Literatura académica sobre el tema "V-ATPase"
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Artículos de revistas sobre el tema "V-ATPase"
Russell, V. E., U. Klein, M. Reuveni, D. D. Spaeth, M. G. Wolfersberger y W. R. Harvey. "Antibodies to mammalian and plant V-ATPases cross react with the V-ATPase of insect cation-transporting plasma membranes". Journal of Experimental Biology 166, n.º 1 (1 de mayo de 1992): 131–43. http://dx.doi.org/10.1242/jeb.166.1.131.
Texto completoParra, Karlett J., Chun-Yuan Chan y Jun Chen. "Saccharomyces cerevisiae Vacuolar H+-ATPase Regulation by Disassembly and Reassembly: One Structure and Multiple Signals". Eukaryotic Cell 13, n.º 6 (4 de abril de 2014): 706–14. http://dx.doi.org/10.1128/ec.00050-14.
Texto completoCollaco, Anne M., Peter Geibel, Beth S. Lee, John P. Geibel y Nadia A. Ameen. "Functional vacuolar ATPase (V-ATPase) proton pumps traffic to the enterocyte brush border membrane and require CFTR". American Journal of Physiology-Cell Physiology 305, n.º 9 (1 de noviembre de 2013): C981—C996. http://dx.doi.org/10.1152/ajpcell.00067.2013.
Texto completoSautin, Yuri Y., Ming Lu, Andrew Gaugler, Li Zhang y Stephen L. Gluck. "Phosphatidylinositol 3-Kinase-Mediated Effects of Glucose on Vacuolar H+-ATPase Assembly, Translocation, and Acidification of Intracellular Compartments in Renal Epithelial Cells". Molecular and Cellular Biology 25, n.º 2 (15 de enero de 2005): 575–89. http://dx.doi.org/10.1128/mcb.25.2.575-589.2005.
Texto completoGogarten, J. P., T. Starke, H. Kibak, J. Fishman y L. Taiz. "Evolution and isoforms of V-ATPase subunits." Journal of Experimental Biology 172, n.º 1 (1 de noviembre de 1992): 137–47. http://dx.doi.org/10.1242/jeb.172.1.137.
Texto completoKane, Patricia M. "The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H+-ATPase". Microbiology and Molecular Biology Reviews 70, n.º 1 (marzo de 2006): 177–91. http://dx.doi.org/10.1128/mmbr.70.1.177-191.2006.
Texto completoNelson, Nathan y William R. Harvey. "Vacuolar and Plasma Membrane Proton-Adenosinetriphosphatases". Physiological Reviews 79, n.º 2 (1 de abril de 1999): 361–85. http://dx.doi.org/10.1152/physrev.1999.79.2.361.
Texto completoForgac, M. "Structure, mechanism and regulation of the clathrin-coated vesicle and yeast vacuolar H(+)-ATPases". Journal of Experimental Biology 203, n.º 1 (1 de enero de 2000): 71–80. http://dx.doi.org/10.1242/jeb.203.1.71.
Texto completoAbe, Michiko, Mayu Saito, Ayana Tsukahara, Shuka Shiokawa, Kazuma Ueno, Hiroki Shimamura, Makoto Nagano, Junko Y. Toshima y Jiro Toshima. "Functional complementation reveals that 9 of the 13 human V-ATPase subunits can functionally substitute for their yeast orthologs". Journal of Biological Chemistry 294, n.º 20 (5 de abril de 2019): 8273–85. http://dx.doi.org/10.1074/jbc.ra118.006192.
Texto completoImada, Katsumi, Tohru Minamino, Yumiko Uchida, Miki Kinoshita y Keiichi Namba. "Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator". Proceedings of the National Academy of Sciences 113, n.º 13 (16 de marzo de 2016): 3633–38. http://dx.doi.org/10.1073/pnas.1524025113.
Texto completoTesis sobre el tema "V-ATPase"
Schempp, Christina Maria. "The V-ATPase inhibitor archazolid". Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-168586.
Texto completoFirmino, Kelly Cristina Silva. "Processos osmorregulatórios no caranguejo Dilocarcinus pagei (Decapoda, Trichodactylidae), um antigo invasor da água doce: estudo das atividades (Na,K)-ATPase e V-ATPase branquiais". Universidade de São Paulo, 2009. http://www.teses.usp.br/teses/disponiveis/59/59138/tde-19082009-112806/.
