erythrosine has been researched along with tritrpticin 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 | 4 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Hahm, KS; Kim, JI; Kim, Y; Kim, YC; Yang, ST; Yub Shin, SY | 1 |
| Kernaghan, SD; Nguyen, LT; Rekdal, Ø; Schibli, DJ; Vogel, HJ | 1 |
| Hahm, KS; Kim, JI; Kim, Y; Lan, H; Lee, JS; Park, IS; Park, Y; Park, YS; Shin, SY; Yang, ST; You, HJ; Zhu, WL | 1 |
| Aarabi, MH; Andrushchenko, VV; Nguyen, LT; Prenner, EJ; Vogel, HJ | 1 |
4 other study(ies) available for erythrosine and tritrpticin
| Article | Year |
|---|---|
Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide.
Topics: Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Bacteria; Cathelicidins; Circular Dichroism; Dose-Response Relationship, Drug; Fluoresceins; Fluorescent Dyes; Fungi; Hemolysin Proteins; Liposomes; Models, Molecular; Oligopeptides; Protein Conformation; Protein Structure, Secondary | 2002 |
Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures.
Topics: Amino Acid Substitution; Anti-Infective Agents; Escherichia coli; Fluoresceins; Hemolysis; Humans; In Vitro Techniques; Liposomes; Magnetic Resonance Spectroscopy; Micelles; Microbial Sensitivity Tests; Models, Molecular; Oligopeptides; Phosphorylcholine; Staphylococcus aureus; Structure-Activity Relationship | 2006 |
Effects of Pro --> peptoid residue substitution on cell selectivity and mechanism of antibacterial action of tritrpticin-amide antimicrobial peptide.
Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Anti-Bacterial Agents; Bacteria; Cell Membrane; Cells, Cultured; Circular Dichroism; Dose-Response Relationship, Drug; Erythrocytes; Fluoresceins; HeLa Cells; Hemolysis; Humans; Mice; Microbial Sensitivity Tests; Microscopy, Confocal; NIH 3T3 Cells; Oligopeptides; Peptides; Peptoids; Plasmids; Proline; Protein Binding | 2006 |
Thermodynamics of the interactions of tryptophan-rich cathelicidin antimicrobial peptides with model and natural membranes.
Topics: Amino Acid Sequence; Antimicrobial Cationic Peptides; Calorimetry; Cathelicidins; Escherichia coli; Fluoresceins; Kinetics; Molecular Sequence Data; Oligopeptides; Protein Binding; Thermodynamics; Tryptophan; Unilamellar Liposomes | 2008 |