2,5-di-tert-butylhydroquinone has been researched along with gadolinium in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (75.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Barrett, PQ; Brophy, C; Isales, CM; Rosales, OR; Sumpio, BE | 1 |
| Ikeda, M; Mills, I; Sumpio, BE; Takei, T | 1 |
| Ho, CM; Jan, CR; Tseng, CJ; Wu, SN | 1 |
| Auld, A; Barritt, GJ; Brereton, HM; Chen, J; Gregory, RB; Wang, YJ | 1 |
4 other study(ies) available for 2,5-di-tert-butylhydroquinone and gadolinium
| Article | Year |
|---|---|
Exposure of endothelial cells to cyclic strain induces elevations of cytosolic Ca2+ concentration through mobilization of intracellular and extracellular pools.
Topics: Animals; Aorta, Thoracic; Calcium; Cattle; Cell Cycle; Cells, Cultured; Culture Media; Endothelium, Vascular; Extracellular Space; Gadolinium; Hydroquinones; Inositol 1,4,5-Trisphosphate; Intracellular Fluid; Kinetics; Stress, Mechanical | 1997 |
Calcium-independent activation of extracellular signal-regulated kinases 1 and 2 by cyclic strain.
Topics: Animals; Calcium; Calcium Channel Blockers; Calcium-Calmodulin-Dependent Protein Kinases; Cattle; Cells, Cultured; Chelating Agents; Egtazic Acid; Endothelium, Vascular; Enzyme Activation; Extracellular Space; Gadolinium; Hydroquinones; Intracellular Fluid; Mitogen-Activated Protein Kinase 1; Mitogen-Activated Protein Kinase 3; Mitogen-Activated Protein Kinases; Phosphorylation; Stress, Mechanical | 1998 |
Mechanism of rise and decay of 2,5-di-tert-butylhydroquinone-induced Ca2+ signals in Madin Darby canine kidney cells.
Topics: Animals; Calcium; Carbonyl Cyanide m-Chlorophenyl Hydrazone; Cell Line; Dogs; Dose-Response Relationship, Drug; Enzyme Inhibitors; Gadolinium; Hydrogen-Ion Concentration; Hydroquinones; Ion Transport; Kidney; Lanthanum; Uncoupling Agents | 1999 |
Store-operated Ca(2+) inflow in Reuber hepatoma cells is inhibited by voltage-operated Ca(2+) channel antagonists and, in contrast to freshly isolated hepatocytes, does not require a pertussis toxin-sensitive trimeric GTP-binding protein.
Topics: Animals; Brefeldin A; Calcium; Calcium Channel Blockers; Calcium Channels; Calcium-Transporting ATPases; Calmodulin; Chelating Agents; Dose-Response Relationship, Drug; Egtazic Acid; Enzyme Inhibitors; Gadolinium; Heterotrimeric GTP-Binding Proteins; Hydroquinones; Imidazoles; Indoles; Liver; Pertussis Toxin; Sulfonamides; Thapsigargin; Tumor Cells, Cultured; Virulence Factors, Bordetella | 2000 |