PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8381483-0 1993 Decreased erythrocyte Na+,K(+)-ATPase activity associated with cellular potassium loss in extremely low birth weight infants with nonoliguric hyperkalemia. Potassium 72-81 dynein axonemal heavy chain 8 Homo sapiens 31-37 7836457-2 1995 Potassium is required for optimal ATPase activity. Potassium 0-9 dynein axonemal heavy chain 8 Homo sapiens 34-40 8253841-5 1993 When coexpressed in Xenopus oocytes with a beta subunit isolated from the same cDNA library, the ATPase is able to transport rubidium (a potassium surrogate) inward, and hydrogen outward, leading to alkalization of the intracellular compartment and acidification of the external medium. Potassium 137-146 dynein axonemal heavy chain 8 Homo sapiens 97-103 8381483-9 1993 Low Na+,K(+)-ATPase activity was associated with lower intracellular potassium/serum potassium ratios (p = 0.006), higher serum potassium values (p = 0.02), and lower intracellular potassium concentration (p = 0.009). Potassium 69-78 dynein axonemal heavy chain 8 Homo sapiens 13-19 8381483-9 1993 Low Na+,K(+)-ATPase activity was associated with lower intracellular potassium/serum potassium ratios (p = 0.006), higher serum potassium values (p = 0.02), and lower intracellular potassium concentration (p = 0.009). Potassium 85-94 dynein axonemal heavy chain 8 Homo sapiens 13-19 8381483-9 1993 Low Na+,K(+)-ATPase activity was associated with lower intracellular potassium/serum potassium ratios (p = 0.006), higher serum potassium values (p = 0.02), and lower intracellular potassium concentration (p = 0.009). Potassium 85-94 dynein axonemal heavy chain 8 Homo sapiens 13-19 8381483-9 1993 Low Na+,K(+)-ATPase activity was associated with lower intracellular potassium/serum potassium ratios (p = 0.006), higher serum potassium values (p = 0.02), and lower intracellular potassium concentration (p = 0.009). Potassium 85-94 dynein axonemal heavy chain 8 Homo sapiens 13-19 1835657-5 1991 Second, we measured the kinetics of 45Ca2+ dissociation from phosphorylated ATPase in a "chase" experiment, by isotopic dilution of calcium under turnover conditions in the presence of potassium. Potassium 185-194 dynein axonemal heavy chain 8 Homo sapiens 76-82 2959578-4 1987 Calcium transport and ATPase share the following properties: (i) magnesium was required with a K0.5 of 0.7 mM and maximal pumping ATPase activity at 5 mM Mg-ATP; (ii) at saturating magnesium concentrations, calcium increased ATP splitting activity up to three times with an apparent K0.5 close to 0.3 microM calcium; (iii) potassium stimulated the high calcium affinity Mg2+-dependent ATPase and calcium transport. Potassium 323-332 dynein axonemal heavy chain 8 Homo sapiens 22-28 2140359-2 1990 At pH 7.0 and 5 degrees C, in the absence of potassium and magnesium, the Ca-ATPase of the sarcoplasmic reticulum slowly hydrolyzes the Ca.ATP at a rate of 0.05 s-1. Potassium 45-54 dynein axonemal heavy chain 8 Homo sapiens 77-83 35110381-1 2022 ATP1A1 encodes the alpha1 subunit of the sodium-potassium ATPase, an electrogenic cation pump highly expressed in the nervous system. Potassium 48-57 dynein axonemal heavy chain 8 Homo sapiens 58-64 2553694-1 1989 In view of the striking homology among various ion-translocating ATPases including Na,K-ATPase, Ca-ATPase, and H,K-ATPase, and the recent evidence that protons can replace cytoplasmic sodium as well as potassium in the reaction mechanism of the Na,K-ATPase (Polvani, C., and Blostein, R. (1988) J. Biol. Potassium 202-211 dynein axonemal heavy chain 8 Homo sapiens 96-121 2974728-7 1988 Addition of calcium to the MgATP complex of the ATPase caused an increase in the FITC inactivation rate, implying that during turnover there is a larger fraction of unliganded enzyme present, i.e., substrate binding is weaker (Ks is larger). Potassium 227-229 dynein axonemal heavy chain 8 Homo sapiens 48-54 2977004-6 1988 Potassium ions produced a further activation of the