histidine has been researched along with glycerophosphoinositol 4,5-bisphosphate in 6 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (33.33) | 18.2507 |
| 2000's | 3 (50.00) | 29.6817 |
| 2010's | 1 (16.67) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Ellis, MV; Katan, M; U, S | 1 |
| Carpenter, G; DeStefano, K; Horstman, DA | 1 |
| Bruzik, KS; Hondal, RJ; Kubiak, RJ; Mihai, C; Tsai, MD; Yue, X | 1 |
| Enkvetchakul, D; Jeliazkova, I; Nichols, CG | 1 |
| Cho, W; Hom, RA; Kutateladze, TG; Regner, M; Stahelin, RV; Subach, OM; Verkhusha, VV; Vora, M | 1 |
| Amzel, LM; Cole, RN; Gabelli, SB; Maheshwari, S; Miller, MS; O'Meally, R | 1 |
6 other study(ies) available for histidine and glycerophosphoinositol 4,5-bisphosphate
| Article | Year |
|---|---|
Mutations within a highly conserved sequence present in the X region of phosphoinositide-specific phospholipase C-delta 1.
Topics: Amino Acid Sequence; Animal Population Groups; Animals; Base Sequence; Calcium; Circular Dichroism; Diethyl Pyrocarbonate; Genes; Histidine; Isoenzymes; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphatidylinositol 4,5-Diphosphate; Phosphatidylinositol Diacylglycerol-Lyase; Phosphatidylinositol Phosphates; Phosphoinositide Phospholipase C; Phosphoric Diester Hydrolases; Protein Conformation; Recombinant Fusion Proteins; Sequence Alignment; Sequence Homology, Amino Acid | 1995 |
Enhanced phospholipase C-gamma1 activity produced by association of independently expressed X and Y domain polypeptides.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cell Line; Conserved Sequence; Histidine; Isoenzymes; Kinetics; Macromolecular Substances; Mammals; Phosphatidylinositol 4,5-Diphosphate; Phospholipase C gamma; Rats; Recombinant Fusion Proteins; Sequence Tagged Sites; Spodoptera; Transfection; Type C Phospholipases | 1996 |
Involvement of the Arg-Asp-His catalytic triad in enzymatic cleavage of the phosphodiester bond.
Topics: Amino Acid Substitution; Arginine; Asparagine; Bacillus cereus; Binding Sites; Catalysis; Catalytic Domain; Glycine max; Histidine; Hydrolysis; Inositol Phosphates; Organophosphates; Phosphatidylinositol Diacylglycerol-Lyase; Phosphoinositide Phospholipase C; Ribonuclease, Pancreatic; Structure-Activity Relationship; Substrate Specificity; Sulfur; Thionucleotides; Type C Phospholipases | 2001 |
Direct modulation of Kir channel gating by membrane phosphatidylinositol 4,5-bisphosphate.
Topics: Amino Acid Sequence; Bacterial Proteins; Cell Membrane; Cytoplasm; Cytoskeleton; Dose-Response Relationship, Drug; Escherichia coli Proteins; Histidine; Ions; Kinetics; Liposomes; Micelles; Molecular Sequence Data; Phosphates; Phosphatidylinositol 4,5-Diphosphate; Phosphatidylinositol Phosphates; Potassium Channels; Potassium Channels, Inwardly Rectifying; Potassium Channels, Voltage-Gated; Protein Structure, Tertiary; Rubidium Radioisotopes | 2005 |
pH-dependent binding of the Epsin ENTH domain and the AP180 ANTH domain to PI(4,5)P2-containing bilayers.
Topics: Adaptor Proteins, Vesicular Transport; Amino Acid Sequence; Animals; Binding Sites; Chlorocebus aethiops; COS Cells; Green Fluorescent Proteins; Histidine; Humans; Hydrogen-Ion Concentration; Lipid Bilayers; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Monomeric Clathrin Assembly Proteins; Phosphatidylinositol 4,5-Diphosphate; Protein Structure, Tertiary; Rats; Sequence Alignment | 2007 |
Kinetic and structural analyses reveal residues in phosphoinositide 3-kinase α that are critical for catalysis and substrate recognition.
Topics: Adenosine Triphosphate; Amino Acid Substitution; Binding Sites; Biocatalysis; Catalytic Domain; Class I Phosphatidylinositol 3-Kinases; Class Ia Phosphatidylinositol 3-Kinase; Histidine; Humans; Kinetics; Lysine; Models, Molecular; Molecular Conformation; Mutagenesis, Site-Directed; Phosphatidylinositol 3-Kinases; Phosphatidylinositol 4,5-Diphosphate; Phosphorylation; Point Mutation; Protein Conformation; Protein Multimerization; Protein Processing, Post-Translational | 2017 |