Relevant bibliographies by topics / V-ATPase

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'V-ATPase'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 March 2023

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Journal articles on the topic "V-ATPase"

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Russell, V. E., U. Klein, M. Reuveni, D. D. Spaeth, M. G. Wolfersberger, and 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, no. 1 (May 1, 1992): 131–43. http://dx.doi.org/10.1242/jeb.166.1.131.

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In immunobiochemical blots, polyclonal antibodies against subunits of plant and mammalian vacuolar-type ATPases (V-ATPases) cross-react strongly with corresponding subunits of larval Manduca sexta midgut plasma membrane V-ATPase. Thus, rabbit antiserum against Kalanchoe daigremontiana tonoplast V-ATPase holoenzyme cross-reacts with the 67, 56, 40, 28 and 20 kDa subunits of midgut V-ATPase separated by SDS-PAGE. Antisera against bovine chromaffin granule 72 and 39 kDa V-ATPase subunits cross-react with the corresponding 67 and 43 kDa subunits of midgut V-ATPase. Antisera against the 57 kDa subu
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Parra, Karlett J., Chun-Yuan Chan, and Jun Chen. "Saccharomyces cerevisiae Vacuolar H+-ATPase Regulation by Disassembly and Reassembly: One Structure and Multiple Signals." Eukaryotic Cell 13, no. 6 (April 4, 2014): 706–14. http://dx.doi.org/10.1128/ec.00050-14.

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ABSTRACTVacuolar H+-ATPases (V-ATPases) are highly conserved ATP-driven proton pumps responsible for acidification of intracellular compartments. V-ATPase proton transport energizes secondary transport systems and is essential for lysosomal/vacuolar and endosomal functions. These dynamic molecular motors are composed of multiple subunits regulated in part by reversible disassembly, which reversibly inactivates them. Reversible disassembly is intertwined with glycolysis, the RAS/cyclic AMP (cAMP)/protein kinase A (PKA) pathway, and phosphoinositides, but the mechanisms involved are elusive. The
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Collaco, Anne M., Peter Geibel, Beth S. Lee, John P. Geibel, and 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, no. 9 (November 1, 2013): C981—C996. http://dx.doi.org/10.1152/ajpcell.00067.2013.

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Vacuolar ATPases (V-ATPases) are highly conserved proton pumps that regulate organelle pH. Epithelial luminal pH is also regulated by cAMP-dependent traffic of specific subunits of the V-ATPase complex from endosomes into the apical membrane. In the intestine, cAMP-dependent traffic of cystic fibrosis transmembrane conductance regulator (CFTR) channels and the sodium hydrogen exchanger (NHE3) in the brush border regulate luminal pH. V-ATPase was found to colocalize with CFTR in intestinal CFTR high expresser (CHE) cells recently. Moreover, apical traffic of V-ATPase and CFTR in rat Brunner's g
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Sautin, Yuri Y., Ming Lu, Andrew Gaugler, Li Zhang, and 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, no. 2 (January 15, 2005): 575–89. http://dx.doi.org/10.1128/mcb.25.2.575-589.2005.

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ABSTRACT Vacuolar H+-ATPases (V-ATPases) are a family of ATP-driven proton pumps. They maintain pH gradients between intracellular compartments and are required for proton secretion out of the cytoplasm. Mechanisms of extrinsic control of V-ATPase are poorly understood. Previous studies showed that glucose is an important regulator of V-ATPase assembly in Saccharomyces cerevisiae. Human V-ATPase directly interacts with aldolase, providing a coupling mechanism for glucose metabolism and V-ATPase function. Here we show that glucose is a crucial regulator of V-ATPase in renal epithelial cells and
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Gogarten, J. P., T. Starke, H. Kibak, J. Fishman, and L. Taiz. "Evolution and isoforms of V-ATPase subunits." Journal of Experimental Biology 172, no. 1 (November 1, 1992): 137–47. http://dx.doi.org/10.1242/jeb.172.1.137.