Zn2+-dependent ATPase system by about 10%. Potassium 0-9 dynein axonemal heavy chain 8 Homo sapiens 67-73 3158341-1 1985 The mechanism of sarcoplasmic reticulum (SR) ATPase Mg2+-dependent phosphorylation from Pi was investigated in the presence of 15% v/v dimethyl sulfoxide at pH 6, 20 degrees C, and in the absence of potassium. Potassium 199-208 dynein axonemal heavy chain 8 Homo sapiens 45-51 2948563-6 1986 It is suggested that this low-affinity acceleration by ATP of the crucial step leading to dissociation of transported Ca2+ is the specific interaction responsible for the low-affinity acceleration of overall ATPase activity generally observed in the presence of potassium at neutral pH. Potassium 262-271 dynein axonemal heavy chain 8 Homo sapiens 208-214 2983540-1 1985 Studies in rats have shown that fecal potassium excretion and colonic mucosa Na-K-ATPase activity are elevated during dietary potassium loading and in chronic renal insufficiency. Potassium 126-135 dynein axonemal heavy chain 8 Homo sapiens 82-88 2983540-6 1985 Like others, however, we found a two-fold increase in Na-K-ATPase activity in potassium loaded rats. Potassium 78-87 dynein axonemal heavy chain 8 Homo sapiens 59-65 3158341-8 1985 In the absence of solvent, the interaction of magnesium with the calcium-deprived ATPase was also characterized from the point of view of phosphoenzyme formation from ATP or Pi at pH 7 in the absence of potassium: we found that calcium-independent phosphorylation was slower when phosphate was added to SR vesicles preincubated with magnesium that when magnesium was added to vesicles preincubated with phosphate, suggesting that preincubation with magnesium had depleted the phosphate-reactive conformation of the ATPase. Potassium 203-212 dynein axonemal heavy chain 8 Homo sapiens 82-88 142633-3 1977 Previous reports of activation of the NaK ATPase at low potassium and high sodium are probably not due to phenytoin but to a potassium contamination in the phenytoin solution. Potassium 56-65 dynein axonemal heavy chain 8 Homo sapiens 42-48 7162976-4 1982 The criteria of effectiveness were clinical, electrocardiographic (reversal of the ventricular fibrillation), biochemical (simultaneous and opposite changes in extra- and intracellular potassium levels, suggesting that ATPase inhibition by digitalis is a reversible process) and toxicological: there was an increase in digitoxin serum levels suggesting displacement of the drug from tissue sites to plasma and other extracellular compartments where the Fab fragments are distributed, and Fab-bound digitoxin appeared fairly rapidly in the urine, which suggested shunting of the normal hepatic metabolic pathway. Potassium 185-194 dynein axonemal heavy chain 8 Homo sapiens 219-225 6462181-1 1982 It has been shown that the induction of earlier described system of potassium-dependent transport of hydrogen ions in mitochondria at low pH values of the incubation medium is inhibited by the inhibitors of mitochondria respiratory chain and ATPase. Potassium 68-77 dynein axonemal heavy chain 8 Homo sapiens 242-248 6462181-3 1982 The uncoupler (FCCP) turns the effect of ATPase inhibitors to the efflux of potassium ions and acceleration of mitochondria respiration under experimental conditions. Potassium 76-85 dynein axonemal heavy chain 8 Homo sapiens 41-47 6462181-5 1982 The data obtained are explained in terms of the postulate that under experimental conditions along with the system of potassium-dependent ion transport there appears leakage of protons through the ATPase channel. Potassium 118-127 dynein axonemal heavy chain 8 Homo sapiens 197-203 6174024-3 1981 At higher concentrations of sodium and potassium ions, ATPase of normal and nitrofurantoin resistant Vibrio el tor responded quite differently. Potassium 39-48 dynein axonemal heavy chain 8 Homo sapiens 55-61 6253559-1 1980 The ultrastructural cytochemical localization of a potassium-dependent oubain-sensitive nitrophenyl phosphatase (transport ATPase) activity in human blood platelets is described. Potassium 51-60 dynein axonemal heavy chain 8 Homo sapiens 123-129 142633-3 1977 Previous reports of activation of the NaK ATPase at low potassium and high sodium are probably not due to phenytoin but to a potassium contamination in the phenytoin solution. Potassium 125-134 dynein axonemal heavy chain 8 Homo sapiens 42-48 19873649-1 1969 The interactions of potassium ions and ATP on transport ATPase activity are discussed, and the interpretation of these interactions is shown to be often ambiguous. Potassium 20-29 dynein axonemal heavy chain 8 Homo sapiens 56-62 4256160-0 1971 Electron-microscopic histochemical examination of potassium-sodium-dependent myocardial ATP-ase activity. Potassium 50-59 dynein axonemal heavy chain 8 Homo sapiens 88-95 19873649-6 1969 When starved sodium-poor red cells are poisoned with iodoacetamide, loaded with phosphate, and incubated in high-sodium potassium-free media, the ouabain-sensitive efflux of potassium appears to be accompanied by the reversal of the entire ATPase system. Potassium 174-183 dynein axonemal heavy chain 8 Homo sapiens 240-246 19873649-8 1969 If potassium is present in the external medium, no ouabain-sensitive synthesis of ATP occurs and the ouabain-sensitive efflux of potassium presumably involves the reversal of only the last part of the ATPase system. Potassium 3-12 dynein axonemal heavy chain 8 Homo sapiens 201-207 19873649-8 1969 If potassium is present in the external medium, no ouabain-sensitive synthesis of ATP occurs and the ouabain-sensitive efflux of potassium presumably involves the reversal of only the last part of the ATPase system. Potassium 129-138 dynein axonemal heavy chain 8 Homo sapiens 201-207 4231042-0 1968 Sodium-potssum tmulated ATPase activity of mammalian hemolysates: clinical observations and ominance of ATPase deficiency in the potassium polymorphism of sheep. Potassium 129-138 dynein axonemal heavy chain 8 Homo sapiens 104-110 4232206-0 1968 The relation between ouabain-sensitive potassium efflux and the hypothetical dephosphorylation step in the "transport ATPase" system. Potassium 39-48 dynein axonemal heavy chain 8 Homo sapiens 118-125 4296201-2 1967 Relationship of ATP-ase to the active transport of sodium and potassium ions. Potassium 62-71 dynein axonemal heavy chain 8 Homo sapiens 16-23 4228075-4 1967 As it is known that the ouabain-sensitive ATPase in fragmented ghosts requires both sodium and potassium ions, these results show that the ATPase is activated by potassium externally and by sodium internally, and suggest that the ions activating the ATPase are the ions that are transported.2. Potassium 95-104 dynein axonemal heavy chain 8 Homo sapiens 42-48 4228075-4 1967 As it is known that the ouabain-sensitive ATPase in fragmented ghosts requires both sodium and potassium ions, these results show that the ATPase is activated by potassium externally and by sodium internally, and suggest that the ions activating the ATPase are the ions that are transported.2. Potassium 95-104 dynein axonemal heavy chain 8 Homo sapiens 139-145 4228075-4 1967 As it is known that the ouabain-sensitive ATPase in fragmented ghosts requires both sodium and potassium ions, these results show that the ATPase is activated by potassium externally and by sodium internally, and suggest that the ions activating the ATPase are the ions that are transported.2. Potassium 95-104 dynein axonemal heavy chain 8 Homo sapiens 139-145 4228075-4 1967 As it is known that the ouabain-sensitive ATPase in fragmented ghosts requires both sodium and potassium ions, these results show that the ATPase is activated by potassium externally and by sodium internally, and suggest that the ions activating the ATPase are the ions that are transported.2. Potassium 162-171 dynein axonemal heavy chain 8 Homo sapiens 42-48 4228075-4 1967 As it is known that the ouabain-sensitive ATPase in fragmented ghosts requires both sodium