502000-00019.

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Background Halogenated anesthetics depress myocardial contractility by altering a number of specific mechanisms. These alterations include decreases in inward calcium current and sarcoplasmic reticulum function and reduced calcium myofilament sensitivity. However, the direct effects of volatile anesthetics on cross-bridge function have yet to be precisely determined. Methods Myosin monomers and actin filaments were isolated from fresh rat left ventricles and rabbit skeletal muscles, respectively. Halothane or isoflurane was added at concentrations equivalent to 1 and 2 minimum alveolar concentration (MAC). Motility of actin filaments over myosin was initiated by adding 2 mm adenosine triphosphate and was analyzed at 30 degrees C. Maximum actomyosin adenosine triphosphatase activity and the association constant of myosin for actin were determined from a double-reciprocal Lineweaver-Burk plot of the adenosine triphosphatase rate versus actin concentration. A known inhibitor of actomyosin function, 2,3-butanedione 2-monoxime (2 mm), was used in positive control experiments. Data are presented as mean +/- SD. Results Motility velocities driven by myosin were not significantly different between baseline and 1 and 2 MAC halothane (2.70 +/- 0.33, 2.72 +/- 0.36, and 2.70 +/- 0.40 microm/s, respectively). Similarly, motility velocities driven by myosin were not significantly different between baseline and 1 and 2 MAC isoflurane (2.73 +/- 0.33, 2.72 +/- 0.37, and 2.72 +/- 0.40 microm/s, respectively). Neither of the two halogenated anesthetics, at any concentration tested, significantly modified the maximum actomyosin adenosine triphosphatase activity or the association constant of myosin for actin as compared with baseline. 2,3-Butanedione 2-monoxime induced a drastic reduction in both motility velocity and maximum actomyosin adenosine triphosphatase activity. Conclusion These results indicate that isoflurane and halothane do not directly depress the mechanical or enzymatic properties of cross-bridges in the heart.
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Eiam-Ong, Somchai, Melvin E. Laski, and Neil A. Kurtzman. "Diseases of Renal Adenosine Triphosphatase." American Journal of the Medical Sciences 309, no. 1 (January 1995): 13–25. http://dx.doi.org/10.1097/00000441-199501000-00003.

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Dissertations / Theses on the topic "Adenosine triphosphatase"

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Therien, Alex Geoffroy. "Tissue-specific regulation of the sodium potassium adenosine triphosphatase." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0015/NQ55385.pdf.

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Therien, Alex Geoffroy. "Tissue-specific regulation of the sodium potassium adenosine triphosphatase." Thesis, McGill University, 1999. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=35550.

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The Na,K-ATPase, or sodium pump, is a membrane-associated protein complex comprising two subunits, alpha and beta, both of which can exist as one of several isoforms. It generates and maintains the electrochemical Na + and K+ gradients across the plasma membrane of animal cells. These gradients are the driving force for a variety of ubiquitous and specialized cell functions, such as transport of solutes, as well as maintenance of membrane potential and cell volume. Agents that modulate the kinetic behaviour of the pump enable cells to adapt to changing needs. Distinct substrate activation profiles in various tissues presumably underlie the specialized functions of the sodium pump in these tissues. Although the tissue-specific distribution of various isoforms accounts for some of the differences in kinetic behaviour of the enzyme, other factors are also important determinants of such behaviour. This study describes the characterization of two mechanisms of sodium pump modulation. The first involves alterations in the susceptibility of the enzyme to competitive inhibition by K+ at Na+ binding sites. Studies on the alpha1 and alpha3 isoform of various tissues and cells have revealed that there exist tissue-specific components that determine the extent to which the two cations compete with each other for cytoplasmic binding sites. Specifically, pumps that are highly susceptible to K +/Na+ antagonism also bind and occlude K+ much more readily on the cytoplasmic site, and this behaviour is abrogated upon fusion of pumps into another membrane environment, that of the red blood cell. The second mechanism of regulation of pump behaviour described in this thesis involves modulation of the apparent affinity of the enzyme for ATP by the gamma subunit. This membrane protein had been previously cloned and sequenced, but very little was known about its function. This study shows that the gamma subunit is expressed uniquely in kidney tubules, and has a C-terminus-in, N-terminus-
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Walpole, Thomas Benjamin. "Studies of methylation of metazoan F-ATPases." Thesis, University of Cambridge, 2015. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708674.

