dodecylphosphocholine has been researched along with 1-palmitoyl-2-oleoylphosphatidylcholine in 3 studies
| Studies (dodecylphosphocholine) | Trials (dodecylphosphocholine) | Recent Studies (post-2010) (dodecylphosphocholine) | Studies (1-palmitoyl-2-oleoylphosphatidylcholine) | Trials (1-palmitoyl-2-oleoylphosphatidylcholine) | Recent Studies (post-2010) (1-palmitoyl-2-oleoylphosphatidylcholine) |
|---|---|---|---|---|---|
| 362 | 0 | 129 | 1,978 | 3 | 932 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (33.33) | 18.2507 |
| 2000's | 1 (33.33) | 29.6817 |
| 2010's | 1 (33.33) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cafiso, DS; Gorzelle, BM; Lonzer, WL; Nagy, JK; Oxenoid, K; Sanders, CR | 1 |
| Aisenbrey, C; Almeida, FC; Bechinger, B; Bemquerer, MP; de Moraes, CM; Piló-Veloso, D; Resende, JM; Valente, AP; Verly, RM | 1 |
| Khadria, AS; Senes, A | 1 |
3 other study(ies) available for dodecylphosphocholine and 1-palmitoyl-2-oleoylphosphatidylcholine
| Article | Year |
|---|---|
Reconstitutive refolding of diacylglycerol kinase, an integral membrane protein.
Topics: Amino Acid Sequence; Amino Acid Substitution; Cross-Linking Reagents; Detergents; Diacylglycerol Kinase; Escherichia coli; Lipid Bilayers; Macromolecular Substances; Membrane Proteins; Micelles; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphatidylcholines; Phosphorylcholine; Protein Folding; Urea | 1999 |
Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy.
Topics: Animals; Antimicrobial Cationic Peptides; Anura; Circular Dichroism; Lipid Bilayers; Micelles; Models, Molecular; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Phosphatidylcholines; Phosphorus Isotopes; Phosphorylcholine; Protein Conformation; Sodium Dodecyl Sulfate; Trifluoroethanol; Unilamellar Liposomes; Water | 2009 |
The transmembrane domains of the bacterial cell division proteins FtsB and FtsL form a stable high-order oligomer.
Topics: Cell Cycle Proteins; Cell Division; Cell Membrane; Detergents; Escherichia coli; Escherichia coli Proteins; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Kinetics; Lipid Bilayers; Membrane Proteins; Models, Biological; Peptide Fragments; Phosphatidylcholines; Phosphorylcholine; Protein Interaction Domains and Motifs; Protein Multimerization; Protein Stability; Protein Structure, Secondary | 2013 |