| P2093 | author name string | Tetsuya Yamamoto | |
| | Kazuyasu Sakaguchi | |
| | Kazuya Taniguchi | |
| | Shunji Kaya | |
| | Toshiaki Imagawa | |
| P2860 | cites work | Replacement of several single amino acid side chains exposed to the inside of the ATP-binding pocket induces different extents of affinity change in the high and low affinity ATP-binding sites of rat Na/K-ATPase | Q38364012 |
| | Structure-function relationships of cation translocation by Ca(2+)- and Na+, K(+)-ATPases studied by site-directed mutagenesis. | Q40600097 |
| | Residues of the fourth transmembrane segments of the Na,K-ATPase and the gastric H,K-ATPase contribute to cation selectivity | Q40906072 |
| | Asp804 and Asp808 in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues | Q41150449 |
| | Substitutions of glutamate 781 in the Na,K-ATPase alpha subunit demonstrate reduced cation selectivity and an increased affinity for ATP. | Q41229967 |
| | Functional consequences of mutation Asn326-->Leu in the 4th transmembrane segment of the alpha-subunit of the rat kidney Na+, K(+)-ATPase. | Q41349835 |
| | Glutamic acid 327 in the sheep alpha 1 isoform of Na+,K(+)-ATPase is a pivotal residue for cation-induced conformational changes | Q41918971 |
| | Mutation of aspartate 804 of Na(+),K(+)-ATPase modifies the cation binding pocket and thereby generates a high Na(+)-ATPase activity | Q42055979 |
| | Critical effects on catalytic function produced by amino acid substitutions at Asp804 and Asp808 of the alpha1 isoform of Na,K-ATPase | Q42811431 |
| | Alanine scanning mutagenesis of oxygen-containing amino acids in the transmembrane region of the Na,K-ATPase | Q42813630 |
| | The Amino Acid Sequence 442GDASE446 in Na/K-ATPase Is an Important Motif in Forming the High and Low Affinity ATP Binding Pockets | Q44605200 |
| | Structure-function relationships of E1-E2 transitions and cation binding in Na,K-pump protein | Q47729683 |
| | Mutation to the glutamate in the fourth membrane segment of Na+,K+-ATPase and Ca2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms | Q47732405 |
| | cDNA cloning and sequence determination of pig gastric (H+ + K+)-ATPase | Q48310634 |
| | Significance of the glutamic acid residues Glu334, Glu959, and Glu960 of the alpha subunits of Torpedo Na+, K+ pumps for transport activity and ouabain binding | Q48946231 |
| | Substitution of glutamic 779 with alanine in the Na,K-ATPase alpha subunit removes voltage dependence of ion transport | Q50193017 |
| | The M4M5 cytoplasmic loop of the Na,K-ATPase, overexpressed in Escherichia coli, binds nucleoside triphosphates with the same selectivity as the intact native protein. | Q54136915 |
| | Substitutions of serine 775 in the alpha subunit of the Na,K-ATPase selectively disrupt K+ high affinity activation without affecting Na+ interaction. | Q54162226 |
| | Mutant Glu781-->Ala of the rat kidney Na+,K(+)-ATPase displays low cation affinity and catalyzes ATP hydrolysis at a high rate in the absence of potassium ions. | Q54182264 |
| | Site-directed mutagenesis of the Na,K-ATPase: consequences of substitutions of negatively-charged amino acids localized in the transmembrane domains. | Q54223687 |
| | Site-directed mutagenesis of a predicted cation binding site of Na, K-ATPase. | Q54249506 |
| | DNA sequencing with chain-terminating inhibitors | Q22066207 |
| | Homology modeling of the cation binding sites of Na+K+-ATPase | Q24541473 |
| | A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding | Q25938984 |
| | Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution | Q27625023 |
| | ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase | Q27641133 |
| | Structural organization, ion transport, and energy transduction of P-type ATPases | Q28279229 |
| | Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences | Q28285061 |
| | The oligomeric nature of Na/K-transport ATPase | Q32066131 |
| | Structure and mechanism of Na,K-ATPase: functional sites and their interactions | Q34170045 |
| | Structure-function relationships of Na(+), K(+), ATP, or Mg(2+) binding and energy transduction in Na,K-ATPase. | Q34180462 |
| | Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum | Q34271890 |
| | Evolution of substrate specificities in the P-type ATPase superfamily. | Q34451276 |
| | Biochemistry of Na,K-ATPase | Q34667442 |
| | Molecular cloning of three distinct forms of the Na+,K+-ATPase alpha-subunit from rat brain | Q36426324 |
| | Occluded cations in active transport | Q36587813 |
| | Glutamic acid 327 in the sheep alpha 1 isoform of Na+,K(+)-ATPase stabilizes a K(+)-induced conformational change | Q36715565 |
| | A Glu329-->Gln variant of the alpha-subunit of the rat kidney Na+,K(+)-ATPase can sustain active transport of Na+ and K+ and Na+,K(+)-activated ATP hydrolysis with normal turnover number | Q36720984 |
| | Glutamate 329 located in the fourth transmembrane segment of the alpha-subunit of the rat kidney Na+,K+-ATPase is not an essential residue for active transport of sodium and potassium ions. | Q36755831 |
| | Chemical modification of Glu-953 of the alpha chain of Na+,K(+)-ATPase associated with inactivation of cation occlusion | Q37127272 |
| | Does binding of ouabain to human alpha1-subunit of Na+, K+-ATPase affect the ATPase activity of adjacent rat alpha1-subunit? | Q38336738 |
| P433 | issue | 19 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | transmembrane protein | Q424204 |
| | transmembrane transport | Q14820680 |
| P304 | page(s) | 18736-18744 | |
| P577 | publication date | 2005-03-11 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Thr-774 (transmembrane segment M5), Val-920 (M8), and Glu-954 (M9) are involved in Na+ transport, and Gln-923 (M8) is essential for Na,K-ATPase activity | |
| P478 | volume | 280 | |