proline and cytidine monophosphate

proline has been researched along with cytidine monophosphate in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19904 (57.14)18.7374
1990's2 (28.57)18.2507
2000's1 (14.29)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Baldwin, RL; Cook, KH; Schmid, FX1
Blaschek, H; Schmid, FX1
Brandts, JF; Lin, LN1
Jaenicke, R; Krebs, H; Schmid, FX1
Dodge, RW; Laity, JH; Rothwarf, DM; Scheraga, HA; Shimotakahara, S1
Houry, WA; Scheraga, HA1
Lorenz, T; Reinstein, J1

Other Studies

7 other study(ies) available for proline and cytidine monophosphate

ArticleYear
Role of proline isomerization in folding of ribonuclease A at low temperatures.
    Proceedings of the National Academy of Sciences of the United States of America, 1979, Volume: 76, Issue:12

    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.
    European journal of biochemistry, 1981, Volume: 114, Issue:1

    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.
    Biochemistry, 1984, Nov-20, Volume: 23, Issue:24

    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.
    Journal of molecular biology, 1983, Sep-15, Volume: 169, Issue:2

    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.
    Journal of protein chemistry, 1994, Volume: 13, Issue:4

    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.
    Biochemistry, 1996, Sep-10, Volume: 35, Issue:36

    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.
    Journal of molecular biology, 2008, Aug-29, Volume: 381, Issue:2

    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