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The plasma membrane proton-translocating ATPase
Cellular and Molecular Life Sciences, 2000 Living cells require membranes and membrane transporters for the maintenance of life. After decades of biochemical scrutiny, the structures and molecular mechanisms by which membrane transporters catalyze transmembrane solute movements are beginning to be understood.
G A Scarborough
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Regulation of proton-translocating V-ATPases [PDF]
Journal of Experimental Biology, 1997 ABSTRACT Vacuolar-type ATPases (V-ATPases) are proton-translocating enzymes that occur in the endomembranes of all eukaryotes and in the plasma membranes of many eukaryotes. They are multisubunit, heteromeric proteins composed of two structural domains, a peripheral, catalytic V1 domain and a membrane-spanning Vo domain.
Hans Merzendorfer +4 more
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Crystallization, structure and dynamics of the proton-translocating P-type ATPase
Journal of Experimental Biology, 2000 ABSTRACT Large single three-dimensional crystals of the dodecylmaltoside complex of the Neurospora crassa plasma membrane H+-ATPase (H+P-ATPase) can be grown in polyethylene-glycol-containing solutions optimized for moderate supersaturation of both the protein surfaces and detergent micellar region.
Gene A. Scarborough
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The proton translocating ATPase responsible for urinary acidification.
Journal of Biological Chemistry, 1982 H+ secretion by the turtle urinary bladder is produced by a proton pump located in the luminal membrane. We show that a microsomal fraction of these cells contains an electrogenic proton translocating ATPase that is inhibited by dicyclohexylcarbodiimide but not oligomycin or vanadate.
Stephen L. Gluck +2 more
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Assembly of a functional F1 of the proton-translocating ATPase of Escherichia coli.
Journal of Biological Chemistry, 1985 Assembly of the F1 portion of the proton-translocating ATPase of Escherichia coli was examined in vivo. Analysis of strains lacking genes which specify the Fo polypeptides a, b, and c showed that the F1 subunits were able to assemble into a complex in the absence of the Fo subunits.
Daniel J. Klionsky, R D Simoni
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Advances in targeting the vacuolar proton-translocating ATPase (V-ATPase) for anti-fungal therapy [PDF]
Frontiers in Pharmacology, 2014 Vacuolar proton-translocating ATPase (V-ATPase) is a membrane-bound, multi-subunit enzyme that uses the energy of ATP hydrolysis to pump protons across membranes. V-ATPase activity is critical for pH homeostasis and organelle acidification as well as for generation of the membrane potential that drives secondary transporters and cellular metabolism.
Summer R. Hayek +2 more
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A proton-translocating ATPase regulates pH of the bacterial cytoplasm.
Journal of Biological Chemistry, 1985 Regulatory mechanisms of cytoplasmic pH in Streptococcus faecalis with no respiratory chain were investigated. In a mutant defective in cytoplasmic alkalization conducted by a proton-translocating ATPase (H+-ATPase), the cytoplasmic pH is approximately 0.4 to 0.5 pH units lower than the medium pH, at pH 5.5 to 9.0.
Hiroshi Kobayashi
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A proton-translocating H+-ATPase is involved in C6 Glial pH regulation
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1998 Glial cells extrude acid equivalents to maintain pHi. Although four mechanisms have been described so far, pHi-control under physiological conditions is still not sufficiently explained. We therefore investigated whether a H+-translocating ATPase is involved in glial pHi homeostasis using an established glial cell line (C6 glioma).
Christopher Volk +2 more
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V1-situated Stalk Subunits of the Yeast Vacuolar Proton-translocating ATPase [PDF]
Journal of Biological Chemistry, 1997 The proton-translocating ATPase of the yeast vacuole is an enzyme complex consisting of a large peripheral membrane sector (V1) and an integral membrane sector (V0), each composed of multiple subunits. The V1 sector contains subunits that hydrolyze ATP, whereas the V0 sector contains subunits that translocate protons across the membrane.
John J. Tomashek +4 more
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Purification and reconstitution of the proton-translocating ATPase of Golgi-enriched membranes. [PDF]
Proceedings of the National Academy of Sciences, 1988 Kidney cortex microsomes enriched in Golgi markers and probably also containing endosomes were isolated by cell fractionation and found to contain a proton-translocating ATPase that was inhibited by N-ethylmaleimide (NEM). This NEM-sensitive ATPase was solubilized with n-octyl glucoside and purified using anion-exchange sievorptive chromatography on ...
Graeme P. Young +2 more
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