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Kiirats, Olavi. "Co-regulation of the electron transport and carbon assimilation in C₃ and C₄4 plants the role of CF₀-CF₁ ATP synthase /." Pullman, Wash. : Washington State University, 2009. http://www.dissertations.wsu.edu/Dissertations/Spring2009/o_kiirats_050909.pdf.

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Flannery, Andrew Rawlins. "Characterization of the structure and regulation of the vacuolar H⁺-ATPase /." view abstract or download file of text, 2005. http://wwwlib.umi.com/cr/uoregon/fullcit?p3190517.

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Thesis (Ph. D.)--University of Oregon, 2005.
Typescript. Includes vita and abstract. Includes bibliographical references (leaves 85-95). Also available for download via the World Wide Web; free to University of Oregon users.
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Zou, Yazhong. "A computational study of energy conversion efficiency of F1-ATPase." HKBU Institutional Repository, 2017. https://repository.hkbu.edu.hk/etd_oa/480.

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ATP synthase (F_1 F_O-ATPase) is an essential enzyme for life. Powered by an electrochemical proton gradient, it catalyzes ADP and phosphate into ATP. The F_1-subunit of ATP synthase is called F_1-ATPase as it also independently catalyzes the reverse reaction in absence of F_O-part. The nearly 100% energy conversion efficiency of the molecular motor has attracted the attention of many physicists and biologists to explore the underlying thermodynamics. Recently, a new nonequilibrium equality derived by Harada and Sasa (Harada & Sasa, 2005) was applied to the experimental time series data on F_1-ATPase to extract heat flow to the environment. A phenomenological model for rotary motion was proposed and shown to reproduce key experimental features. Interested in the high efficiency of F_1-ATPase and the good performance of the corresponding model, we carried out a detailed computational study of the model to understand its behavior in a broader range of parameter values. We solved the model using a modified Gillespie algorithm for stochastic simulation and by integrating the Fokker-Planck equation. Various physical properties of the model, such as the relation between rotational velocity and parameters characterizing angular dependence (q) and ATP switching rates (W), the relation between two kinds of dissipation and rotational velocity, the negative heat flow from environment to system through ATP binding etc. are analyzed in detail. Importantly, we modified the driving potential to investigate the factors affecting the efficiency. Additionally, we found some inconsistences between properties of this model and previous studies and we could unify them by some adjustments, which may be useful for constructing more precise models in the future.
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Manolson, Morris F. "Characterization of the vacuolar H r-AtPase of higher plants." Thesis, McGill University, 1988. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=75838.

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The tonoplast H$ sp+$-ATPase of Beta vulgaris L. was partially purified by Triton X-100 solubilization and Sepharose 4B chromatography resulting in the enrichment of two polypeptides (57 and 67 kDa). Kinetic analysis of ($ alpha$-$ sp{32}$P) BzATP labeling identified the 57 kDa polypeptide as a nucleotide-binding subunit with a possible regulatory function. In addition, ($ sp{14}$C) DCCD-labeling identified a 16 kDa polypeptide as a putative transmembrane proton channel. It is concluded that the tonoplast H$ sp+$-ATPase is a multimer composed of at least three polypeptides.
Anti-57 and anti-67 kDa sera reacted with polypeptides of the corresponding size in bovine chromaffin granules, bovine clathrin-coated vesicles, and yeast vacuolar membranes, suggesting common structural features and common ancestry for endomembrane H$ sp+$-ATPases of different organelles and different phyla. Anti-57 serum was used to isolate a cDNA encoding the corresponding subunit from Arabidopsis. Protein sequence analysis revealed homologies between endomembrane, F$ sb0$F$ sb1$ and archaebacterial ATPases, suggesting that these different classes of ATPases have evolved from a common ancestor.
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Shi, Xianli, and 石现丽. "VCP/p97 is required for the timely degradation of p27 in G0/G1 to S phase transition in MCF-7 cell." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2014. http://hdl.handle.net/10722/208005.

