Results 301 to 310 of about 547,455 (357)
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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.
T D, DuBose, J, Gitomer, J, Codina
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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.
T D, DuBose, J, Gitomer, J, Codina
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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
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Current Opinion in Nephrology and Hypertension, 1996
At least four unique H,K-ATPases have been cloned and are expressed in several tissues. Recent findings have enhanced our appreciation of the roles of H,K-ATPases in the kidney with respect to their molecular identities, functional properties, segmental and intrarenal distribution, and regulatory features. The major role of the H,K-ATPases expressed in
T D, DuBose, J, Codina
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At least four unique H,K-ATPases have been cloned and are expressed in several tissues. Recent findings have enhanced our appreciation of the roles of H,K-ATPases in the kidney with respect to their molecular identities, functional properties, segmental and intrarenal distribution, and regulatory features. The major role of the H,K-ATPases expressed in
T D, DuBose, J, Codina
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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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Nihon rinsho. Japanese journal of clinical medicine, 1997
Gastric H+, K+ -ATPase comprised of alpha- and beta-subunits was functionally expressed in an animal cell-line. When glutamic acid (345) of the alpha-subunit was mutated to glutamine, the affinity of K+ decreased 10-fold, indicating that this residue in the 4th transmembrane domain engages in the determination of the K+ affinity.
N, Takeguchi, S, Asano, M, Morii
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Gastric H+, K+ -ATPase comprised of alpha- and beta-subunits was functionally expressed in an animal cell-line. When glutamic acid (345) of the alpha-subunit was mutated to glutamine, the affinity of K+ decreased 10-fold, indicating that this residue in the 4th transmembrane domain engages in the determination of the K+ affinity.
N, Takeguchi, S, Asano, M, Morii
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Actomyosin ATPase. II. Fiber typing by histochemical ATPase reaction
Muscle & Nerve, 1980AbstractA new method for fiber typing based on staining for actomyosin Ca, Mg‐ATPase is presented. Inclusion of ethanol in the medium enhanced the differentiation of type 2A and 2B fibers. With this technique, type 1, 2A, and 2B fibers can be distinguished in a single‐step procedure for human biopsy samples.
K, Mabuchi, F A, Sréter
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Regulatory proteins of F1F0-ATPase: Role of ATPase inhibitor
Journal of Bioenergetics and Biomembranes, 1990An intrinsic ATPase inhibitor inhibits the ATP-hydrolyzing activity of mitochondrial F1F0-ATPase and is released from its binding site on the enzyme upon energization of mitochondrial membranes to allow phosphorylation of ADP. The mitochondrial activity to synthesize ATP is not influenced by the absence of the inhibitor protein.
T, Hashimoto, Y, Yoshida, K, Tagawa
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Regulation of Ca2+-ATPases,V-ATPases and F-ATPases
2016The biological membranes of cellular organization enfold an important group of membrane proteins called the ATPases, which are not only versatile in maintaining chemical gradient and electrical potential across the membrane but also bring metabolites necessary for cell metabolism and drive out toxins, waste products and solutes that otherwise can curb ...
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Journal of Biochemistry, 1995
Sliding machines composed of F-actin and myosin or microtubules and kinesin or dynein convert the free energy of ATP hydrolysis into sliding movements and mechanical work. Development of optical microscopy with micromanipulation techniques has made possible direct observation of single events of sliding exhibited by single sliding machines.
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Sliding machines composed of F-actin and myosin or microtubules and kinesin or dynein convert the free energy of ATP hydrolysis into sliding movements and mechanical work. Development of optical microscopy with micromanipulation techniques has made possible direct observation of single events of sliding exhibited by single sliding machines.
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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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