selenium has been researched along with pteridines in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (50.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Eady, RR; Gangeswaran, R; Lowe, DJ | 1 |
| Dismukes, GC; Gladyshev, VN; Khangulov, SV; Stadtman, TC | 1 |
| Dobbek, H; Gremer, L; Huber, R; Kiefersauer, R; Meyer, O | 1 |
| Mihara, H | 1 |
1 review(s) available for selenium and pteridines
| Article | Year |
|---|---|
[Discovery and molecular function analysis of sulfur- and selenium-eliminating enzymes crucial for biosynthesis of iron-sulfur clusters and selenoproteins].
Topics: Animals; Coenzymes; Cystathionine gamma-Lyase; Humans; Iron-Sulfur Proteins; Lyases; Metalloproteins; Molybdenum Cofactors; Pteridines; RNA, Transfer; Selenium; Selenoproteins; Sulfides; Sulfur | 2011 |
3 other study(ies) available for selenium and pteridines
| Article | Year |
|---|---|
Purification and characterization of the assimilatory nitrate reductase of Azotobacter vinelandii.
Topics: Azotobacter vinelandii; Chromatography, Gel; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Coenzymes; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Iron; Kinetics; Metalloproteins; Molecular Weight; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrate Reductases; Pteridines; Selenium; Spectrophotometry; Sulfides | 1993 |
Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer.
Topics: Binding Sites; Carbon Dioxide; Catalysis; Coenzymes; Electron Spin Resonance Spectroscopy; Escherichia coli; Formate Dehydrogenases; Formates; Hydrogenase; Iron; Metalloproteins; Molybdenum Cofactors; Multienzyme Complexes; Mutation; Oxidation-Reduction; Oxygen; Photochemistry; Protons; Pteridines; Selenium; Sulfur; Thermodynamics | 1998 |
Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.
Topics: Aldehyde Oxidoreductases; Alphaproteobacteria; Bacterial Proteins; Binding Sites; Catalysis; Coenzymes; Copper; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Metalloproteins; Models, Molecular; Molybdenum; Molybdenum Cofactors; Multienzyme Complexes; Nitriles; Oxidation-Reduction; Potassium Cyanide; Pteridines; Selenium; Structure-Activity Relationship; Sulfur | 2002 |