3-hydroxyaspartic acid has been researched along with 1-carboxyglutamic acid in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (50.00) | 18.7374 |
| 1990's | 2 (50.00) | 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 |
|---|---|
| Long, GL; Nelson, RM | 1 |
| Kisiel, W; Morita, T | 1 |
| Fernlund, P; Stenflo, J | 1 |
| Girolami, A; James, HL; Kim, DJ | 1 |
4 other study(ies) available for 3-hydroxyaspartic acid and 1-carboxyglutamic acid
| Article | Year |
|---|---|
Binding of protein S to C4b-binding protein. Mutagenesis of protein S.
Topics: 1-Carboxyglutamic Acid; Amino Acid Sequence; Animals; Asparagine; Aspartic Acid; Base Sequence; Blood Proteins; Carrier Proteins; Cattle; Cells, Cultured; Complement Inactivator Proteins; Glycoproteins; Humans; Kidney; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein S; Recombinant Proteins; Solutions; Thrombin; Transfection | 1992 |
Calcium binding to a human factor IXa derivative lacking gamma-carboxyglutamic acid: evidence for two high-affinity sites that do not involve beta-hydroxyaspartic acid.
Topics: 1-Carboxyglutamic Acid; Amino Acids; Aspartic Acid; Binding Sites; Calcium; Chromatography, Ion Exchange; Factor IX; Factor IXa; Glutamates; Humans; Time Factors | 1985 |
Beta-hydroxyaspartic acid in vitamin K-dependent plasma proteins from scorbutic and warfarin-treated guinea pigs.
Topics: 1-Carboxyglutamic Acid; Animals; Ascorbic Acid; Ascorbic Acid Deficiency; Aspartic Acid; Blood Coagulation; Blood Proteins; Guinea Pigs; Hydroxylation; Protein Processing, Post-Translational; Vitamin K; Warfarin | 1984 |
Characterization of recombinant human coagulation factor XFriuli.
Topics: 1-Carboxyglutamic Acid; Aspartic Acid; Base Sequence; Binding Sites; Cell Line; DNA, Complementary; Enzyme Activation; Factor X; Hemorrhagic Disorders; Humans; Hydrogen Bonding; Kidney; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Proline; Protein Processing, Post-Translational; Protein Structure, Secondary; Recombinant Proteins; Serine; Transfection | 1996 |