Texto completoCrustacean arose in the sea but, during evolution, several species invaded lower salinity biotopes, reaching fresh water. The ability of crustaceans to successfully colonize the freshwater biotope depends on efficient mechanisms of hyperosmoregulation. In dilute media, crustaceans\' hemolymph osmolality and ionic composition reflect a balance between diffusive and urinary ion losses, and active ion capture through the gills. The gill (Na,K)- ATPase plays a pivotal role in Na+ capture from dilute environments and its kinetic characteristics are under investigation in recent years, although freshwater crab enzymes are poorly known. According to the most recent model, the apparent affinity for Na+ is the most variable kinetic parameter among gill enzymes from different species, and reflects the salinity of the species\' habitat. Thus, enzymes from species which are well adapted to freshwater usually present higher affinities for Na+. However, several recent results are incompatible with this model. On the other hand, it has been proposed that a V-ATPase is also involved in Na+ capture through the gills of hololimnetic crustaceans. This enzyme is almost completely unknown: its kinetic characteristics have not been studied yet and the relationship between the magnitude of its activity in the gills and the external medium salinity has not been established. This work aimed to characterize the (Na,K)-ATPase and V-ATPase from the posterior gill from the holimnetic crab Dilocarcinus pagei, considered an old fresh water colonizer. The (Na,K)- ATPase was characterized in animals maintained in fresh water, in order to establish a comparison of its kinetic properties with those of enzymes from other crab species that inhabit more saline media. This comparison may enhance our understanding of the biochemical adaptations associated to fresh water invasion. V-ATPase was characterized in animals kept in fresh water or exposed for varying time intervals to a medium of 21? salinity, or else acclimated for 10 days to media of different salinities (5-21?), aiming to establish a relationship between the enzyme specific activity in the gill tissue and the external salinity, and also investigate the mechanisms involved in enzyme activity regulation. The analysis of D. pagei gill microsomes in a continuous-density sucrose gradient revealed two protein peaks (25-35% and 35-45% sucrose), both showing K+-phosphatase, (Na,K)-ATPase and V-ATPase activities. These results indicate the presence of membrane fractions of distinct densities, both presenting the main ion pumps involved in Na+ capture. These membranes may originate from different places in the asymmetric posterior gill epithelium from this crab. Western compared to those reported for other freshwater animals, but similar to those found for estuarine/marine species. In contrast, the apparent affinity for K+ is 2.5 to 5-fold higher than those estimated for species that inhabit more saline media, and is apparently more related to the animals\' habitat than Na+ affinity. This possibility is consistent with the location of the (Na,K)-ATPase in crabs gill tissue, with K+ binding sites exposed to the hemolymph, allowing the direct modulation of enzyme activity by hemolymph K+ concentration. In contrast to data reported for other crab species, D. pagei gill (Na,K)-ATPase activity was not synergistically stimulated by K+ and NH4 +. However, the presence of one of these ions in the reaction medium results in an increase of about 3-fold in the apparent affinity of the enzyme for the other. This kinetic characteristic may be physiologically relevant to assure the transport of both ions, even in the presence of elevated concentrations of the other. Ouabain (3 mmol L-1) inhibited total ATPase activity (? 78%) through a biphasic curve (KI= 6.21 ± 0.32 mol L-1 and 101.2 ± 5.1 mol L-1) reinforcing previous results suggesting the presence of two isoenzymes in the microsomal preparations. A biphasic inhibition by orthovanadate (10 mol L-1) to about 15% residual activity was also observed. Optimal pH for D. pagei gill V-ATPase activity was 7.5. The modulation of enzyme activity of the animal kept in fresh water by ATP (V= 26.5 ± 1.3 U mg-1; K0.5= 3.9 ± 0.2 mmol L-1) and Mg2+ (V = 27.9 ± 1.4 U mg-1; K0.5 =0.80 ± 0.04 mmol L-1) occurred with positive cooperativity. The inhibition of the orthovanadate insensitive ATPase activity by bafilomycin A1 followed a monophasic curve (KI= 55.0 ± 2.8 nmol L-1). About 44 % of total ATPase activity was inhibited, corresponding to the V-ATPase. Dilocarcinus pagei gill V-ATPase activity substantially decreased in response to animal\'s exposure to 21? salinity. After 1h exposure, the activity diminished about 3-fold, reaching 4- fold after 24h, indicating