proline has been researched along with cytidine monophosphate in 7 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 4 (57.14) | 18.7374 |
| 1990's | 2 (28.57) | 18.2507 |
| 2000's | 1 (14.29) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Baldwin, RL; Cook, KH; Schmid, FX | 1 |
| Blaschek, H; Schmid, FX | 1 |
| Brandts, JF; Lin, LN | 1 |
| Jaenicke, R; Krebs, H; Schmid, FX | 1 |
| Dodge, RW; Laity, JH; Rothwarf, DM; Scheraga, HA; Shimotakahara, S | 1 |
| Houry, WA; Scheraga, HA | 1 |
| Lorenz, T; Reinstein, J | 1 |
7 other study(ies) available for proline and cytidine monophosphate
| Article | Year |
|---|---|
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 |
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 |
Involvement of prolines-114 and -117 in the slow refolding phase of ribonuclease A as determined by isomer-specific proteolysis.
Topics: Amino Acid Sequence; Aminopeptidases; Chymotrypsin; Cytidine Monophosphate; Endopeptidases; Hydrolysis; Isomerism; Kinetics; Mercaptoethanol; Pepsin A; Peptide Hydrolases; Proline; Prolyl Oligopeptidases; Protein Conformation; Ribonuclease, Pancreatic; Serine Endopeptidases; Spectrophotometry | 1984 |
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 |
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 |
Nature of the unfolded state of ribonuclease A: effect of cis-trans X-Pro peptide bond isomerization.
Topics: Animals; Cattle; Cytidine Monophosphate; Enzyme Inhibitors; Guanidine; Guanidines; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Chemical; Models, Molecular; Peptides; Proline; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Ribonuclease, Pancreatic; Spectrophotometry | 1996 |
The influence of proline isomerization and off-pathway intermediates on the folding mechanism of eukaryotic UMP/CMP Kinase.
Topics: Animals; Circular Dichroism; Cytidine Monophosphate; Dictyostelium; Fluorescence Resonance Energy Transfer; Isomerism; Kinetics; Nucleoside-Phosphate Kinase; Proline; Protein Folding; Protein Structure, Secondary; Protozoan Proteins; Thermodynamics; Uridine Monophosphate | 2008 |