gallamine triethiodide has been researched along with obidoxime chloride 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 |
|---|---|
| Ellis, J; Seidenberg, M | 1 |
| Antony, J; Grossmüller, M; Holzgrabe, U; Mohr, K; Tränkle, C | 1 |
| Pisterzi, LF; Redka, DS; Wells, JW | 1 |
| Agnusdei, M; Belinskaya, T; Borriello, M; Brindisi, M; Butini, S; Campiani, G; Catalanotti, B; Fattorusso, C; Fiorini, I; Gemma, S; Nacci, V; Novellino, E; Panico, A; Persico, M; Ros, S; Saxena, A | 1 |
4 other study(ies) available for gallamine triethiodide and obidoxime chloride
| Article | Year |
|---|---|
Two allosteric modulators interact at a common site on cardiac muscarinic receptors.
Topics: Allosteric Regulation; Animals; Binding Sites; Gallamine Triethiodide; Gallic Acid; In Vitro Techniques; Myocardium; Obidoxime Chloride; Rats; Rats, Sprague-Dawley; Receptors, Muscarinic; Tacrine | 1992 |
Allosteric site in M2 acetylcholine receptors: evidence for a major conformational change upon binding of an orthosteric agonist instead of an antagonist.
Topics: Allosteric Regulation; Allosteric Site; Animals; Binding, Competitive; Gallamine Triethiodide; In Vitro Techniques; Isoindoles; Muscarinic Agonists; Muscarinic Antagonists; Myocardium; N-Methylscopolamine; Obidoxime Chloride; Oxotremorine; Phthalimides; Protein Conformation; Pyridinium Compounds; Receptor, Muscarinic M2; Swine | 2006 |
Binding of orthosteric ligands to the allosteric site of the M(2) muscarinic cholinergic receptor.
Topics: Allosteric Regulation; Allosteric Site; Animals; Binding, Competitive; Cell Line; Gallamine Triethiodide; Humans; Insecta; Kinetics; Ligands; N-Methylscopolamine; Obidoxime Chloride; Protein Structure, Quaternary; Receptor, Muscarinic M2; Solubility | 2008 |
Exploiting protein fluctuations at the active-site gorge of human cholinesterases: further optimization of the design strategy to develop extremely potent inhibitors.
Topics: Acetylcholinesterase; Binding Sites; Butyrylcholinesterase; Cholinesterase Inhibitors; Computational Biology; Crystallography, X-Ray; Drug Design; Humans; Models, Molecular; Protein Conformation; Structure-Activity Relationship; Tacrine | 2008 |