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The structure of V- and F-ATPases/ATP synthases is remarkably conserved throughout evolution. Sequence analyses show that the V- and F-ATPases evolved from the same enzyme that was already present in the last common ancestor of all known extant life forms. The catalytic and non-catalytic subunits found in the dissociable head groups of both V-ATPases and F-ATPases are paralogous subunits, i.e. these two types of subunits evolved from a common ancestral gene. The gene duplication giving rise to these two genes (i.e. those encoding the catalytic and non-catalytic subunits) pre-dates the time of
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Kane, Patricia M. "The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H+-ATPase." Microbiology and Molecular Biology Reviews 70, no. 1 (March 2006): 177–91. http://dx.doi.org/10.1128/mmbr.70.1.177-191.2006.

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SUMMARY All eukaryotic cells contain multiple acidic organelles, and V-ATPases are central players in organelle acidification. Not only is the structure of V-ATPases highly conserved among eukaryotes, but there are also many regulatory mechanisms that are similar between fungi and higher eukaryotes. These mechanisms allow cells both to regulate the pHs of different compartments and to respond to changing extracellular conditions. The Saccharomyces cerevisiae V-ATPase has emerged as an important model for V-ATPase structure and function in all eukaryotic cells. This review discusses current kno
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Nelson, Nathan, and William R. Harvey. "Vacuolar and Plasma Membrane Proton-Adenosinetriphosphatases." Physiological Reviews 79, no. 2 (April 1, 1999): 361–85. http://dx.doi.org/10.1152/physrev.1999.79.2.361.

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The vacuolar H+-ATPase (V-ATPase) is one of the most fundamental enzymes in nature. It functions in almost every eukaryotic cell and energizes a wide variety of organelles and membranes. V-ATPases have similar structure and mechanism of action with F-ATPase and several of their subunits evolved from common ancestors. In eukaryotic cells, F-ATPases are confined to the semi-autonomous organelles, chloroplasts, and mitochondria, which contain their own genes that encode some of the F-ATPase subunits. In contrast to F-ATPases, whose primary function in eukaryotic cells is to form ATP at the expens
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Forgac, M. "Structure, mechanism and regulation of the clathrin-coated vesicle and yeast vacuolar H(+)-ATPases." Journal of Experimental Biology 203, no. 1 (January 1, 2000): 71–80. http://dx.doi.org/10.1242/jeb.203.1.71.

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The vacuolar H(+)-ATPases (or V-ATPases) are a family of ATP-dependent proton pumps that carry out acidification of intracellular compartments in eukaryotic cells. This review is focused on our work on the V-ATPases of clathrin-coated vesicles and yeast vacuoles. The coated-vesicle V-ATPase undergoes trafficking to endosomes and synaptic vesicles, where it functions in receptor recycling and neurotransmitter uptake, respectively. The yeast V-ATPase functions to acidify the central vacuole and is necessary both for protein degradation and for coupled transport processes across the vacuolar memb
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Abe, Michiko, Mayu Saito, Ayana Tsukahara, Shuka Shiokawa, Kazuma Ueno, Hiroki Shimamura, Makoto Nagano, Junko Y. Toshima, and 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, no. 20 (April 5, 2019): 8273–85. http://dx.doi.org/10.1074/jbc.ra118.006192.

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Vacuolar-type H+-ATPase (V-ATPase) is a highly conserved proton pump responsible for acidification of intracellular organelles and potential drug target. It is a multisubunit complex comprising a cytoplasmic V1 domain responsible for ATP hydrolysis and a membrane-embedded Vo domain that contributes to proton translocation across the membrane. Saccharomyces cerevisiae V-ATPase is composed of 14 subunits, deletion of any one of which results in well-defined growth defects. As the structure of V-ATPase and the function of each subunit have been well-characterized in yeast, this organism has been
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Imada, Katsumi, Tohru Minamino, Yumiko Uchida, Miki Kinoshita, and 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, no. 13 (March 16, 2016): 3633–38. http://dx.doi.org/10.1073/pnas.1524025113.

