tryptophan has been researched along with phosphoserine in 7 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (42.86) | 29.6817 |
| 2010's | 4 (57.14) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bowman, ME; Hunter, T; Lu, KP; Noel, JP; Verdecia, MA | 1 |
| Greenleaf, AL; Morris, DP; Myers, JK; Oas, TG | 1 |
| Riemen, AJ; Waters, ML | 1 |
| Daubner, SC; Fitzpatrick, PF; Lasagna, M; Reinhart, GD; Wang, S | 1 |
| Chu, IK; Hao, Q; Quan, Q; Siu, CK; Song, T | 1 |
| Benstein, RM; Flügge, UI; Frerigmann, H; Gierth, M; Gigolashvili, T; Krueger, S; Ludewig, K; Wittek, S; Wulfert, S | 1 |
| Delangle, P; Laporte, FA; Lebrun, C; Oros, S; Sisommay, N; Starck, M | 1 |
7 other study(ies) available for tryptophan and phosphoserine
| Article | Year |
|---|---|
Structural basis for phosphoserine-proline recognition by group IV WW domains.
Topics: Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Fluorescence Polarization; Humans; Models, Molecular; Molecular Sequence Data; NIMA-Interacting Peptidylprolyl Isomerase; Peptide Fragments; Peptidylprolyl Isomerase; Phosphopeptides; Phosphoserine; Proline; Protein Binding; Protein Structure, Tertiary; Recombinant Fusion Proteins; RNA Polymerase II; Sequence Alignment; Structure-Activity Relationship; Substrate Specificity; Thermodynamics; Tryptophan | 2000 |
Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1.
Topics: Circular Dichroism; Enzyme Stability; Ligands; NIMA-Interacting Peptidylprolyl Isomerase; Peptide Fragments; Peptidylprolyl Isomerase; Phosphates; Phosphorylation; Phosphoserine; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; RNA Polymerase II; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sodium Chloride; Spectrometry, Fluorescence; Temperature; Titrimetry; Tryptophan | 2001 |
Controlling peptide folding with repulsive interactions between phosphorylated amino acids and tryptophan.
Topics: Circular Dichroism; Glutamic Acid; Hydrogen-Ion Concentration; Nuclear Magnetic Resonance, Biomolecular; Peptides; Phosphorylation; Phosphoserine; Protein Folding; Protein Processing, Post-Translational; Serine; Threonine; Tryptophan; Tyrosine | 2009 |
Fluorescence spectroscopy as a probe of the effect of phosphorylation at serine 40 of tyrosine hydroxylase on the conformation of its regulatory domain.
Topics: Acrylamide; Fluorescence Polarization; Phosphorylation; Phosphoserine; Protein Structure, Tertiary; Spectrometry, Fluorescence; Tryptophan; Tyrosine 3-Monooxygenase | 2011 |
Mechanistic investigation of phosphate ester bond cleavages of glycylphosphoserinyltryptophan radical cations under low-energy collision-induced dissociation.
Topics: Cations; Free Radicals; Glycine; Mass Spectrometry; Phosphopeptides; Phosphorylation; Phosphoserine; Thermodynamics; Tryptophan | 2013 |
Arabidopsis phosphoglycerate dehydrogenase1 of the phosphoserine pathway is essential for development and required for ammonium assimilation and tryptophan biosynthesis.
Topics: Ammonium Compounds; Arabidopsis; Arabidopsis Proteins; Biosynthetic Pathways; Feedback, Physiological; Gene Expression Regulation, Plant; Isoenzymes; Phosphoglycerate Dehydrogenase; Phosphoserine; Plastids; Tryptophan | 2013 |
Preorganized Peptide Scaffolds as Mimics of Phosphorylated Proteins Binding Sites with a High Affinity for Uranyl.
Topics: Amino Acid Sequence; Binding Sites; Calcium; Chelating Agents; Circular Dichroism; Glutamic Acid; Imino Acids; Molecular Mimicry; Osteopontin; Peptides, Cyclic; Phosphopeptides; Phosphoserine; Protein Structure, Secondary; Spectrometry, Mass, Electrospray Ionization; Tryptophan; Uranyl Nitrate | 2015 |