aspartic acid has been researched along with web 2086 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 |
---|---|
Le Gouill, C; Parent, JL; Rola-Pleszczynski, M; Stanková, J | 1 |
Escher, E; Gouill, CL; Parent, JL; Rola-Pleszczynski, M; Staková, J | 1 |
Asano, K; Fukunaga, K; Ishii, S; Shimizu, T; Shiomi, T; Yamaguchi, K; Yokomizo, T | 1 |
3 other study(ies) available for aspartic acid and web 2086
Article | Year |
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Mutation of an aspartate at position 63 in the human platelet-activating factor receptor augments binding affinity but abolishes G-protein-coupling and inositol phosphate production.
Topics: Amino Acid Sequence; Animals; Aspartic Acid; Azepines; Binding Sites; Binding, Competitive; Cell Line; Chlorocebus aethiops; CHO Cells; Conserved Sequence; Cricetinae; GTP-Binding Proteins; Inositol Phosphates; Kinetics; Mutagenesis, Site-Directed; Platelet Activating Factor; Platelet Aggregation Inhibitors; Platelet Membrane Glycoproteins; Point Mutation; Protein Conformation; Receptors, Cell Surface; Receptors, G-Protein-Coupled; Recombinant Proteins; Transfection; Triazoles | 1996 |
Identification of transmembrane domain residues determinant in the structure-function relationship of the human platelet-activating factor receptor by site-directed mutagenesis.
Topics: Amino Acid Sequence; Animals; Asparagine; Aspartic Acid; Azepines; CHO Cells; Cricetinae; Dose-Response Relationship, Drug; Humans; Inositol Phosphates; Molecular Sequence Data; Mutagenesis, Site-Directed; Phenylalanine; Platelet Activating Factor; Platelet Aggregation Inhibitors; Platelet Membrane Glycoproteins; Protein Conformation; Proto-Oncogene Proteins c-myc; Receptors, Cell Surface; Receptors, G-Protein-Coupled; Structure-Activity Relationship; Transfection; Triazoles | 1996 |
Single nucleotide polymorphism of human platelet-activating factor receptor impairs G-protein activation.
Topics: Adenylate Cyclase Toxin; Adenylyl Cyclase Inhibitors; Alanine; Alleles; Amino Acid Sequence; Animals; Aspartic Acid; Azepines; Cell Line; Chemotaxis; CHO Cells; Colforsin; Cricetinae; Cyclic AMP; Dose-Response Relationship, Drug; GTP-Binding Proteins; Humans; Inositol Phosphates; Kinetics; Ligands; Molecular Sequence Data; Mutation; Phenotype; Platelet Aggregation Inhibitors; Platelet Membrane Glycoproteins; Polymorphism, Genetic; Polymorphism, Single Nucleotide; Protein Binding; Radioligand Assay; Receptors, Cell Surface; Receptors, G-Protein-Coupled; Signal Transduction; Transfection; Triazoles; Virulence Factors, Bordetella | 2001 |