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VCP/p97 works as a segregase to extract the ubiquitylated proteins from protein complexes, lipid membranes and chromosomes, thereby promoting their degradation or recycling. VCP/p97 plays essential roles in ubiquitin-dependent proteasome degradation, ERAD, autophagy, endocytosis, reassembly of ER, Golgi and nuclear envelop, and cell cycle regulation. In ubiquitin dependent proteasome degradation pathway, VCP/p97, as a special ubiquitin binding-shuttle factor, is required for the successful cell cycle progression in regulating IκB, CDT-1, Aurora B, and CDC25A. Here, we studied the role of VCP/p97 in G1 to S phase transition in MCF-7 human breast cancer cells. We found that VCP/p97 knockdown or inhibition by DBeQ, a potent VCP/p97 inhibitor, decreased cell proliferating rates and reduced S phase cell percentages in asynchronized MCF-7 cells.VCP/p97 inhibition by DBeQ also arrested cells at G1 phase in synchronized MCF-7 cells. These data suggest that VCP/p97 is required for G0/G1 to S phase transition in MCF-7 cells. In addition, in either asynchronized or synchronized MCF-7 cells, VCP/p97 knockdown or DBeQ treatment resulted in the accumulation of p21 and p27, two CDK inhibitors. Moreover, p27, not p21, knockdown in MCF-7 cells rescued the defects of S phase entry caused by VCP/p97 knockdown or DBeQ treatment. Taken together, our results suggest that VCP/p97 regulates the timely degradation of p27 to promote G1 to S phase transition in MCF-7 cells.
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Physiology
Master
Master of Philosophy
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Bergdall, Kristin Miller. "Cytochemical localization of adenosine triphosphatase in the nuclear envelope of necturus maculosus oocytes." Virtual Press, 1988. http://liblink.bsu.edu/uhtbin/catkey/544010.

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Cytochemical localization of nuclear-envelope nucleos-side triphosphatase was exhibited in the nuclear membrane and nuclear pores of the Necturus, maculosus oocyte. This enzyme is thought to promote nucleocytoplasmic transport of mRNA through the nuclear pores. Various tissue preparations were performed to assure optimum results of reaction product formation and preservation of tissue ultrastructure.Incubation of frozen oocyte sections in a modified Wachstein-Meisel medium resulted in positive staining of the nuclear membrane and the nucleoli as evidenced in light and electron micrographs. Whole oocytes were incubated in the Wachstein-Meisel medium and then embedded in Epon for electron microscopy. The whole oocytes contained reaction product associated with microvilli and plasma membranes. Exposure of manually isolated nuclei to the same experimental medium resulted in lead deposits in the nuclear envelope, the nuclear pores, and randomly dispersed among chromatin granules. Thus, these nuclear structures may play a role in transport of mRNA to the cytoplasm.
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Charlesworth, Thomas James. "Studies of F-ATPases from fungal mitochondria." Thesis, University of Cambridge, 2015. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.708466.

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Books on the topic "Adenosine triphosphatase"

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International, Seminar/Workshop on the Molecular Structure Function and Assembly of ATP Synthases (1987 Honolulu Hawaii). Molecular structure, function, and assembly of the ATP synthases. New York: Plenum Press, 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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Yoh, Wada, and Kaplan Jack H, eds. Handbook of ATPases: Biochemistry, cell biology, pathophysiology. Weinheim: Wiley-VCH., 2004.

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P, Marin Bernard, ed. Biochemistry and function of vacuolar adenosine-triphosphatase in fungi and plants. Berlin: Springer-Verlag, 1985.

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Marin, Bernard P., ed. Biochemistry and Function of Vacuolar Adenosine-Triphosphatase in Fungi and Plants. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70320-1.

