maltoheptaose has been researched along with aspartic acid in 2 studies
| Studies (maltoheptaose) | Trials (maltoheptaose) | Recent Studies (post-2010) (maltoheptaose) | Studies (aspartic acid) | Trials (aspartic acid) | Recent Studies (post-2010) (aspartic acid) |
|---|---|---|---|---|---|
| 114 | 0 | 39 | 23,005 | 417 | 4,018 |
| Protein | Taxonomy | maltoheptaose (IC50) | aspartic acid (IC50) |
|---|---|---|---|
| Glutamate receptor ionotropic, NMDA 1 | Rattus norvegicus (Norway rat) | 1.638 | |
| Excitatory amino acid transporter 1 | Homo sapiens (human) | 90.1265 | |
| Excitatory amino acid transporter 2 | Homo sapiens (human) | 11 | |
| Glutamate receptor ionotropic, NMDA 2A | Rattus norvegicus (Norway rat) | 1.638 | |
| Glutamate receptor ionotropic, NMDA 2B | Rattus norvegicus (Norway rat) | 1.638 | |
| Glutamate receptor ionotropic, NMDA 2C | Rattus norvegicus (Norway rat) | 1.638 | |
| Glutamate receptor ionotropic, NMDA 2D | Rattus norvegicus (Norway rat) | 1.638 | |
| Glutamate receptor ionotropic, NMDA 3B | Rattus norvegicus (Norway rat) | 1.638 | |
| Glutamate receptor ionotropic, NMDA 3A | Rattus norvegicus (Norway rat) | 1.638 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (50.00) | 18.2507 |
| 2000's | 1 (50.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Ford, C; Reilly, PJ; Sierks, MR; Svensson, B | 1 |
| Christensen, T; Frandsen, TP; Kaarsholm, NC; Sigurskjold, BW; Svensson, B | 1 |
2 other study(ies) available for maltoheptaose and aspartic acid
| Article | Year |
|---|---|
Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori.
Topics: Amino Acid Sequence; Aspartic Acid; Aspergillus; Base Sequence; Binding Sites; Catalysis; DNA Restriction Enzymes; Glucan 1,4-alpha-Glucosidase; Glucans; Glutamates; Glutamic Acid; Hydrogen-Ion Concentration; Isomaltose; Kinetics; Maltose; Molecular Sequence Data; Mutation; Sequence Homology, Nucleic Acid; Structure-Activity Relationship; Thermodynamics | 1990 |
Physicochemical characterisation of the two active site mutants Trp(52)-->Phe and Asp(55)-->Val of glucoamylase from Aspergillus niger.
Topics: Amino Acid Substitution; Aspartic Acid; Aspergillus niger; Binding Sites; Calorimetry; Glucan 1,4-alpha-Glucosidase; Glucans; Guanidine; Kinetics; Maltose; Mutation; Phenylalanine; Protein Conformation; Protein Denaturation; Sequence Deletion; Substrate Specificity; Tryptophan; Valine | 2002 |