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FliI and FliJ form the FliI6FliJ ATPase complex of the bacterial flagellar export apparatus, a member of the type III secretion system. The FliI6FliJ complex is structurally similar to the α3β3γ complex of F1-ATPase. The FliH homodimer binds to FliI to connect the ATPase complex to the flagellar base, but the details are unknown. Here we report the structure of the homodimer of a C-terminal fragment of FliH (FliHC2) in complex with FliI. FliHC2shows an unusually asymmetric homodimeric structure that markedly resembles the peripheral stalk of the A/V-type ATPases. The FliHC2–FliI hexamer model
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Dissertations / Theses on the topic "V-ATPase"

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Schempp, Christina Maria. "The V-ATPase inhibitor archazolid." Diss., Ludwig-Maximilians-Universität München, 2014. http://nbn-resolving.de/urn:nbn:de:bvb:19-168586.

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Fighting metastasis is a major challenge in cancer therapy and novel therapeutic targets and drugs are highly appreciated. Resistance of invasive cells to anoikis, a particular type of apoptosis induced by loss of cell-extracellular matrix (ECM) contact, is a major prerequisite for their metastatic spread. Inducing anoikis in metastatic cancer cells is therefore a promising therapeutic approach. The vacuolar H+-ATPase (V-ATPase), a proton pump located at the membrane of acidic organelles, has recently come to focus as an anti-metastatic cancer target. As V-ATPase inhibitors have shown to prev
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Firmino, 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/.

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Os crustáceos são originariamente marinhos; ao longo da evolução, diversas espécies invadiram ambientes de salinidades menores, chegando à água doce. A capacidade dos crustáceos colonizarem com sucesso o ambiente dulcícola depende do desenvolvimento de mecanismos eficientes de hiperosmorregulação. A osmolalidade e a composição iônica da hemolinfa de um crustáceo, em meios diluídos, refletem o equilíbrio dinâmico entre a perda de íons por difusão e pela urina e sua reabsorção do meio externo, através das brânquias. A (Na,K)-ATPase branquial desempenha um papel chave no processo de captura de Na
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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.

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Miles, Anna Louise. "V-ATPase regulation of Hypoxia Inducible transcription Factors." Thesis, University of Cambridge, 2018. https://www.repository.cam.ac.uk/handle/1810/283217.

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Metazoans have evolved conserved mechanisms to promote cell survival under low oxygen tensions by initiating a transcriptional cascade centered on the action of Hypoxia Inducible transcription Factors (HIFs). In aerobic conditions, HIFs are inactivated by ubiquitin-proteasome-mediated degradation of their a subunit, which is dependent on prolyl hydroxylation by 2-oxoglutarate (2-OG) and Fe(II)-dependent prolyl hydroxylases (PHDs). In hypoxia, HIF-$\alpha$ is no longer hydroxylated and is therefore stabilised, activating a global transcriptional response to ensure cell survival. Interestingly,
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Voß, Martin. "Regulation der vakuolären H(+)-ATPase durch reversible Proteinphosphorylierung." Phd thesis, Universität Potsdam, 2008. http://opus.kobv.de/ubp/volltexte/2008/1961/.

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Die vakuoläre Protonen-ATPase, kurz V-ATPase, ist ein multimerer Enzymkomplex, der in fast jeder eukaryotischen Zelle zu finden ist und den aktiven elektrogenen Transport von Protonen über Membranen katalysiert. Die Aktivität der V-ATPase ist essentiell für eine Vielzahl physiologischer Prozesse. Ein grundlegender Mechanismus zur Regulation der V-ATPase-Aktivität ist die reversible Dissoziation des Holoenzyms in den integralen VO-Komplex, der als Protonenkanal dient, und den cytosolischen V1-Komplex, der ATP hydrolysiert und somit den Protonentransport energetisiert. Die Untereinheit C, die im
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Owegi, Margaret. "Site-directed mutagenesis of yeast V-ATPase subunit d." Virtual Press, 2005. http://liblink.bsu.edu/uhtbin/catkey/1319550.

