rubidium has been researched along with spermine in 6 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (33.33) | 18.7374 |
| 1990's | 1 (16.67) | 18.2507 |
| 2000's | 3 (50.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Eterović, VA; Ferchmin, PA; Hann, RM; Szczawinska, K | 1 |
| Harmony, JA; Himes, RH; Shaffer, PJ | 1 |
| Ballas, SK; Clark, MR; Mohandas, N; Shohet, SB | 1 |
| Forment, J; Mulet, JM; Serrano, R; Vicente, O | 1 |
| Fujiwara, Y; Kubo, Y | 1 |
| Boyett, MR; Claydon, TW; Dibb, KM; Makary, SM | 1 |
6 other study(ies) available for rubidium and spermine
| Article | Year |
|---|---|
Electric organ polyamines and their effects on the acetylcholine receptor.
Topics: Animals; Binding, Competitive; Bungarotoxins; Carbachol; Cell Membrane; Electric Organ; Polyamines; Receptors, Cholinergic; Rubidium; Spermine; Torpedo | 1992 |
Cation- and anion-dependent reassociation of formyltetrahydrofolate synthetase subunits.
Topics: Adenosine Triphosphate; Ammonium Chloride; Anions; Cations, Monovalent; Cesium; Clostridium; Drug Stability; Enzyme Activation; Formates; Hydrogen-Ion Concentration; Kinetics; Ligases; Lithium; Macromolecular Substances; Magnesium; Osmolar Concentration; Potassium; Rubidium; Sodium; Species Specificity; Spectrophotometry, Ultraviolet; Spermine; Tellurium; Temperature; Tetrahydrofolates | 1974 |
Polyamines do not inhibit erythrocyte ATPase activities.
Topics: Adenosine Triphosphatases; Biological Transport, Active; Cell Membrane Permeability; Erythrocyte Membrane; Erythrocytes; Humans; Polyamines; Potassium; Putrescine; Radioisotopes; Rubidium; Sodium; Sodium-Potassium-Exchanging ATPase; Spermine | 1983 |
The yeast SR protein kinase Sky1p modulates salt tolerance, membrane potential and the Trk1,2 potassium transporter.
Topics: ATP-Binding Cassette Transporters; Cation Transport Proteins; Lithium; Manganese; Membrane Potentials; Mutation; Protein Serine-Threonine Kinases; Protein-Arginine N-Methyltransferases; Repressor Proteins; Rubidium; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Signal Transduction; Sodium; Spermine | 2002 |
Ser165 in the second transmembrane region of the Kir2.1 channel determines its susceptibility to blockade by intracellular Mg2+.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cations; Ion Channel Gating; Magnesium; Membrane Potentials; Mutagenesis, Site-Directed; Oocytes; Patch-Clamp Techniques; Point Mutation; Potassium Channels, Inwardly Rectifying; Protein Conformation; Protein Structure, Tertiary; Rubidium; Serine; Spermine; Structure-Activity Relationship; Xenopus | 2002 |
Base of pore loop is important for rectification, activation, permeation, and block of Kir3.1/Kir3.4.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cesium; G Protein-Coupled Inwardly-Rectifying Potassium Channels; In Vitro Techniques; Ion Channel Gating; Models, Molecular; Molecular Sequence Data; Mutation; Oocytes; Patch-Clamp Techniques; Protein Conformation; Rubidium; Spermine; Xenopus | 2006 |