erythrosine has been researched along with pardaxin in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 7 (87.50) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (12.50) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Pouny, Y; Shai, Y | 1 |
| Rapaport, D; Shai, Y | 1 |
| Bach, D; Shai, Y; Yanovsky, A | 1 |
| Nagaraj, R; Saberwal, G | 1 |
| Carafoli, E; Eshel, Y; Salomon, Y; Shai, Y; Vorherr, T | 1 |
| Nir, S; Peled, R; Rapaport, D; Shai, Y | 1 |
| Adermann, K; Erdmann, G; Hochman, J; Kassebaum, C; Lazarovici, P; Paul, Y; Weiss, A; Wellhöner, H | 1 |
| Bertelsen, K; Johansen, CH; Nielsen, NC; Otzen, DE; Pedersen, JM; Skrydstrup, T; Vad, BS | 1 |
8 other study(ies) available for erythrosine and pardaxin
| Article | Year |
|---|---|
Interaction of D-amino acid incorporated analogues of pardaxin with membranes.
Topics: Amino Acids; Cell Membrane Permeability; Circular Dichroism; Diffusion; Erythrocyte Membrane; Fish Venoms; Fluoresceins; Fluorescence; Fluorescent Dyes; Humans; Liposomes; Proline; Protein Structure, Secondary; Solubility; Stereoisomerism; Valinomycin | 1992 |
Aggregation and organization of pardaxin in phospholipid membranes. A fluorescence energy transfer study.
Topics: Amino Acid Sequence; Chromatography, High Pressure Liquid; Coloring Agents; Fish Venoms; Fluoresceins; Fluorescence; Lipid Bilayers; Liposomes; Molecular Sequence Data; Peptides; Phospholipids; Rhodamines | 1992 |
Channel formation properties of synthetic pardaxin and analogues.
Topics: Amino Acid Sequence; Cell Survival; Erythrocytes; Fish Venoms; Fluoresceins; Humans; Indicators and Reagents; Ion Channels; Lipid Bilayers; Membrane Potentials; Molecular Sequence Data; Peptides; Structure-Activity Relationship | 1990 |
Interaction of hydrophobic peptides with model membranes: slow binding to membranes and not subtle variations in pore structure is responsible for the gradual release of entrapped solutes.
Topics: Amino Acid Sequence; Fish Venoms; Fluoresceins; Membranes; Molecular Sequence Data; Peptides; Phosphatidylcholines | 1993 |
Synthetic peptides corresponding to the calmodulin-binding domains of skeletal muscle myosin light chain kinase and human erythrocyte Ca2+ pump interact with and permeabilize liposomes and cell membranes.
Topics: alpha-MSH; Amino Acid Sequence; Animals; Binding Sites; Calcium-Transporting ATPases; Calmodulin; Calmodulin-Binding Proteins; Cell Membrane; Cell Membrane Permeability; Erythrocytes; Fish Venoms; Fluoresceins; Humans; Lipid Bilayers; Melanoma, Experimental; Melitten; Mice; Molecular Sequence Data; Muscles; Myosin-Light-Chain Kinase; Peptides; Tumor Cells, Cultured | 1993 |
Reversible surface aggregation in pore formation by pardaxin.
Topics: Amino Acid Sequence; Biophysical Phenomena; Biophysics; Cholesterol; Fish Venoms; Fluoresceins; Fluorescent Dyes; Kinetics; Liposomes; Models, Chemical; Molecular Sequence Data; Phosphatidylcholines; Phosphatidylserines; Surface Properties; Temperature | 1996 |
Translocation of acylated pardaxin into cells.
Topics: Acylation; Animals; Binding Sites; Binding, Competitive; Biological Transport; Cattle; Cell Line; Cell Membrane; Cell Membrane Permeability; Cell Nucleolus; Chromaffin Cells; Dose-Response Relationship, Drug; Fish Venoms; Fluoresceins; Microscopy, Confocal; Temperature; Time Factors | 1998 |
Pardaxin permeabilizes vesicles more efficiently by pore formation than by disruption.
Topics: Amino Acid Sequence; Fish Venoms; Fluoresceins; Hydrogen-Ion Concentration; Kinetics; Lipid Metabolism; Lipids; Magnetic Resonance Spectroscopy; Microscopy, Confocal; Molecular Sequence Data; Permeability; Porosity; Protein Conformation; Protons; Unilamellar Liposomes | 2010 |