dodecylphosphocholine has been researched along with dimyristoylphosphatidylcholine in 12 studies
| Studies (dodecylphosphocholine) | Trials (dodecylphosphocholine) | Recent Studies (post-2010) (dodecylphosphocholine) | Studies (dimyristoylphosphatidylcholine) | Trials (dimyristoylphosphatidylcholine) | Recent Studies (post-2010) (dimyristoylphosphatidylcholine) |
|---|---|---|---|---|---|
| 362 | 0 | 129 | 3,474 | 1 | 855 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (16.67) | 18.2507 |
| 2000's | 4 (33.33) | 29.6817 |
| 2010's | 6 (50.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Buchko, GW; Cushley, RJ; Pierens, GK; Wang, G | 1 |
| Carpenter, KA; Schiller, PW; Wilkes, BC | 1 |
| Kang, S; Kim, SD; Kim, Y; Ryu, PD; Yu, K | 1 |
| Kamath, S; Wong, TC | 1 |
| Andersson, A; Bárány-Wallje, E; Gräslund, A; Mäler, L | 1 |
| Alves, ID; Bouaziz, S; Feller, SE; Marquant, R; Salgado, GF; Vogel, A | 1 |
| Cocco, MJ; Schulz, J; Vasudevan, SV; Zhou, C | 1 |
| Grage, SL; Nolandt, OV; Ulrich, AS; Walther, TH | 1 |
| Allsopp, M; Hénin, J; Klauda, JB; Lee, S; Lim, JB; Tran, A | 1 |
| Ding, Y; Fujimoto, LM; Marassi, FM; Plano, GV; Yao, Y | 1 |
| Bayoumi, M; Carulla, N; Gairí, M; Maglia, G; Ninot-Pedrosa, M; Serra-Batiste, M | 1 |
| Bessonov, K; Harauz, G; Vassall, KA | 1 |
12 other study(ies) available for dodecylphosphocholine and dimyristoylphosphatidylcholine
| Article | Year |
|---|---|
Conformational studies of an amphipathic peptide corresponding to human apolipoprotein A-II residues 18-30 with a C-terminal lipid binding motif EWLNS.
Topics: Amino Acid Sequence; Apolipoprotein A-II; Binding Sites; Computer Simulation; Detergents; Dimyristoylphosphatidylcholine; Humans; Lipid Metabolism; Lipids; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Peptide Fragments; Phosphorylcholine; Protein Conformation; Protons; Sodium Dodecyl Sulfate; Solutions; Spectrum Analysis | 1996 |
The octapeptide angiotensin II adopts a well-defined structure in a phospholipid environment.
Topics: Angiotensin II; Cell Membrane; Dimyristoylphosphatidylcholine; Lipid Bilayers; Magnetic Resonance Spectroscopy; Micelles; Models, Molecular; Phospholipids; Phosphorylcholine; Protein Conformation; Water | 1998 |
Interactions between mastoparan B and the membrane studied by 1H NMR spectroscopy.
Topics: Alanine; Cell Membrane; Circular Dichroism; Dimyristoylphosphatidylcholine; Intercellular Signaling Peptides and Proteins; Lipid Bilayers; Magnetic Resonance Spectroscopy; Micelles; Models, Molecular; Peptides; Phospholipid Ethers; Phosphorylcholine; Protein Conformation; Protein Structure, Secondary; Structure-Activity Relationship; Tryptophan; Wasp Venoms | 2001 |
Molecular dynamics simulations of adrenocorticotropin (1-24) peptide in a solvated dodecylphosphocholine (DPC) micelle and in a dimyistoylphosphatidylcholine (DMPC) bilayer.
Topics: Adrenocorticotropic Hormone; Computer Simulation; Dimyristoylphosphatidylcholine; Lipid Bilayers; Micelles; Peptides; Phosphorylcholine; Protein Binding; Time Factors | 2002 |
NMR solution structure and position of transportan in neutral phospholipid bicelles.
Topics: Amides; Amino Acid Sequence; Circular Dichroism; Dimyristoylphosphatidylcholine; Drug Carriers; Galanin; Glycerophosphates; Lipid Bilayers; Micelles; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Phospholipid Ethers; Phosphorylcholine; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Fusion Proteins; Spin Labels; Wasp Venoms | 2004 |
The role of membranes in the organization of HIV-1 Gag p6 and Vpr: p6 shows high affinity for membrane bilayers which substantially increases the interaction between p6 and Vpr.
Topics: Amino Acid Sequence; Calorimetry, Differential Scanning; Cell Membrane; Dimyristoylphosphatidylcholine; gag Gene Products, Human Immunodeficiency Virus; Gene Products, vpr; HIV-1; Lipid Bilayers; Micelles; Molecular Conformation; Molecular Dynamics Simulation; Molecular Sequence Data; Ovum; Phase Transition; Phosphorylcholine; Protein Binding | 2009 |
Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface.
Topics: Animals; Cell Membrane; Central Nervous System; Dimyristoylphosphatidylcholine; GPI-Linked Proteins; Magnetic Resonance Spectroscopy; Mice; Models, Molecular; Molecular Conformation; Myelin Proteins; Nogo Receptor 1; Phosphorylcholine; Protein Binding; Protein Folding; Protein Isoforms; Protein Structure, Tertiary; Receptors, Cell Surface | 2010 |
Magnetically oriented dodecylphosphocholine bicelles for solid-state NMR structure analysis.
Topics: Dimyristoylphosphatidylcholine; Membrane Proteins; Membranes, Artificial; Nuclear Magnetic Resonance, Biomolecular; Phosphorylcholine | 2012 |
CHARMM36 united atom chain model for lipids and surfactants.
Topics: Cholesterol; Dimyristoylphosphatidylcholine; Lipid Bilayers; Lipids; Micelles; Molecular Dynamics Simulation; Phosphorylcholine; Surface-Active Agents | 2014 |
Influence of the lipid membrane environment on structure and activity of the outer membrane protein Ail from Yersinia pestis.
Topics: Amino Acid Sequence; Bacterial Outer Membrane Proteins; Dimyristoylphosphatidylcholine; Escherichia coli; Fibronectins; Gene Expression; Glycolipids; Humans; Inositol Phosphates; Ligands; Magnetic Resonance Spectroscopy; Membrane Lipids; Molecular Sequence Data; Nanostructures; Phosphatidylglycerols; Phospholipid Ethers; Phosphorylcholine; Protein Folding; Protein Structure, Secondary; Recombinant Proteins; Virulence Factors; Yersinia pestis | 2015 |
Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments.
Topics: Amino Acid Sequence; Amyloid beta-Peptides; Cell Membrane; Detergents; Dimyristoylphosphatidylcholine; Lipid Bilayers; Micelles; Phosphorylcholine; Protein Multimerization; Protein Structure, Secondary | 2016 |
Docking and molecular dynamics simulations of the Fyn-SH3 domain with free and phospholipid bilayer-associated 18.5-kDa myelin basic protein (MBP)-Insights into a noncanonical and fuzzy interaction.
Topics: Amino Acid Sequence; Animals; Binding Sites; Dimyristoylphosphatidylcholine; Humans; Lipid Bilayers; Mice; Molecular Docking Simulation; Molecular Dynamics Simulation; Myelin Basic Protein; Peptides; Phosphorylcholine; Proline; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Structure, Tertiary; Proto-Oncogene Proteins c-fyn; src Homology Domains; Thermodynamics; Unithiol; Water | 2017 |