willardiine has been researched along with 2,3-diphosphoglycerate in 1 studies
*2,3-Diphosphoglycerate: A highly anionic organic phosphate which is present in human red blood cells at about the same molar ratio as hemoglobin. It binds to deoxyhemoglobin but not the oxygenated form, therefore diminishing the oxygen affinity of hemoglobin. This is essential in enabling hemoglobin to unload oxygen in tissue capillaries. It is also an intermediate in the conversion of 3-phosphoglycerate to 2-phosphoglycerate by phosphoglycerate mutase (EC 5.4.2.1). (From Stryer Biochemistry, 4th ed, p160; Enzyme Nomenclature, 1992, p508) [MeSH]
*2,3-Diphosphoglycerate: A highly anionic organic phosphate which is present in human red blood cells at about the same molar ratio as hemoglobin. It binds to deoxyhemoglobin but not the oxygenated form, therefore diminishing the oxygen affinity of hemoglobin. This is essential in enabling hemoglobin to unload oxygen in tissue capillaries. It is also an intermediate in the conversion of 3-phosphoglycerate to 2-phosphoglycerate by phosphoglycerate mutase (EC 5.4.2.1). (From Stryer Biochemistry, 4th ed, p160; Enzyme Nomenclature, 1992, p508) [MeSH]
| Studies (willardiine) | Trials (willardiine) | Recent Studies (post-2010) (willardiine) | Studies (2,3-diphosphoglycerate) | Trials (2,3-diphosphoglycerate) | Recent Studies (post-2010) (2,3-diphosphoglycerate) |
|---|---|---|---|---|---|
| 43 | 0 | 10 | 1,418 | 39 | 117 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (100.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Tobi, D | 1 |
1 other study(ies) available for willardiine and 2,3-diphosphoglycerate
| Article | Year |
|---|---|
Dynamical differences of hemoglobin and the ionotropic glutamate receptor in different states revealed by a new dynamics alignment method.
Topics: 2,3-Diphosphoglycerate; Alanine; Algorithms; Allosteric Site; Animals; Binding Sites; Excitatory Amino Acid Agonists; Halogenation; Hemoglobins; Humans; Kainic Acid; Ligands; Molecular Dynamics Simulation; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Rats; Receptors, AMPA; Sequence Alignment; Sequence Homology, Amino Acid; Thermodynamics; Uracil | 2017 |