the action of efficient short-time regulation mechanisms. Interestingly, V-ATPase activity was about 2-fold higher after 120h exposure, compared to 24h, although 2- fold lower compared to that estimated in fresh water. After 240h, the activity returned to the low levels observed for 1 and 24 h, indicating efficient long-term regulation. Besides the decrease in specific activity, it was also observed an increase in enzyme\'s apparent affinity for ATP (12 fold) and Mg2+ (3 fold) in response to animal\'s exposure to 21? salinity. Simultaneously, the enzyme\'s affinity for bafilomycin A1 increased up to 190-fold. We propose that, in response to salinity alteration, conformational changes take place both in V1 (in which the ATP and Mg2+ binding sites are located) and V0 (which contains the bafilomycin A1 bindind site), resulting in higher exposition of the inhibitor binding site and also higher affinity for Mg2+ and ATP. As the affinity increases are observed after just 1h exposure, this regulatory mechanism seems to be independent of protein expression and, thus, should not be related to the expression of distinct isoforms of some enzyme subunit. The lowering of gill V-ATPase activity in D. pagei in response to exposure to an elevated salinity is consistent with the mechanisms proposed for the role of this enzyme in active Na+ capture in hololimnetic crustaceans. After 10 days at 21, the gill microsomal fractions still show a little V-ATPase activity, possibly related to acid-base regulation and ammonia excretion processes. The results obtained for the acclimation of D. pagei for 10 days at salinities in the range 5 to 21? also showed a substantial decrease of V-ATPase activity in response to the increase in medium salinity. However, except for 5?, it was not observed an increase of enzyme\'s affinity for bafilomycin, suggesting that this alteration is limited to shorter periods of exposure. However, a significant increase in the enzyme\'s affinity for ATP and Mg2+ was also observed.
Reineke, Stephan. "Topologie und Regulation der Manduca sexta V-ATPase". Doctoral thesis, [S.l.] : [s.n.], 2002. http://deposit.ddb.de/cgi-bin/dokserv?idn=970381719.
Texto completoMiles, Anna Louise. "V-ATPase regulation of Hypoxia Inducible transcription Factors". Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/283217.
Texto completoVoß, Martin. "Regulation der vakuolären H(+)-ATPase durch reversible Proteinphosphorylierung". Phd thesis, Universität Potsdam, 2008. http://opus.kobv.de/ubp/volltexte/2008/1961/.
Texto completoThe vacuolar-type H+-ATPase (V-ATPase) is a multimeric enzyme that can be found in nearly every eukaryotic cell. It catalyses the active electrogenic transport of protons across membranes and is essential for a multitude of physiological processes. A fundamental mechanism to regulate V-ATPase activity is the reversible dissociation of the holoenzyme into an integral proton conducting VO-complex and a cytosolic V1-complex that hydrolyses ATP and thus energises proton translocation. Subunit C occurs isolated in the cytoplasm upon dissociation of the V-ATPase complexes and seems to be critical for the formation of active holoenzymes. In the salivary glands of the blowfly Calliphora vicina the V-ATPase is involved in fluid secretion. In secretory cells, formation of the V-ATPase holoenzyme is stimulated by the hormone serotonin (5-HT). The effect of 5-HT on V-ATPase activity is mediated by protein kinase A (PKA) and persists for the duration of the 5-HT stimulus. In this study, it was shown by phosphoprotein stainings and two-dimensional electrophoresis that subunit C of the V-ATPase becomes phosphorylated by PKA upon exposure of blowfly salivary glands to 5-HT. Parallel to the phosphorylation event, subunit C translocates from the cytoplasm to the apical plasma membrane for the assembly of active V-ATPase holoenzymes. Using immunofluorescence staining, it could be shown that PKA catalytic subunit translocates as well to the apical membrane upon 5-HT stimulation. To examine which protein phosphatase counteracts PKA, luminal pH-measurements were carried out. Based on the results with protein phosphatase inhibitors and esterified chelating agents of bivalent cations, it may be concluded that a protein phosphatase 2C is involved in the process leading to V-ATPase inactivation. Phosphoprotein stainings revealed that dephosphorylation of subunit C is likewise catalysed by a protein phosphatase 2C. Therefore the dephosphorylation of subunit C seems to promote dissociation of VO- and V1-complexes. Finally, luminal pH-measurements and supplemental biochemical experiments revealed a Ca2+/calcineurin-mediated modulation of the cAMP/PKA signalling cascade and an influence of intracellular calcium on the V-ATPase activity.
