glutamic acid has been researched along with 1-palmitoyl-2-oleoylphosphatidylcholine in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 3 (75.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Chisholm, JW; Gebre, AK; Parks, JS; Wang, J; Zhao, Y | 1 |
| Musgaard, M; Schiøtt, B; Thøgersen, L | 1 |
| Althoff, T; Banerjee, S; Gouaux, E; Hibbs, RE | 1 |
| Gnanasambandam, R; Nishizawa, K; Nishizawa, M; Sachs, F; Suchyna, TM; Sukharev, SI | 1 |
4 other study(ies) available for glutamic acid and 1-palmitoyl-2-oleoylphosphatidylcholine
| Article | Year |
|---|---|
Negative charge at amino acid 149 is the molecular determinant for substrate specificity of lecithin: cholesterol acyltransferase for phosphatidylcholine containing 20-carbon sn-2 fatty acyl chains.
Topics: Alanine; Amino Acid Substitution; Animals; Chlorocebus aethiops; CHO Cells; COS Cells; Cricetinae; Fatty Acids; Glutamic Acid; Humans; Hydrophobic and Hydrophilic Interactions; Kinetics; Phosphatidylcholine-Sterol O-Acyltransferase; Phosphatidylcholines; Rats; Static Electricity; Substrate Specificity | 2003 |
Protonation states of important acidic residues in the central Ca²⁺ ion binding sites of the Ca²⁺-ATPase: a molecular modeling study.
Topics: Amino Acids, Acidic; Animals; Aspartic Acid; Binding Sites; Calcium; Chemical Phenomena; Databases, Protein; Enzyme Stability; Glutamic Acid; Kinetics; Lipid Bilayers; Membrane Fluidity; Models, Molecular; Molecular Dynamics Simulation; Phosphatidylcholines; Potassium; Protein Conformation; Protons; Rabbits; Sarcoplasmic Reticulum Calcium-Transporting ATPases | 2011 |
X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors.
Topics: Allosteric Regulation; Animals; Apoproteins; Binding Sites; Binding, Competitive; Caenorhabditis elegans; Cell Membrane; Chloride Channels; Crystallography, X-Ray; Cysteine Loop Ligand-Gated Ion Channel Receptors; Drug Partial Agonism; Glutamic Acid; Ion Channel Gating; Ivermectin; Ligands; Models, Molecular; Movement; Phosphatidylcholines; Protein Binding; Protein Multimerization; Protein Structure, Tertiary; Structure-Activity Relationship | 2014 |
Effects of Lys to Glu mutations in GsMTx4 on membrane binding, peptide orientation, and self-association propensity, as analyzed by molecular dynamics simulations.
Topics: Cell Membrane; Glutamic Acid; Intercellular Signaling Peptides and Proteins; Kinetics; Lipid Bilayers; Lysine; Membrane Lipids; Molecular Dynamics Simulation; Mutation, Missense; Peptides; Phosphatidylcholines; Protein Binding; Spider Venoms; Thermodynamics | 2015 |