glycerate 1,3-biphosphate has been researched along with 2,3-diphosphoglycerate in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 4 (100.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Ouellet, M; Shoubridge, EA | 1 |
| Fujii, H | 1 |
| Dainyak, MB; Fokina, KV; Muronetz, VI; Nagradova, NK | 1 |
| Fothergill-Gilmore, LA; Phillips, SE; Rigden, DJ; Walter, RA | 1 |
1 review(s) available for glycerate 1,3-biphosphate and 2,3-diphosphoglycerate
| Article | Year |
|---|---|
[Red cell glycolytic intermediates].
Topics: 2,3-Diphosphoglycerate; Blood Glucose; Dihydroxyacetone Phosphate; Diphosphoglyceric Acids; Fructosediphosphates; Fructosephosphates; Glucose-6-Phosphate; Glucosephosphates; Glyceraldehyde 3-Phosphate; Glyceric Acids; Humans; Lactates; Lactic Acid; Phosphoenolpyruvate; Pyruvates; Pyruvic Acid | 1995 |
3 other study(ies) available for glycerate 1,3-biphosphate and 2,3-diphosphoglycerate
| Article | Year |
|---|---|
Phosphocreatine-dependent protein phosphorylation in rat skeletal muscle.
Topics: 2,3-Diphosphoglycerate; Adenosine Triphosphate; Animals; Binding Sites; Bisphosphoglycerate Mutase; Creatine Kinase; Cytosol; Diphosphoglyceric Acids; Histidine; Kinetics; Male; Molecular Weight; Muscle Proteins; Muscles; Phosphocreatine; Phosphoglycerate Kinase; Phosphoglycerate Mutase; Phosphorus Radioisotopes; Phosphorylation; Rats; Rats, Inbred Strains | 1992 |
A study on the complexes between human erythrocyte enzymes participating in the conversions of 1,3-diphosphoglycerate.
Topics: 2,3-Diphosphoglycerate; Antibodies, Monoclonal; Bisphosphoglycerate Mutase; Chromatography, Affinity; Dimerization; Diphosphoglyceric Acids; Erythrocytes; Glucose; Glyceraldehyde-3-Phosphate Dehydrogenases; Glyceric Acids; Glycolysis; Humans; Hydrogen-Ion Concentration; Multienzyme Complexes; Phosphoglycerate Kinase; Protein Binding | 1997 |
Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism.
Topics: 2,3-Diphosphoglycerate; Binding Sites; Catalysis; Crystallization; Diphosphoglyceric Acids; Hydrogen Bonding; Ions; Kinetics; Ligands; Models, Molecular; Mutation; Phosphates; Phosphoglycerate Mutase; Phosphorylation; Protein Binding; Protein Conformation; Saccharomyces cerevisiae; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Structure-Activity Relationship; Sulfates | 1999 |