Owegi, Margaret. "Site-directed mutagenesis of yeast V-ATPase subunit d". Virtual Press, 2005. http://liblink.bsu.edu/uhtbin/catkey/1319550.
Texto completoDepartment of Chemistry
Gerle, Christoph. "Two-dimensional crystallization of intact Thermus thermophilus V-ATPase". 京都大学 (Kyoto University), 2006. http://hdl.handle.net/2433/144145.
Texto completoWiedmann, Romina Madeleine. "Anticancer effects of the V-ATPase inhibitor Archazolid B". Diss., Ludwig-Maximilians-Universität München, 2011. http://nbn-resolving.de/urn:nbn:de:bvb:19-139515.
Texto completoCheng, Tak Sum. "Molecular identification and characterization of novel osteoclast V-ATPase subunits". University of Western Australia. School of Surgery and Pathology, 2008. http://theses.library.uwa.edu.au/adt-WU2008.0068.
Texto completoSTORACI, ALESSANDRA MARIA. "FURTHER INSIGHT INTO V-ATPASE ROLE IN GLIOMA STEM CELLS". Doctoral thesis, Università degli Studi di Milano, 2020. http://hdl.handle.net/2434/703269.
Texto completoLibros sobre el tema "V-ATPase"
Chakraborti, Sajal y Naranjan S. Dhalla, eds. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-24780-9.
Texto completo(Editor), Luis A. Beauge, David C. Gadsby (Editor) y Patricio J. Garrahan (Editor), eds. Na/K-Atpase and Related Transport Atpases: Structure, Mechanism, and Regulation (Annals of the New York Academy of Sciences, V. 834). New York Academy of Sciences, 1997.
Buscar texto completo(Editor), Peter Leth Jorgensen, Steven J. D. Karlish (Editor) y Arvid Bernhard Maunsbach (Editor), eds. Na,K-Atpase and Related Cation Pumps: Structure, Function, and Regulatory Mechanisms (Annals of the New York Academy of Sciences, V. 986). New York Academy of Sciences, 2003.
Buscar texto completoOchotny, Noelle Marie. Effects of human a3 and a4 mutations that result in osteopetrosis and distal renal tubular acidosis on yeast V-ATPase expression and activity. 2006.
Buscar texto completoChakraborti, Sajal y Naranjan S. Dhalla. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Springer, 2015.
Buscar texto completoDhalla, Naranjan S. y Sajal Chakraborti. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Springer London, Limited, 2016.
Buscar texto completoChakraborti, Sajal y Naranjan S. Dhalla. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Springer, 2019.
Buscar texto completoCapítulos de libros sobre el tema "V-ATPase"
Kartner, Norbert y Morris F. Manolson. "The Vacuolar Proton ATPase (V-ATPase): Regulation and Therapeutic Targeting". En Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 407–37. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_20.
Texto completoMartínez-Zaguilán, Raul y Souad R. Sennoune. "Vacuolar H+-ATPase Signaling in Cancer". En Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 371–92. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_18.
Texto completoProdromou, Chrisostomos y Rhodri M. L. Morgan. "“Tuning” the ATPase Activity of Hsp90". En Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 469–90. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_23.
Texto completoRahman, Suhaila, Ichiro Yamato y Takeshi Murata. "Function and Regulation of Mammalian V-ATPase Isoforms". En Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 283–99. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_15.
Texto completoPagliarani, Alessandra, Salvatore Nesci, Fabiana Trombetti y Vittoria Ventrella. "Thiol-Related Regulation of the Mitochondrial F1FO-ATPase Activity". En Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 441–58. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_21.
Texto completoSun, Yirong. "F1F0-ATPase Functions Under Markedly Acidic Conditions in Bacteria". En Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 459–68. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_22.
