aspartic acid has been researched along with leukotriene c4 in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cole, SP; Deeley, RG; Gao, M; Payen, LF; Westlake, CJ | 1 |
| Cole, SP; Deeley, RG; Gu, HM; Haimeur, A; Situ, D; Zhang, DW | 1 |
| Cole, SP; Conseil, G; Deeley, RG; Haimeur, A; Situ, D; Sparks, KE; Zhang, D | 1 |
3 other study(ies) available for aspartic acid and leukotriene c4
| Article | Year |
|---|---|
Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1).
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Motifs; Amino Acid Sequence; Animals; Aspartic Acid; Biological Transport; Carboxylic Acids; Catalysis; Cell Line; Cell Membrane; DNA, Complementary; Drug Resistance, Multiple; Electrophoresis, Polyacrylamide Gel; Glutamic Acid; Humans; Hydrolysis; Insecta; Leukotriene C4; Light; Molecular Sequence Data; Multidrug Resistance-Associated Proteins; Mutation; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Time Factors; Vanadates | 2003 |
Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): identification of an aspartate residue critical for conversion from a high to low affinity substrate binding state.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Motifs; Amino Acid Sequence; Amino Acids; Animals; Anions; Asparagine; Aspartic Acid; Binding Sites; Biological Transport; Cell Line; Cytoplasm; Drug Resistance; Estradiol; Humans; Hydrolysis; Kinetics; Leukotriene C4; Lysine; Mice; Models, Molecular; Molecular Sequence Data; Multidrug Resistance-Associated Proteins; Mutagenesis, Site-Directed; Mutation; Nucleic Acid Synthesis Inhibitors; Protein Binding; Protein Structure, Tertiary; Rats; Serine; Time Factors; Transfection | 2003 |
Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression and catalytic activity of the transporter.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Anions; Arginine; Aspartic Acid; Biological Transport; Catalysis; Cell Line, Transformed; Cytoplasm; DNA Mutational Analysis; DNA, Complementary; Glutamic Acid; Humans; Ions; Leukotriene C4; Models, Molecular; Molecular Sequence Data; Multidrug Resistance-Associated Proteins; Mutagenesis, Site-Directed; Mutation; Organic Anion Transporters; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Time Factors; Transfection; Vanadates | 2004 |