surfactin peptide has been researched along with valine in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 4 (100.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bonmatin, JM; Das, BC; Labbé, H; Michel, G; Peypoux, F; Ptak, M | 1 |
| Bonmatin, JM; Das, BC; Grangemard, I; Labbe, H; Michel, G; Peypoux, F; Ptak, M; Wallach, J | 1 |
| Cosmina, P; de Ferra, F; Galli, G; Grandi, G; van Sinderen, D; Venema, G; Withoff, S | 1 |
| Quadri, LE; Walsh, CT; Weinreb, PH; Zuber, P | 1 |
4 other study(ies) available for surfactin peptide and valine
| Article | Year |
|---|---|
Isolation and characterization of a new variant of surfactin, the [Val7]surfactin.
Topics: Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Genetic Variation; Lipopeptides; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Peptides, Cyclic; Spectrometry, Mass, Fast Atom Bombardment; Valine | 1991 |
[Ala4]surfactin, a novel isoform from Bacillus subtilis studied by mass and NMR spectroscopies.
Topics: Alanine; Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Chromatography, Gas; Chromatography, Thin Layer; Culture Media; Hydrolysis; Lipopeptides; Magnetic Resonance Spectroscopy; Mass Spectrometry; Molecular Sequence Data; Peptides, Cyclic; Stereoisomerism; Structure-Activity Relationship; Surface Tension; Surface-Active Agents; Valine | 1994 |
Characterization of the srfA locus of Bacillus subtilis: only the valine-activating domain of srfA is involved in the establishment of genetic competence.
Topics: Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Binding Sites; Gene Expression Regulation, Bacterial; Lipopeptides; Molecular Sequence Data; Open Reading Frames; Peptide Synthases; Peptides, Cyclic; Protein Structure, Tertiary; Signal Transduction; Spores, Bacterial; Transformation, Bacterial; Valine | 1993 |
Stoichiometry and specificity of in vitro phosphopantetheinylation and aminoacylation of the valine-activating module of surfactin synthetase.
Topics: Acylation; Adenosine Monophosphate; Aminoacyltransferases; Bacillus subtilis; Bacterial Proteins; Catalysis; Enzyme Stability; Escherichia coli; Genetic Vectors; Kinetics; Lipopeptides; Pantetheine; Peptide Synthases; Peptides, Cyclic; Protein Processing, Post-Translational; Recombinant Proteins; Substrate Specificity; Transferases (Other Substituted Phosphate Groups); Valine | 1998 |