Texto completoManzoor, Nikhat. "Plasma Membrane ATPase: Potential Target for Antifungal Drug Therapy". En Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 519–30. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_26.
Texto completoKannan, Subburaj, Vijayan Elimban, Pascal Bogaert, Monika Bartekova y Naranjan S. Dhalla. "Regulation of Ca2+/Mg2+ Ecto-ATPase in the Heart". En Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 117–34. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_8.
Texto completoCarafoli, Ernesto. "The Plasma Membrane Calcium ATPase: Historical Appraisal and Some New Concepts". En Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 3–11. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_1.
Texto completoKurtz, Ira, Irina Rogova, Vladimir Turygin, Jingbo Huang, Natalia Abuladze y Alexander Pushkin. "Renal H+-ATPase Function, Regulation, and Role in Distal Renal Tubular Acidosis". En Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 505–18. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_25.
Texto completoActas de conferencias sobre el tema "V-ATPase"
Stein, B., T. Pap, M. George, WJ Parak, O. Müller, S. Gay y WK Aicher. "THU0110 V-atpase inhibitor bafilomycin a1 reduces proton secretion in fibroblasts". En Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.987.
Texto completoBertolini, Irene, Andrea Terrasi, Andrea Di Cristofori, Silvano Bosari y Valentina Vaira. "Abstract 2889: V-ATPase control of EV signaling in glioma stem cells". En 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.am2017-2889.
Texto completoOnken, Horst. "V-ATPase and Na+/K+-ATPase energize postprandial fluid absorption from the isolated midgut of female yellow fever mosquitoes (Aedes aegypti)". En 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.93236.
Texto completoIbrahim, Safaa A., Valerie Riehl, Sylvia Schneiderman y Kenneth D. Beaman. "Abstract 2845: Role of neutrophil associated a2 isoform of V-ATPase in cancer". En Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-2845.
Texto completoErnst, Stefan, Claire Batisse, Nawid Zarrabi, Bettina Böttcher y Michael Börsch. "Regulatory assembly of the vacuolar proton pump V o V 1 -ATPase in yeast cells by FLIM-FRET". En BiOS, editado por Ammasi Periasamy, Peter T. C. So y Karsten König. SPIE, 2010. http://dx.doi.org/10.1117/12.841169.
Texto completoStoraci, A., I. Bertolini, M. Caroli, S. Ferrero y V. Vaira. "PO-080 V-ATPase G1 expression in human glioma stem cells correlates with ERK activation". En Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.123.
Texto completoLi, X., I. Thornell, R. Villacreses Rada, C. Brommel, L. Lu, S. Mather, A. Ehler, P. Karp, M. Welsh y J. Zabner. "V-Type ATPase Mediates Airway Surface Liquid Acidification in Cultured Pig Small Airway Epithelial Cells". En American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a2573.
Texto completoStransky, Laura A. y Michael Forgac. "Abstract 27: Understanding mechanisms of nutrient homeostasis: Amino acid availability and regulation of V-ATPase activity". En Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-27.
Texto completoWang, Fangyang, Ying Yang, Gabriel Boudagh, Eeva-Liisa Eskelinen, Daniel J. Klionsky y Sami N. Malek. "Abstract 1939: Follicular Lymphoma-associated mutations in the V-ATPase assembly factor VMA21 activate autophagic flux". En Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1939.
Texto completoChang, Yu-Chan y Michael Hsiao. "Abstract 1092: V-ATPase family regulates lysosomal exocytosis and neutralizes with tumor-infiltrating lymphocytes for glioblastoma cells". En Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-1092.
Texto completoInformes sobre el tema "V-ATPase"
Nelson, Nathan y Randy Schekman. Functional Biogenesis of V-ATPase in the Vacuolar System of Plants and Fungi. United States Department of Agriculture, septiembre de 1996. http://dx.doi.org/10.32747/1996.7574342.bard.
Texto completoSadot, Einat, Christopher Staiger y Mohamad Abu-Abied. Studies of Novel Cytoskeletal Regulatory Proteins that are Involved in Abiotic Stress Signaling. United States Department of Agriculture, septiembre de 2011. http://dx.doi.org/10.32747/2011.7592652.bard.
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