Results 31 to 40 of about 10,440,305 (287)
PLoS ONE, 2013 The ATPase 6 accessory protein 2 (ATP6AP2)/(pro)renin receptor (PRR) is essential for the biogenesis of active vacuolar H(+)-ATPase (V-ATPase). Genetic deletion of ATP6AP2/PRR causes V-ATPase dysfunction and compromises vesicular acidification.
Kenichiro Kinouchi +12 more
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An extended nomenclature for mammalian V-ATPase subunit genes and splice variants. [PDF]
PLoS ONE, 2010 The vacuolar-type H(+)-ATPase (V-ATPase) is a multisubunit proton pump that is involved in both intra- and extracellular acidification processes throughout the body.
Kevin C Miranda +2 more
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V-ATPases and osteoclasts: ambiguous future of V-ATPases inhibitors in osteoporosis
Theranostics, 2018 Vacuolar ATPases (V-ATPases) play a critical role in regulating extracellular acidification of osteoclasts and bone resorption. The deficiencies of subunit a3 and d2 of V-ATPases result in increased bone density in humans and mice. One of the traditional drug design strategies in treating osteoporosis is the use of subunit a3 inhibitor. Recent findings
Duan, Xiaohong +3 more
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Regulation of V-ATPase assembly and function of V-ATPases in tumor cell invasiveness
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2016 V-ATPases are ATP-driven proton pumps that function within both intracellular compartments and the plasma membrane in a wide array of normal physiological and pathophysiological processes. V-ATPases are composed of a peripheral V(1) domain that hydrolyzes ATP and an integral V(0) domain that transports protons.
Christina, McGuire +3 more
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Regulation of V-ATPase activity
Frontiers in Bioscience, 2017 V-ATPases are ATP-driven proton pumps present in both intracellular and cell surface membranes of eukaryotes that function in many normal and disease processes. V-ATPases are large, multi-subunit complexes composed of a peripheral domain (V1) that hydrolyzes ATP and a membrane integral domain (V0) that translocates protons.
Christina, McGuire +3 more
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V-ATPase engagement in autophagic processes [PDF]
Autophagy, 2011 The proton pumping activity of V-ATPase is responsible for acidification of the lysosome/vacuole. The low lumenal pH of this organelle stimulates the activity of a battery of resident hydrolases responsible for the degradation of various nonselective and selective cargos delivered by autophagic processes.
Dalibor, Mijaljica +2 more
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Conformational studies of peptides representing a segment of TM7 from Vo-H+-V-ATPase in SDS micelles [PDF]
, 2009 The conformation of a transmembrane peptide, sMTM7, encompassing the cytoplasmic hemi-channel domain of the seventh transmembrane section of subunit a from V-ATPase from Saccharomyces cerevisiae solubilized in SDS solutions was studied by circular ...
Jong, E.R., de +7 more
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Retrieval of the vacuolar H-ATPase from phagosomes revealed by live cell imaging. [PDF]
PLoS ONE, 2010 BackgroundThe vacuolar H+-ATPase, or V-ATPase, is a highly-conserved multi-subunit enzyme that transports protons across membranes at the expense of ATP.
Margaret Clarke +3 more
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Regulation and Isoform Function of the V-ATPases [PDF]
Biochemistry, 2010 The vacuolar (H(+))-ATPases are ATP-dependent proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane of eukaryotic cells. Intracellular V-ATPases play an important role in normal physiological processes such as receptor-mediated endocytosis, intracellular membrane trafficking, pro-hormone ...
Masashi, Toei +2 more
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F-actin reorganization by V-ATPase inhibition in prostate cancer
Biology Open, 2017 The vacuolar ATPase (V-ATPase) proton pump sustains cellular pH homeostasis, and its inhibition triggers numerous stress responses. However, the cellular mechanisms involved remain largely elusive in cancer cells.
Yamhilette Licon-Munoz +3 more
doaj +1 more source