Results 211 to 220 of about 220,750 (263)
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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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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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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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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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Cellular physiology of the renal H+ATPase
Current Opinion in Nephrology and Hypertension, 2009Vacuolar-type H+ATPases are multisubunit macromolecules that play an essential role in renal acid-base homeostasis. Other cellular processes also rely on the proton pumping ability of H+ATPases to acidify organellar or lumenal spaces. Several diseases, including distal renal tubular acidosis, osteoporosis and wrinkly skin syndrome, are due to mutations
Katherine G, Blake-Palmer +1 more
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Biogenesis of the yeast vacuolar H+-ATPase
Journal of Experimental Biology, 1992ABSTRACT Achieving an understanding of the biosynthesis, assembly and intracellular targeting of the vacuolar H+-ATPase is critical for understanding the distribution of acidic compartments and the regulation of organelle acidification.
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2021
This thesis was scanned from the print manuscript for digital preservation and is copyright the author. Researchers can access this thesis by asking their local university, institution or public library to make a request on their behalf. Monash staff and postgraduate students can use the link in the References field.
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This thesis was scanned from the print manuscript for digital preservation and is copyright the author. Researchers can access this thesis by asking their local university, institution or public library to make a request on their behalf. Monash staff and postgraduate students can use the link in the References field.
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2014
Vacuolar H+-ATPase Assembly Structure of Prokaryotic V type ATPase/synthase The function of V-ATPase in the degradation of gluconeogenic enzymes in the yeast vacuole The Role of Vacuolar ATPase in the Regulation of Npt2a Trafficking Cytosolic pH regulated by glucose promotes V-ATPase assembly Vacuolar H+-ATPase (V-ATPase) activated by glucose, a ...
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Vacuolar H+-ATPase Assembly Structure of Prokaryotic V type ATPase/synthase The function of V-ATPase in the degradation of gluconeogenic enzymes in the yeast vacuole The Role of Vacuolar ATPase in the Regulation of Npt2a Trafficking Cytosolic pH regulated by glucose promotes V-ATPase assembly Vacuolar H+-ATPase (V-ATPase) activated by glucose, a ...
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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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Assembly and Regulation of the Yeast Vacuolar H+-ATPase
Journal of Bioenergetics and Biomembranes, 2003The yeast vacuolar proton-translocating ATPase (V-ATPase) is an excellent model for V-ATPases in all eukaryotic cells. Activity of the yeast V-ATPase is reversibly down-regulated by disassembly of the peripheral (V1) sector, which contains the ATP-binding sites, from the membrane (V0) sector, which contains the proton pore.
Patricia M, Kane, Anne M, Smardon
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