tryptophan has been researched along with inositol 1,4,5-trisphosphate 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 | 1 (25.00) | 29.6817 |
| 2010's | 2 (50.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Sato, T; Uchida, Y | 1 |
| Joseph, SK; Zhang, X | 1 |
| Chan, J; Ikura, M; Michikawa, T; Mikoshiba, K; Yamazaki, H | 1 |
| Chan, J; Ikura, M; Ishiyama, N; Mal, TK; Michikawa, T; Mikoshiba, K; Seo, MD; Yamazaki, H | 1 |
4 other study(ies) available for tryptophan and inositol 1,4,5-trisphosphate
| Article | Year |
|---|---|
Changes in outward K+ currents in response to two types of sweeteners in sweet taste transduction of gerbil taste cells.
Topics: Animals; Calcium; Cyclic AMP; Gerbillinae; Inositol 1,4,5-Trisphosphate; Ion Transport; Ionomycin; Ionophores; Membrane Potentials; Patch-Clamp Techniques; Plant Proteins; Potassium Channels; Saccharin; Signal Transduction; Sweetening Agents; Taste; Taste Buds; Tryptophan | 1997 |
Effect of mutation of a calmodulin binding site on Ca2+ regulation of inositol trisphosphate receptors.
Topics: Alanine; Amino Acid Substitution; Animals; Binding Sites; Calcium; Calcium Channels; Calmodulin; COS Cells; Humans; Inositol 1,4,5-Trisphosphate; Inositol 1,4,5-Trisphosphate Receptors; Microsomes; Mutagenesis, Site-Directed; Protein Isoforms; Receptors, Cytoplasmic and Nuclear; Transfection; Tryptophan | 2001 |
Tyr-167/Trp-168 in type 1/3 inositol 1,4,5-trisphosphate receptor mediates functional coupling between ligand binding and channel opening.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; Blotting, Western; Calcium; Cell Line, Tumor; Inositol 1,4,5-Trisphosphate; Inositol 1,4,5-Trisphosphate Receptors; Ion Channel Gating; Ligands; Mice; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Protein Binding; Protein Isoforms; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Trypsin; Tryptophan; Tyrosine | 2010 |
Structural studies of inositol 1,4,5-trisphosphate receptor: coupling ligand binding to channel gating.
Topics: Amino Acid Sequence; Animals; Binding Sites; Crystallography, X-Ray; Inositol 1,4,5-Trisphosphate; Inositol 1,4,5-Trisphosphate Receptors; Ion Channel Gating; Ligands; Magnetic Resonance Spectroscopy; Mice; Models, Molecular; Molecular Sequence Data; Mutation; Protein Isoforms; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Tryptophan; Tyrosine | 2010 |