Compounds > aspartic acid
Page last updated: 2024-08-17

aspartic acid and web 2086

aspartic acid has been researched along with web 2086 in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (66.67)18.2507
2000's1 (33.33)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Le Gouill, C; Parent, JL; Rola-Pleszczynski, M; Stanková, J1
Escher, E; Gouill, CL; Parent, JL; Rola-Pleszczynski, M; Staková, J1
Asano, K; Fukunaga, K; Ishii, S; Shimizu, T; Shiomi, T; Yamaguchi, K; Yokomizo, T1

Other Studies

3 other study(ies) available for aspartic acid and web 2086

ArticleYear
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.
    Biochemical and biophysical research communications, 1996, Feb-27, Volume: 219, Issue:3

    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.
    The Journal of biological chemistry, 1996, Sep-20, Volume: 271, Issue:38

    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.
    The Journal of biological chemistry, 2001, Nov-16, Volume: 276, Issue:46

    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