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V-ATPases are enzymes found in all eukaryotic cells. They are organized into a peripheral membrane complex (V1) and an integral membrane complex (V0). VI is responsible for ATP hydrolysis and generates the energy used by Vo to pump protons from the cytosol into the vacuole. Subunit d is a component of Vo possibly located at the interface between V 1 and V. in the V-ATPase complex. We hypothesize that subunit d could be involved in the structural and functional coupling of VI and Vo. This was tested by generating point mutations along the open reading frame of subunit d from yeast. The mutation
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Gerle, Christoph. "Two-dimensional crystallization of intact Thermus thermophilus V-ATPase." 京都大学 (Kyoto University), 2006. http://hdl.handle.net/2433/144145.

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Wiedmann, 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.

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Cheng, 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.

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[Truncated abstract] Osteoclasts are multinucleated giant cells responsible for the resorption of the mineralized bone matrix during the process of bone remodelling. During activation towards bone resorption, polarization of the osteoclast results in the formation of a unique plasma membrane, the ruffled border, the actual resorptive organelle of the osteoclast. Through this domain protons are actively pumped into the resorption lacuna creating an acidic microenvironment that favours the dissolution of the mineralized bone matrix. The polarised secretion of protons is carried out by the action
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STORACI, 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.

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V-ATPase is a proton pump mainly localized on lysosomes and on plasma membrane of specialized cells. It is responsible of proton translocation and acidification of intra- and extra-cellular environment. Our group demonstrated that the over-expression of the subunit G1 (V1G1) is involved in the maintenance of the stem cell niche in glioblastoma (GBM) and correlates with poor prognosis in GBM patients. In this work we aimed to elucidate the role of V-ATPase in GBM stem cells from a functional perspective. We demonstrated that neurospheres (NS) with higher levels of V1G1 subunit (High-V1G1), comp
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Books on the topic "V-ATPase"

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Chakraborti, Sajal, and 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.

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(Editor), Luis A. Beauge, David C. Gadsby (Editor), and 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.

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(Editor), Peter Leth Jorgensen, Steven J. D. Karlish (Editor), and 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.

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Ochotny, 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.

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Chakraborti, Sajal, and Naranjan S. Dhalla. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Springer, 2015.

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Dhalla, Naranjan S., and Sajal Chakraborti. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Springer London, Limited, 2016.

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Chakraborti, Sajal, and Naranjan S. Dhalla. Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Springer, 2019.

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Book chapters on the topic "V-ATPase"

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Kartner, Norbert, and Morris F. Manolson. "The Vacuolar Proton ATPase (V-ATPase): Regulation and Therapeutic Targeting." In 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.

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Martínez-Zaguilán, Raul, and Souad R. Sennoune. "Vacuolar H+-ATPase Signaling in Cancer." In 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.

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Prodromou, Chrisostomos, and Rhodri M. L. Morgan. "“Tuning” the ATPase Activity of Hsp90." In 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.

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Rahman, Suhaila, Ichiro Yamato, and Takeshi Murata. "Function and Regulation of Mammalian V-ATPase Isoforms." In 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.

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Pagliarani, Alessandra, Salvatore Nesci, Fabiana Trombetti, and Vittoria Ventrella. "Thiol-Related Regulation of the Mitochondrial F1FO-ATPase Activity." In 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.

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Sun, Yirong. "F1F0-ATPase Functions Under Markedly Acidic Conditions in Bacteria." In 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.

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Manzoor, Nikhat. "Plasma Membrane ATPase: Potential Target for Antifungal Drug Therapy." In 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.

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Kannan, Subburaj, Vijayan Elimban, Pascal Bogaert, Monika Bartekova, and Naranjan S. Dhalla. "Regulation of Ca2+/Mg2+ Ecto-ATPase in the Heart." In 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.

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Carafoli, Ernesto. "The Plasma Membrane Calcium ATPase: Historical Appraisal and Some New Concepts." In 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.

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Kurtz, Ira, Irina Rogova, Vladimir Turygin, Jingbo Huang, Natalia Abuladze, and Alexander Pushkin. "Renal H+-ATPase Function, Regulation, and Role in Distal Renal Tubular Acidosis." In 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.

