phosphatidylcholines has been researched along with magainin 1 peptide, xenopus in 2 studies
| Studies (phosphatidylcholines) | Trials (phosphatidylcholines) | Recent Studies (post-2010) (phosphatidylcholines) | Studies (magainin 1 peptide, xenopus) | Trials (magainin 1 peptide, xenopus) | Recent Studies (post-2010) (magainin 1 peptide, xenopus) |
|---|---|---|---|---|---|
| 32,204 | 443 | 5,593 | 67 | 0 | 10 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (50.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (50.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Duclohier, H; Molle, G; Spach, G | 1 |
| Kawano, R; Watanabe, H | 1 |
2 other study(ies) available for phosphatidylcholines and magainin 1 peptide, xenopus
| Article | Year |
|---|---|
Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers.
Topics: Amino Acid Sequence; Animals; Anti-Infective Agents; Antimicrobial Cationic Peptides; Circular Dichroism; Electric Conductivity; Ion Channels; Lipid Bilayers; Models, Biological; Molecular Sequence Data; Peptides; Phosphatidylcholines; Phosphatidylethanolamines; Protein Conformation; Skin; Xenopus laevis; Xenopus Proteins | 1989 |
Channel Current Analysis for Pore-forming Properties of an Antimicrobial Peptide, Magainin 1, Using the Droplet Contact Method.
Topics: Amino Acid Sequence; Animals; Antimicrobial Cationic Peptides; Electric Conductivity; Lab-On-A-Chip Devices; Lipid Bilayers; Magainins; Membranes, Artificial; Microfluidic Analytical Techniques; Models, Theoretical; Molecular Sequence Data; Patch-Clamp Techniques; Permeability; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylglycerols; Porosity; Xenopus laevis; Xenopus Proteins | 2016 |