aspartic acid has been researched along with Amaurotic Familial Idiocy in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (66.67) | 18.2507 |
| 2000's | 1 (33.33) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cherney, MM; James, MN; Lemieux, MJ; Mahuran, DJ; Mark, BL; Withers, SG | 1 |
| Hou, Y; Mahuran, DJ; Tse, R; Vavougios, G | 1 |
| Brown, C; Hechtman, P; Kaplan, F; Mahuran, D; Trop, I | 1 |
3 other study(ies) available for aspartic acid and Amaurotic Familial Idiocy
| Article | Year |
|---|---|
Crystallographic structure of human beta-hexosaminidase A: interpretation of Tay-Sachs mutations and loss of GM2 ganglioside hydrolysis.
Topics: Acetylglucosamine; Amino Acid Substitution; Arginine; Aspartic Acid; beta-N-Acetylhexosaminidases; Binding Sites; Crystallography, X-Ray; Dimerization; Gangliosidoses, GM2; Glycine; Glycosylation; Hexosaminidase A; Humans; Hydrolysis; Models, Molecular; Mutation; Protein Conformation; Protein Subunits; Tay-Sachs Disease; Thiazoles | 2006 |
Identification of an active acidic residue in the catalytic site of beta-hexosaminidase.
Topics: Amino Acid Sequence; Animals; Aspartic Acid; Bacteria; Base Sequence; beta-N-Acetylhexosaminidases; Binding Sites; Cats; Cell Line; Chlorocebus aethiops; DNA, Complementary; Exons; Female; G(M2) Ganglioside; Hexosaminidase A; Hexosaminidase B; Humans; Isoenzymes; Kidney; Macromolecular Substances; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Placenta; Point Mutation; Pregnancy; Recombinant Proteins; Sequence Homology, Amino Acid; Substrate Specificity; Swine; Tay-Sachs Disease; Transfection | 1996 |
A glycine250--> aspartate substitution in the alpha-subunit of hexosaminidase A causes juvenile-onset Tay-Sachs disease in a Lebanese-Canadian family.
Topics: Amino Acid Sequence; Animals; Aspartic Acid; Base Sequence; beta-N-Acetylhexosaminidases; Canada; Cell Line; Chlorocebus aethiops; Consanguinity; Female; Glycine; Hexosaminidase A; Humans; Kidney; Lebanon; Macromolecular Substances; Male; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oligodeoxyribonucleotides; Pedigree; Polymerase Chain Reaction; Protein Structure, Secondary; Recombinant Proteins; Tay-Sachs Disease; Transfection | 1992 |