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Tonomura, Yuji. Energy-transducing ATPases: Structure and kinetics. Cambridge: Cambridge University Press, 1986.

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International Workshop on Ecto-ATPases and Related Ectonucleotidases (2nd 1999 Diepenbeek, Belgium). Ecto-ATPases and related ectonucleotidases: Proceedings of the Second International Workshop on Ecto-ATPases and Related Ecotonucleotidases, held in Diepenbeek, Belgium, June 14-18, 1999. Maastricht, Netherlands: Shaker, 2000.

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F, Eccleston J., and Royal Society (Great Britain), eds. Nucleoside triphosphatases in energy transduction, cellular regulation and information transfer in biological systems: A discussion meeting of the Royal Society. London: Portland Press, 1992.

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L, Beaugé, Gadsby David C, and Garrahan Patricio J, eds. Na/K-ATPase and related transport ATPases: Structure, mechanism, and regulation. New York: New York Academy of Sciences, 1997.

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1932-, Mukohata Yasuo, Morales Manuel F, Fleischer Sidney, Yamada Kagaku Shinko Zaidān, and Yamada Conference on Energy Transduction in ATPases (11th : 1985 : Kōbe-shi, Japan), eds. Perspectives of biological energy transduction. Tokyo: Academic Press, 1987.

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Book chapters on the topic "Adenosine triphosphatase"

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Gunst, Susan J. "Sodium/Potassium-Dependent Adenosine Triphosphatase." In Airways Smooth Muscle: Peptide Receptors, Ion Channels and Signal Transduction, 255–71. Basel: Birkhäuser Basel, 1995. http://dx.doi.org/10.1007/978-3-0348-7362-8_12.

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Glynn, I. M. "The Na+, K+-Transporting Adenosine Triphosphatase." In The Enzymes of Biological Membranes, 35–114. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4601-2_2.

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Dreyfus, Georges. "The Mitochondrial F0–F1 Adenosine Triphosphatase: Isolation by Sepharose Hexylammonium Chromatography." In Recent Advances in Biological Membrane Studies, 499–510. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4979-2_29.

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Salyaev, R. K. "Plant Vacuole Membrane: Structure and Properties." In Biochemistry and Function of Vacuolar Adenosine-Triphosphatase in Fungi and Plants, 3–13. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70320-1_1.

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Poole, R. J., R. J. Mehlhorn, and L. Packer. "A Study of Transport in Tonoplast Vesicles Using Spin-Labelled Probes." In Biochemistry and Function of Vacuolar Adenosine-Triphosphatase in Fungi and Plants, 114–18. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70320-1_10.

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Bennett, Alan B., and Roger M. Spanswick. "The Use of Optical Probes to Monitor the Formation of pH Gradients and Membrane Potential in Tonoplast Membrane Vesicles." In Biochemistry and Function of Vacuolar Adenosine-Triphosphatase in Fungi and Plants, 119–28. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70320-1_11.

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Ohsumi, Yoshinori, Etsuko Uchida, and Yasuhiro Anraku. "The H+-Translocating ATPase in Vacuolar Membranes of Saccharomyces Cerevisiae." In Biochemistry and Function of Vacuolar Adenosine-Triphosphatase in Fungi and Plants, 131–40. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70320-1_12.

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Bowman, E. J., and B. J. Bowman. "The H+-Translocating ATPase in Vacuolar Membranes of Neurospora Crassa." In Biochemistry and Function of Vacuolar Adenosine-Triphosphatase in Fungi and Plants, 141–50. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70320-1_13.

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Gidrol, X., B. Marin, H. Chréstin, and J. D’Auzac. "The Functioning of Tonoplast H+-Translocating ATPase from Hevea Latex in Physiological Conditions." In Biochemistry and Function of Vacuolar Adenosine-Triphosphatase in Fungi and Plants, 151–63. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70320-1_14.

