tyrosine has been researched along with cytidine monophosphate in 10 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 6 (60.00) | 18.7374 |
| 1990's | 3 (30.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (10.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Das, MK; Vithayathil, PJ | 1 |
| Beintema, JJ; Bolscher, BG; Kaptein, R; Lenstra, JA | 1 |
| Baldwin, RL; Cook, KH; Schmid, FX | 1 |
| Marshall, SH; Muñoz, G | 1 |
| Cozzone, AJ; Manai, M | 1 |
| Blaschek, H; Schmid, FX | 1 |
| Jaenicke, R; Krebs, H; Schmid, FX | 1 |
| Baldwin, RL; Udgaonkar, JB | 1 |
| Dodge, RW; Laity, JH; Rothwarf, DM; Scheraga, HA; Shimotakahara, S | 1 |
| Aoki, K; Ishida, N; Kawakita, M; Sakaguchi, M; Sanai, Y; Sugahara, Y; Takeshima-Futagami, T; Uehara, E | 1 |
10 other study(ies) available for tyrosine and cytidine monophosphate
| Article | Year |
|---|---|
Influence of phosphate ligands in abolishing the conformational difference between ribonuclease A and its acid-denatured derivative.
Topics: Amides; Catalysis; Cytidine Monophosphate; Hydrogen-Ion Concentration; Ligands; Phosphates; Protein Conformation; Protein Denaturation; Ribonucleases; Tyrosine | 1978 |
The aromatic residues of bovine pancreatic ribonuclease studied by 1H nuclear magnetic resonance.
Topics: Animals; Binding Sites; Cattle; Cytidine Monophosphate; Histidine; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Pancreas; Phenylalanine; Protein Conformation; Ribonucleases; Tyrosine; Uridine Monophosphate | 1979 |
Role of proline isomerization in folding of ribonuclease A at low temperatures.
Topics: Ammonium Sulfate; Cytidine Monophosphate; Guanidines; Isomerism; Kinetics; Proline; Protein Conformation; Ribonucleases; Temperature; Tyrosine | 1979 |
An alternative method for a fast separation of phosphotyrosine.
Topics: Adenosine Triphosphate; Animals; Chromatography, Thin Layer; Cytidine Monophosphate; Humans; Liver; Lymphocytes; Mice; Phosphorus Radioisotopes; Phosphoserine; Phosphothreonine; Phosphotyrosine; Tyrosine; Uridine Monophosphate | 1990 |
Two-dimensional separation of phosphoamino acids from nucleoside monophosphates.
Topics: Adenosine Monophosphate; Chromatography, Thin Layer; Cytidine Monophosphate; Electrophoresis; Escherichia coli; Guanosine Monophosphate; Nucleotides; Phosphoserine; Phosphothreonine; Phosphotyrosine; Serine; Threonine; Thymidine Monophosphate; Tyrosine; Uracil Nucleotides; Uridine Monophosphate | 1982 |
A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A.
Topics: Cytidine Monophosphate; Endonucleases; Isomerism; Kinetics; Proline; Protein Conformation; Ribonuclease, Pancreatic; Ribonucleases; Spectrum Analysis; Tyrosine | 1981 |
Folding of homologous proteins. The refolding of different ribonucleases is independent of sequence variations, proline content and glycosylation.
Topics: Amino Acid Sequence; Animals; Carbohydrates; Cattle; Cytidine Monophosphate; Deer; Kinetics; Proline; Protein Conformation; Ribonuclease, Pancreatic; Ribonucleases; Sheep; Spectrophotometry; Temperature; Tyrosine | 1983 |
Nature of the early folding intermediate of ribonuclease A.
Topics: Animals; Binding Sites; Cattle; Cytidine Monophosphate; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Models, Structural; Protein Folding; Protein Structure, Secondary; Ribonuclease, Pancreatic; Tyrosine | 1995 |
Folding pathway of guanidine-denatured disulfide-intact wild-type and mutant bovine pancreatic ribonuclease A.
Topics: Alanine; Animals; Binding Sites; Cattle; Cytidine Monophosphate; Disulfides; Guanidine; Guanidines; Kinetics; Mutagenesis, Site-Directed; Point Mutation; Proline; Protein Denaturation; Protein Folding; Recombinant Proteins; Ribonuclease, Pancreatic; Tyrosine | 1994 |
Amino acid residues important for CMP-sialic acid recognition by the CMP-sialic acid transporter: analysis of the substrate specificity of UDP-galactose/CMP-sialic acid transporter chimeras.
Topics: Amino Acid Motifs; Animals; Biological Transport; CHO Cells; Cricetinae; Cricetulus; Cytidine Monophosphate; Galactose; Monosaccharide Transport Proteins; Mutation, Missense; N-Acetylneuraminic Acid; Nucleotide Transport Proteins; Protein Structure, Tertiary; Recombinant Fusion Proteins; Substrate Specificity; Tyrosine; Uridine Diphosphate | 2012 |