ouabain has been researched along with isothiuronium in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (25.00) | 18.2507 |
2000's | 3 (75.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Argüello, JM; Blostein, R; Karlish, SJ; Lingrel, JB; Wilczynska, A | 1 |
Apell, HJ; Karlish, SJ; Schneeberger, A; Shainskaya, A | 1 |
Beaugé, L; Garrahan, PJ; González-Lebrero, RM; Karlish, SJ; Rossi, RC; Shimon, MB; Yudowski, GA | 1 |
Bar Shimon, M; Beaugé, LA; Garrahan, PJ; González-Lebrero, RM; Karlish, SJ; Rossi, RC; Tal, DM; Yudowski, GA | 1 |
4 other study(ies) available for ouabain and isothiuronium
Article | Year |
---|---|
Evidence that Ser775 in the alpha subunit of the Na,K-ATPase is a residue in the cation binding pocket.
Topics: Adenosine Triphosphate; Alanine; Animals; Binding Sites; Cations, Monovalent; Enzyme Inhibitors; HeLa Cells; Humans; Isothiuronium; Kinetics; Macromolecular Substances; Mutagenesis, Site-Directed; Ouabain; Point Mutation; Potassium; Recombinant Proteins; Rubidium; Serine; Sheep; Sodium-Potassium-Exchanging ATPase; Time Factors; Transfection | 1997 |
Entrance port for Na(+) and K(+) ions on Na(+),K(+)-ATPase in the cytoplasmic loop between trans-membrane segments M6 and M7 of the alpha subunit. Proximity Of the cytoplasmic segment of the beta subunit.
Topics: Amino Acid Sequence; Animals; Calcium; Chymotrypsin; Cytoplasm; Dose-Response Relationship, Drug; Enzyme Inhibitors; Isothiuronium; Kidney; Kinetics; Models, Molecular; Molecular Sequence Data; Ouabain; Potassium; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Rubidium; Sodium; Sodium-Potassium-Exchanging ATPase; Swine; Temperature; Time Factors | 2000 |
Extracellularly applied Br-TITU inhibits the Na+/K+ pump by interacting with tryptophan at the entrance to the cation sites.
Topics: Binding Sites; Cations; Enzyme Inhibitors; Erythrocytes; Humans; Isothiuronium; Kinetics; Ouabain; Sodium; Sodium-Potassium-Exchanging ATPase; Tryptophan | 2003 |
Evidence for tryptophan residues in the cation transport path of the Na(+),K(+)-ATPase.
Topics: Animals; Binding Sites; Biological Transport, Active; Cations; Cell Membrane; Enzyme Inhibitors; Erythrocytes; Humans; Isothiuronium; Models, Molecular; Ouabain; Phosphorylation; Rubidium; Sodium; Sodium Radioisotopes; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Swine; Tryptophan | 2003 |