Results 191 to 200 of about 309,313 (234)
Journal of Experimental Biology, 1992 ABSTRACT Protons migrate much faster than other ions through water, ice and water-lined membrane channels because they participate in hydrogen bonding and H+H2O exchange. Similarly, hydrogen bonding enables protons with amino, carbonyl, phosphoryl and sulfonyl residues to influence critically the charge, conformation and stability of ...
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Current Opinion in Nephrology and Hypertension, 1999
The H+,K+-ATPases comprise a group of integral membrane proteins that belong to the X+,K+-ATPase subfamily of P-type cation-transporting ATPases. Although these H+,K+-ATPase isoforms share approximately 60-70% amino acid identity, they exhibit discrete kinetic and pharmacological properties when expressed in heterologous systems.
Thomas D. DuBose +2 more
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The H+,K+-ATPases comprise a group of integral membrane proteins that belong to the X+,K+-ATPase subfamily of P-type cation-transporting ATPases. Although these H+,K+-ATPase isoforms share approximately 60-70% amino acid identity, they exhibit discrete kinetic and pharmacological properties when expressed in heterologous systems.
Thomas D. DuBose +2 more
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The interaction between the mitochondrial ATPase (F1) and the ATPase inhibitor
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 19731. The naturally occurring mitochondrial ATPase inhibitor inhibits the mitochondrial ATPase (F1) non-competitively. 2. The interaction between inhibitor and inhibitor-depleted F1 or submitochondrial particles is diminished when the ratio of ATP/ADP is low or when energy is generated by substrate oxidation. 3.
B. de Boer +2 more
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2016
The Na+/K+-ATPase is a universally expressed membrane protein responsible for maintaining the low intracellular Na+ and high intracellular K+ concentrations required for multitude of cellular functions. Besides, the Na+ /K+-ATPase helps maintaining resting potential, import of amino acids, glucose, and other nutrients into cells and regulates cellular ...
Obradović, Milan +4 more
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The Na+/K+-ATPase is a universally expressed membrane protein responsible for maintaining the low intracellular Na+ and high intracellular K+ concentrations required for multitude of cellular functions. Besides, the Na+ /K+-ATPase helps maintaining resting potential, import of amino acids, glucose, and other nutrients into cells and regulates cellular ...
Obradović, Milan +4 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 ...
Jian-Zhong Shao +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 ...
Jian-Zhong Shao +2 more
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Science Signaling, 2010
By promoting an inhibitory autophosphorylation event, the ATPase XP24 decreases immune responses mediated by the XA21 pattern recognition receptor.
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By promoting an inhibitory autophosphorylation event, the ATPase XP24 decreases immune responses mediated by the XA21 pattern recognition receptor.
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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.
Lincoln Taiz, Nathan Nelson
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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.
Lincoln Taiz, Nathan Nelson
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Journal of Bioenergetics and Biomembranes, 1981
F1-ATPases are large multimeric proteins that can be isolated from the membrane bound system that catalyzes the phosphorylation of ADP by inorganic phosphate in bacteria, plants, and mitochondria. They can be visualized in electron micrographs of the inner mitochondrial membranes where they appear as large protruding spheres 90 A in diameter.
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F1-ATPases are large multimeric proteins that can be isolated from the membrane bound system that catalyzes the phosphorylation of ADP by inorganic phosphate in bacteria, plants, and mitochondria. They can be visualized in electron micrographs of the inner mitochondrial membranes where they appear as large protruding spheres 90 A in diameter.
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Properties of ATPase in chloroplasts
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1969Abstract 1. 1. Mg 2+ -ATPase (light-triggered Mg 2+ -dependent ATPase) activity in chloroplasts was stimulated by atebrin, NH 4 Cl and gramicidin when the uncouplers were added after light triggering. The stimulation was followed in time by inhibition when the reaction took place in the dark. 2. 2.
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Current Biology, 1992
Proton pumps that belong to the families of F-ATPases and V-ATPases operate without the formation of a phosphorylated intermediate and contain several subunits grouped into distinct catalytic and membrane sectors. Recent studies on the structure and molecular biology of V-ATPases shed light not only on the structure-function relations between the two ...
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Proton pumps that belong to the families of F-ATPases and V-ATPases operate without the formation of a phosphorylated intermediate and contain several subunits grouped into distinct catalytic and membrane sectors. Recent studies on the structure and molecular biology of V-ATPases shed light not only on the structure-function relations between the two ...
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