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Conference papers on the topic "V-ATPase"

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Stein, B., T. Pap, M. George, WJ Parak, O. Müller, S. Gay, and WK Aicher. "THU0110 V-atpase inhibitor bafilomycin a1 reduces proton secretion in fibroblasts." In 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.

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Bertolini, Irene, Andrea Terrasi, Andrea Di Cristofori, Silvano Bosari, and Valentina Vaira. "Abstract 2889: V-ATPase control of EV signaling in glioma stem cells." 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.am2017-2889.

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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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Ibrahim, Safaa A., Valerie Riehl, Sylvia Schneiderman, and Kenneth D. Beaman. "Abstract 2845: Role of neutrophil associated a2 isoform of V-ATPase in cancer." In 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.

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Ernst, Stefan, Claire Batisse, Nawid Zarrabi, Bettina Böttcher, and Michael Börsch. "Regulatory assembly of the vacuolar proton pump V o V 1 -ATPase in yeast cells by FLIM-FRET." In BiOS, edited by Ammasi Periasamy, Peter T. C. So, and Karsten König. SPIE, 2010. http://dx.doi.org/10.1117/12.841169.

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Storaci, A., I. Bertolini, M. Caroli, S. Ferrero, and V. Vaira. "PO-080 V-ATPase G1 expression in human glioma stem cells correlates with ERK activation." In 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.

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Li, X., I. Thornell, R. Villacreses Rada, C. Brommel, L. Lu, S. Mather, A. Ehler, P. Karp, M. Welsh, and J. Zabner. "V-Type ATPase Mediates Airway Surface Liquid Acidification in Cultured Pig Small Airway Epithelial Cells." In 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.

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Stransky, Laura A., and Michael Forgac. "Abstract 27: Understanding mechanisms of nutrient homeostasis: Amino acid availability and regulation of V-ATPase activity." In 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.

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Wang, Fangyang, Ying Yang, Gabriel Boudagh, Eeva-Liisa Eskelinen, Daniel J. Klionsky, and Sami N. Malek. "Abstract 1939: Follicular Lymphoma-associated mutations in the V-ATPase assembly factor VMA21 activate autophagic flux." In 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.

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Chang, Yu-Chan, and Michael Hsiao. "Abstract 1092: V-ATPase family regulates lysosomal exocytosis and neutralizes with tumor-infiltrating lymphocytes for glioblastoma cells." In 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.

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Reports on the topic "V-ATPase"

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Nelson, Nathan, and Randy Schekman. Functional Biogenesis of V-ATPase in the Vacuolar System of Plants and Fungi. United States Department of Agriculture, September 1996. http://dx.doi.org/10.32747/1996.7574342.bard.

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The vacuolar H+-ATPase (V-ATPase) is one of the most fundamental enzymes in nature. It pumps protons into the vacuolar system of eukaryotic cells and provides the energy for numerous transport systems. Through our BARD grant we discovered a novel family of membrane chaperones that modulate the amount of membrane proteins. We also elucidated the mechanism by which assembly factors guide the membrane sector of V-ATPase from the endoplasmic reticulum to the Golgi apparatus. The major goal of the research was to understand the mechanism of action and biogenesis of V-ATPase in higher plants and fun
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Sadot, Einat, Christopher Staiger, and Mohamad Abu-Abied. Studies of Novel Cytoskeletal Regulatory Proteins that are Involved in Abiotic Stress Signaling. United States Department of Agriculture, September 2011. http://dx.doi.org/10.32747/2011.7592652.bard.

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In the original proposal we planned to focus on two proteins related to the actin cytoskeleton: TCH2, a touch-induced calmodulin-like protein which was found by us to interact with the IQ domain of myosin VIII, ATM1; and ERD10, a dehydrin which was found to associate with actin filaments. As reported previously, no other dehydrins were found to interact with actin filaments. In addition so far we were unsuccessful in confirming the interaction of TCH2 with myosin VIII using other methods. In addition, no other myosin light chain candidates were found in a yeast two hybrid survey. Nevertheless
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