4-aminophenylalanine has been researched along with chloramphenicol in 5 studies
Studies (4-aminophenylalanine) | Trials (4-aminophenylalanine) | Recent Studies (post-2010) (4-aminophenylalanine) | Studies (chloramphenicol) | Trials (chloramphenicol) | Recent Studies (post-2010) (chloramphenicol) |
---|---|---|---|---|---|
52 | 0 | 14 | 20,113 | 388 | 1,464 |
Protein | Taxonomy | 4-aminophenylalanine (IC50) | chloramphenicol (IC50) |
---|---|---|---|
30S ribosomal protein S6 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S7 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L15 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L10 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L11 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L7/L12 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L19 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L1 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L20 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L27 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L28 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L29 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L31 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L31 type B | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L32 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L33 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L34 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L35 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L36 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S10 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S11 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S12 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S13 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S16 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S18 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S19 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S20 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S2 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S3 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S4 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S5 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S8 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S9 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L13 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L14 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L16 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L23 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S15 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L17 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L21 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L30 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L6 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S14 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S17 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S1 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L18 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L2 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L3 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L24 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L4 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L22 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L5 | Escherichia coli K-12 | 0.43 | |
30S ribosomal protein S21 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L25 | Escherichia coli K-12 | 0.43 | |
50S ribosomal protein L36 2 | Escherichia coli K-12 | 0.43 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 3 (60.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 1 (20.00) | 29.6817 |
2010's | 1 (20.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Francis, MM; Jones, A; Vining, LC | 1 |
Beschle, HG; Lingens, F; Süssmuth, R | 1 |
Adamek, TL; Lewis, EA; Vining, LC; White, RL | 1 |
McGrath, R; Sala, F; Siddiqueullah, M; Vining, LC; Westlake, DW | 1 |
Chakrabarti, M; Lipscomb, JD; Makris, TM; Münck, E | 1 |
5 other study(ies) available for 4-aminophenylalanine and chloramphenicol
Article | Year |
---|---|
Biosynthesis of chloramphenicol in Streptomyces sp. 3022a. Properties of an aminotransferase accepting p-aminophenylalanine as a substrate.
Topics: Amino Acids, Diamino; Cell-Free System; Chloramphenicol; Phenylalanine; Stereoisomerism; Streptomyces; Substrate Specificity; Transaminases; Tyrosine | 1978 |
Conversion of chloramphenicol degradation products by tyrosine aminotransferase from Flavobacteria.
Topics: Chloramphenicol; Flavobacterium; Kinetics; Phenylalanine; Substrate Specificity; Tyrosine; Tyrosine Transaminase | 1982 |
Metabolites of a blocked chloramphenicol producer.
Topics: 4-Aminobenzoic Acid; Anti-Bacterial Agents; Chloramphenicol; Chromatography, High Pressure Liquid; Magnetic Resonance Spectroscopy; Mass Spectrometry; Molecular Structure; Phenylalanine; Streptomyces | 2003 |
p-Aminophenylalanine and threo-p-aminophenylserine; specific precursors of chloramphenicol.
Topics: Carbon Radioisotopes; Chloramphenicol; Nitrogen Isotopes; Phenylalanine; Serine; Streptomyces | 1967 |
A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis.
Topics: Amino Acid Sequence; Bacterial Proteins; Biosynthetic Pathways; Chloramphenicol; Electron Spin Resonance Spectroscopy; Hydroxylation; Iron; Kinetics; Mixed Function Oxygenases; Models, Chemical; Molecular Sequence Data; Molecular Structure; Operon; Peptide Synthases; Phenylalanine; Sequence Homology, Amino Acid; Spectroscopy, Mossbauer; Streptomyces; Substrate Specificity | 2010 |