tryptophan has been researched along with exenatide in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Andersen, NH; Fesinmeyer, RM; Neidigh, JW; Prickett, KS | 1 |
| Andersen, NH; Neidigh, JW | 1 |
| Lau, J; Madsen, K; Rudolph, R; Runge, S; Thøgersen, H | 1 |
3 other study(ies) available for tryptophan and exenatide
| Article | Year |
|---|---|
Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states.
Topics: Amino Acid Sequence; Binding Sites; Circular Dichroism; Exenatide; Glucagon; Glucagon-Like Peptide 1; Glycine; Humans; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutation; Peptide Fragments; Peptides; Phosphatidylcholines; Protein Precursors; Protein Structure, Secondary; Sequence Homology, Amino Acid; Stereoisomerism; Trifluoroethanol; Tryptophan; Venoms | 2001 |
Peptide conformational changes induced by tryptophan-phosphocholine interactions in a micelle.
Topics: Amino Acid Sequence; Circular Dichroism; Exenatide; In Vitro Techniques; Micelles; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Peptides; Phosphorylcholine; Protein Conformation; Solutions; Tryptophan; Venoms | 2002 |
Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain.
Topics: Amino Acid Sequence; Cell Membrane; Crystallography, X-Ray; Exenatide; Glucagon-Like Peptide-1 Receptor; Humans; Insulin-Secreting Cells; Ligands; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Peptides; Protein Binding; Protein Conformation; Protein Structure, Secondary; Receptors, Glucagon; Sequence Homology, Amino Acid; Tryptophan; Venoms | 2008 |