cinnamoyl-coenzyme a has been researched along with vanillin in 1 studies
Studies (cinnamoyl-coenzyme a) | Trials (cinnamoyl-coenzyme a) | Recent Studies (post-2010) (cinnamoyl-coenzyme a) | Studies (vanillin) | Trials (vanillin) | Recent Studies (post-2010) (vanillin) |
---|---|---|---|---|---|
20 | 0 | 6 | 1,470 | 19 | 840 |
Protein | Taxonomy | cinnamoyl-coenzyme a (IC50) | vanillin (IC50) |
---|---|---|---|
Transcription intermediary factor 1-alpha | Homo sapiens (human) | 0.162 | |
E3 ubiquitin-protein ligase TRIM33 | Homo sapiens (human) | 0.3256 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 1 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Brzozowski, AM; Grogan, G; Lebedev, A; Leonard, PM; Marshall, CM; Smith, DJ; Verma, CS; Walton, NJ | 1 |
1 other study(ies) available for cinnamoyl-coenzyme a and vanillin
Article | Year |
---|---|
The 1.8 A resolution structure of hydroxycinnamoyl-coenzyme A hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that catalyses the transformation of feruloyl-coenzyme A to vanillin.
Topics: Acyl Coenzyme A; Benzaldehydes; Binding Sites; Catalysis; Crystallography, X-Ray; Enoyl-CoA Hydratase; Hydro-Lyases; Models, Molecular; Protein Folding; Protein Structure, Quaternary; Protein Structure, Secondary; Pseudomonas fluorescens | 2006 |