aspartic acid has been researched along with Deficiency of GP 2b 3a Complex in 2 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (50.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (50.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Einav, Y; Hauschner, H; Koren, A; Mansour, W; Rosenberg, N; Seligsohn, U | 1 |
| Bennett, JS; Coller, BS; Fortina, P; Newman, PJ; Parrella, T; Poncz, M; Rifat, S; Shattil, SJ | 1 |
2 other study(ies) available for aspartic acid and Deficiency of GP 2b 3a Complex
| Article | Year |
|---|---|
An αIIb mutation in patients with Glanzmann thrombasthenia located in the N-terminus of blade 1 of the β-propeller (Asn2Asp) disrupts a calcium binding site in blade 6.
Topics: Adolescent; Amino Acid Sequence; Animals; Arabs; Asparagine; Aspartic Acid; Binding Sites; Blood Platelets; Calcium; Cell Line; Child; Child, Preschool; Cricetinae; DNA Mutational Analysis; Female; Genetic Predisposition to Disease; Glutamine; Hemostasis; Heredity; Humans; Hydrogen Bonding; Integrin alpha2; Integrin beta3; Israel; Leucine; Male; Models, Molecular; Molecular Sequence Data; Mutation; Pedigree; Phenotype; Protein Conformation; Protein Structure, Tertiary; Protein Transport; Thrombasthenia; Transfection | 2011 |
Glanzmann thrombasthenia secondary to a Gly273-->Asp mutation adjacent to the first calcium-binding domain of platelet glycoprotein IIb.
Topics: Adenosine Diphosphate; Amino Acid Sequence; Aspartic Acid; Base Sequence; Binding Sites; Calcium; DNA; DNA Primers; Epinephrine; Female; Glycine; Humans; Infant, Newborn; Male; Molecular Sequence Data; Mutagenesis, Site-Directed; Pedigree; Platelet Adhesiveness; Platelet Aggregation; Platelet Membrane Glycoproteins; Point Mutation; Polymerase Chain Reaction; Reading Frames; Recombinant Proteins; Thrombasthenia | 1994 |