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Myocardin reverses insulin resistance and ameliorates cardiomyopathy by increasing IRS-1 expression in a murine model of lipodystrophy caused by adipose deficiency of vacuolar H<sup>+</sup>-ATPase V0d1 subunit. [PDF]
TheranosticsYuan W +16 more
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The International Journal of Biochemistry & Cell Biology, 2008
The vacuolar H(+)-ATPase (V-ATPase) is a universal component of eukaryotic organisms, which is present in both intracellular compartments and the plasma membrane. In the latter, its proton-pumping action creates the low intravacuolar pH, benefiting many processes such as, membrane trafficking, protein degradation, renal acidification, bone resorption ...
Yong-Tao, Xiao +2 more
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The vacuolar H(+)-ATPase (V-ATPase) is a universal component of eukaryotic organisms, which is present in both intracellular compartments and the plasma membrane. In the latter, its proton-pumping action creates the low intravacuolar pH, benefiting many processes such as, membrane trafficking, protein degradation, renal acidification, bone resorption ...
Yong-Tao, Xiao +2 more
openaire +2 more sources
Trends in Biochemical Sciences, 1989
Since the pioneering work of Peter Mitchell 1, the central role of proton gradients in biological energy transduc- tion has been widely ackrLowledged. The enzymes directly involved in generating and harnessing the energy of proton gradients (H+-ATPases), are found in nearly all cells and presumably appeared very early in cell evolution 2.
N, Nelson, L, Taiz
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Since the pioneering work of Peter Mitchell 1, the central role of proton gradients in biological energy transduc- tion has been widely ackrLowledged. The enzymes directly involved in generating and harnessing the energy of proton gradients (H+-ATPases), are found in nearly all cells and presumably appeared very early in cell evolution 2.
N, Nelson, L, Taiz
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Inherited disorders of the H+-ATPase
Current Opinion in Nephrology and Hypertension, 2002The alpha-intercalated cell in the distal nephron shares a number of molecular features with the osteoclast, including site-limited proton pumps that are present at high density. These are multisubunit H -ATPases, which are essential for acid-base homeostasis and for the maintenance of normal bone turnover.
Katherine J, Borthwick, Fiona E, Karet
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Structure and function of H+-ATPase
Journal of Bioenergetics and Biomembranes, 1979(1) Extensive studies on proton-translocating ATPase (H+-ATPase) revealed that H+-ATPase is an energy transforming device universally distributed in membranes of almost all kinds of cells. (2) Crystallization of the catalytic portion (F1) of H+-ATPase showed that F1 is a hexagonal molecule with a central hole.
Y, Kagawa +3 more
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Vacuolar H+-ATPase Signaling Pathway in Cancer
Current Protein & Peptide Science, 2012Up-regulated aerobic glycolysis is a hallmark of malignant cancers. Little is understood about the reasons why malignant tumors up-regulate glycolysis and acidify their microenvironment. Signaling pathways involved in glucose changes are numerous. However, the identity of the internal glucose signal remains obscure.
Souad R, Sennoune +1 more
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Selective Inhibition of Osteoclast Vacuolar H+-ATPase
Current Pharmaceutical Design, 2002The proton pump expressed on the plasma membrane of bone resorbing osteoclasts, and which mediates the acidification of the extracellular environment in resorption lacuna, belongs to the family of vacuolar H(+)-ATPases, which are enzymes ubiquitously distributed among all cells and are evolutionary conserved.
Carlo, Farina, S, Gagliardi
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Intrinsic Fluorescence of the Chloroplast H+-ATPase
Archives of Biochemistry and Biophysics, 1995We have examined the intrinsic fluorescence properties of a highly purified chloroplast H(+)-ATPase (CF0F1) preparation [R. D. Kirch and P. Graber (1992) Acta Physiol. Scand. 746, 9-12). Unlike the catalytic CF1 portion alone, CF0F1 fluorescence was dominated by tryptophan fluorescence both at 277-nm excitation, favoring tyrosine excitation, and at 295-
Kirch, Robert Dale +3 more
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Kidney Vacuolar H+-ATPase: Physiology and Regulation
Seminars in Nephrology, 2006The vacuolar H(+)-ATPase is a multisubunit protein consisting of a peripheral catalytic domain (V(1)) that binds and hydrolyzes adenosine triphosphate (ATP) and provides energy to pump H(+) through the transmembrane domain (V(0)) against a large gradient.
Patricia, Valles +3 more
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