and potassium ions, these results show that the ATPase is activated by potassium externally and by sodium internally, and suggest that the ions activating the ATPase are the ions that are transported.2. Potassium 162-171 dynein axonemal heavy chain 8 Homo sapiens 139-145 4228075-4 1967 As it is known that the ouabain-sensitive ATPase in fragmented ghosts requires both sodium and potassium ions, these results show that the ATPase is activated by potassium externally and by sodium internally, and suggest that the ions activating the ATPase are the ions that are transported.2. Potassium 162-171 dynein axonemal heavy chain 8 Homo sapiens 139-145 4225829-0 1966 Studies on the activity of sodium and potassium activated ATP-ase in normal and leukemic granulocytes. Potassium 38-47 dynein axonemal heavy chain 8 Homo sapiens 58-65 24233809-8 2013 Magnesium deficiency by interfering with ATPase functions causes increased intracellular calcium and sodium and decreases intracellular potassium concentration. Potassium 136-145 dynein axonemal heavy chain 8 Homo sapiens 41-47 14163532-0 1964 SPECIES DIFFERENCES IN THE EFFECT OF SODIUM AND POTASSIUM IONS ON THE ATPASE OF ERYTHROCYTE MEMBRANES. Potassium 48-57 dynein axonemal heavy chain 8 Homo sapiens 70-76 14006658-0 1961 The sensitivity of a kidney ATPase to ouabain and to sodium and potassium. Potassium 64-73 dynein axonemal heavy chain 8 Homo sapiens 28-34 33437698-3 2020 TPP is due to increased sodium/potassium ATPase activity during thyrotoxic states, which is due to mutations encoding potassium channels. Potassium 31-40 dynein axonemal heavy chain 8 Homo sapiens 41-47 31984791-2 2020 NHERF1 is involved in the regulation of the sodium hydrogen exchanger 3 (NHE3), the sodium dependent phosphate transporter 2a (Npt2a), and the sodium potassium ATPase through its ability to scaffold these transporters to the plasma membrane, allowing regulation of these protein complexes with their associated hormone receptors. Potassium 143-159 dynein axonemal heavy chain 8 Homo sapiens 160-166 22668657-7 2012 Magnesium deficiency by interfering with ATPase functions causes increased intracellular calcium and sodium and decreases intracellular potassium concentration. Potassium 136-145 dynein axonemal heavy chain 8 Homo sapiens 41-47 19666591-0 2009 Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain. Potassium 32-41 dynein axonemal heavy chain 8 Homo sapiens 55-61 12680712-1 2003 Previously, we reported that the ATPase activity of GroEL that requires potassium and magnesium was highly temperature dependent in the 25-60 degrees C range. Potassium 72-81 dynein axonemal heavy chain 8 Homo sapiens 33-39 16636594-10 2006 High K+-ATPase activity in the erythrocytes correlated with low plasma potassium. Potassium 71-80 dynein axonemal heavy chain 8 Homo sapiens 8-14 16636594-11 2006 The K+-ATPase activity correlated positively with the amount of potassium administered to dehydrated infants. Potassium 64-73 dynein axonemal heavy chain 8 Homo sapiens 7-13 16636594-12 2006 CONCLUSION: These findings suggest that the erythrocytes Na+,K+-ATPase and K+-ATPase both protect against plasma potassium abnormalities in dehydrated infants. Potassium 113-122 dynein axonemal heavy chain 8 Homo sapiens 64-70 16636594-12 2006 CONCLUSION: These findings suggest that the erythrocytes Na+,K+-ATPase and K+-ATPase both protect against plasma potassium abnormalities in dehydrated infants. Potassium 113-122 dynein axonemal heavy chain 8 Homo sapiens 78-84 15198370-1 2004 Na+,K(+)-ATPase is an ubiquitous membrane enzyme that allows the extrusion of three sodium ions from the cell and two potassium ions from the extracellular fluid. Potassium 118-127 dynein axonemal heavy chain 8 Homo sapiens 9-15 12134182-0 2002 Endogenous sodium-potassium ATPase inhibition related biochemical cascade in trisomy 21 and Huntington"s disease: neural regulation of genomic function. Potassium 18-27 dynein axonemal heavy chain 8 Homo sapiens 28-34