proline has been researched along with phosphoglycolate in 3 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (33.33) | 18.2507 |
2000's | 2 (66.67) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Delboni, LF; Hol, WG; Mainfroid, V; Mande, SC; Martial, JA; Rentier-Delrue, F; Turley, S; Vellieux, FM | 1 |
Cabrera, N; de Gómez-Puyou, MT; Gómez-Puyou, A; Hernández-Alcantara, G; López-Velazquez, G; Pérez-Montfort, R; Reyes-Vivas, H | 1 |
Kursula, I; Wierenga, RK | 1 |
3 other study(ies) available for proline and phosphoglycolate
Article | Year |
---|---|
Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions.
Topics: Amino Acid Sequence; Binding Sites; Binding, Competitive; Chemical Phenomena; Chemistry, Physical; Crystallization; Crystallography, X-Ray; Enzyme Inhibitors; Enzyme Stability; Geobacillus stearothermophilus; Glycolates; Hot Temperature; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Molecular Structure; Proline; Recombinant Proteins; Structure-Activity Relationship; Triose-Phosphate Isomerase | 1995 |
Factors that control the reactivity of the interface cysteine of triosephosphate isomerase from Trypanosoma brucei and Trypanosoma cruzi.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Cysteine; Dimerization; Enzyme Activation; Enzyme Inhibitors; Glutamic Acid; Glutamine; Glycolates; Hydrogen-Ion Concentration; Leishmania mexicana; Methyl Methanesulfonate; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Fragments; Proline; Protein Structure, Tertiary; Triose-Phosphate Isomerase; Trypanosoma brucei brucei; Trypanosoma cruzi | 2001 |
Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution.
Topics: Animals; Anisotropy; Binding Sites; Crystallography, X-Ray; Dimerization; Glutamic Acid; Glycolates; Histidine; Hydrogen Bonding; Leishmania mexicana; Models, Chemical; Models, Molecular; Proline; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protons; Triose-Phosphate Isomerase | 2003 |