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Briskin, Donald P., and Ronald J. Poole. "Proton Pump and ATPase Activities in Tonoplast Vesicles from Storage Tissue of Red Beet." In Biochemistry and Function of Vacuolar Adenosine-Triphosphatase in Fungi and Plants, 164–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70320-1_15.

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Conference papers on the topic "Adenosine triphosphatase"

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Zhao, Bo. "MicroRNA-275 directly targets sarco/endoplasmic reticulum Ca2+adenosine triphosphatase (SERCA) to control key functions in the mosquito gut." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.112707.

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Sundaresan, Vishnu Baba, Stephen Andrew Sarles, and Donald J. Leo. "Chemoelectrical energy conversion of adenosine triphosphate." In The 14th International Symposium on: Smart Structures and Materials & Nondestructive Evaluation and Health Monitoring, edited by Yuji Matsuzaki, Mehdi Ahmadian, and Donald J. Leo. SPIE, 2007. http://dx.doi.org/10.1117/12.715715.

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Casey, Abigail, and Gregory E. Triplett. "Real time analysis of phosphate transitions from adenosine triphosphate." In Integrated Sensors for Biological and Neural Sensing, edited by Hooman Mohseni. SPIE, 2021. http://dx.doi.org/10.1117/12.2575994.

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Lázár, Zsófia, András Bikov, Márta Orosz, Gabriella Gálffy, Zsolt I. Komlósi, György Losonczy, and Ildiko Horvath. "Adenosine Triphosphate Concentration Of Exhaled Breath Condensate In Asthma." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4275.

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Holderfield, Matthew, and Kanika Sharma. "Abstract 1365: Sensitivity of oncogenic KRAS to adenosine triphosphate suppression." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1365.

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Belete, Hewan A., and Rolf D. Hubmayr. "Adenosine Triphosphate (ATP) Promotes Plasma Membrane Wound Repair By A P2Y2R Dependent Mechanism." 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.a5110.

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Santi, Abdul Wahid Wahab, Indah Raya, and Ahyar Ahmad. "Synthesis and interaction of adenosine-5'-triphosphate with rare earth metal Europium (Eu3+)." In INTERNATIONAL CONFERENCE ON SCIENCE AND APPLIED SCIENCE (ICSAS2020). AIP Publishing, 2020. http://dx.doi.org/10.1063/5.0030666.

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Olotu, Cynthia, Anne Mecklenburg, Sven Hammerschmidt, Alwin E. Goetz, and Rainer Kiefmann. "Streptococcus Pneumoniae Inhibits Adenosine-Triphosphate (ATP)-Mediated Calcium Release In Alveolar Epithelial Cells." 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.a1780.

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Maciaszek, J. L., B. Andemariam, and G. Lykotrafitis. "Red Blood Cell Surface Receptor Expression of BCAM/Lu is Regulated by Protein Kinase A Activity." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14311.

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Abstract:
Irregular sickle red blood cells (RBCs) can contribute to the pathogenesis of vasoocclusion and other complications of sickle cell disease (SCD) via abnormal adherence to the vascular endothelium. It has previously been demonstrated that epinephrine enhances SCD RBC adhesion by activating the BCAM/Lu and ICAM-4 surface receptors [1–2]. Epinephrine acts on the RBC β2-adrenergic receptor, thereby activating Gas proteins that stimulate adenylyl cyclase (AC). This enzyme catalyzes the conversion of adenosine triphosphate (ATP) to cyclic adenosine monophosphate (cAMP), leading to protein kinase A (PKA) activation, an intermediate step in the upregulation of BCAM/Lu and ICAM-4 mediated adhesion. The interaction of BCAM/Lu with the α5 chain of laminin may contribute to vaso-occlusive events in SCD due to overexpression of BCAM on SCD RBCs.
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Suzuki, Y., I. Lewkowich, S. Lajoie, Y. Inoue, A. Nathan, E. Peterson, K. Dienger, and M. Wills-Karp. "House Dust Mite Extract Promotes Adenosine-5′-Triphosphate (ATP) Release from Airway Epithelial Cells." 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.a1407.

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