3-methylcatechol has been researched along with 4-methylcatechol in 7 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (28.57) | 18.2507 |
| 2000's | 1 (14.29) | 29.6817 |
| 2010's | 2 (28.57) | 24.3611 |
| 2020's | 2 (28.57) | 2.80 |
| Authors | Studies |
|---|---|
| Araki, M; Iwata, H; Kanda, N; Masuda, K; Okuno, Y; Sagae, Y | 1 |
| Cerdan, P; Harayama, S; Rekik, M; Timmis, KN; Wasserfallen, A | 1 |
| Aoki, K; Kodama, N; Murakami, S; Shinke, R | 1 |
| Damborsky, J; Hatta, T; Kimbara, K; Kiyohara, H; Mukerjee-Dhar, G | 1 |
| Guzik, U; Hupert-Kocurek, K; Wojcieszyńska, D | 1 |
| Huang, J; Li, X; Su, Y; Wang, M; Wang, W; Wang, Y; Zhao, X | 1 |
| Cao, M; Li, J; Li, Z; Liu, J | 1 |
7 other study(ies) available for 3-methylcatechol and 4-methylcatechol
| Article | Year |
|---|---|
Discovery of natural TRPA1 activators through pharmacophore-based virtual screening and a biological assay.
Topics: Biological Products; Dose-Response Relationship, Drug; Drug Discovery; Drug Evaluation, Preclinical; Humans; Molecular Structure; Structure-Activity Relationship; TRPA1 Cation Channel | 2021 |
Substrate specificity of catechol 2,3-dioxygenase encoded by TOL plasmid pWW0 of Pseudomonas putida and its relationship to cell growth.
Topics: Ascorbic Acid; Catechol 2,3-Dioxygenase; Catechols; Cell Division; Dioxygenases; Enzyme Reactivators; Ferrous Compounds; Iron; Kinetics; Mutation; Oxygen; Oxygenases; Plasmids; Pseudomonas putida; Substrate Specificity | 1994 |
Classification of catechol 1,2-dioxygenase family: sequence analysis of a gene for the catechol 1,2-dioxygenase showing high specificity for methylcatechols from Gram+ aniline-assimilating Rhodococcus erythropolis AN-13.
Topics: Amino Acid Sequence; Arthrobacter; Base Sequence; Binding Sites; Catechol 1,2-Dioxygenase; Catechols; Cloning, Molecular; Dioxygenases; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Gene Library; Molecular Sequence Data; Open Reading Frames; Oxygenases; Restriction Mapping; Rhodococcus; Ribosomes; Sequence Homology, Amino Acid; Substrate Specificity; Transformation, Genetic | 1997 |
Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8.
Topics: Amino Acid Sequence; Bacillus; Binding Sites; Biphenyl Compounds; Catechols; Chelating Agents; Chromatography; Cloning, Molecular; Dioxygenases; DNA; Edetic Acid; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Ethanolamines; Hydrogen-Ion Concentration; Kinetics; Ligands; Manganese; Models, Chemical; Models, Molecular; Molecular Sequence Data; Naphthalenes; Oxygenases; Phylogeny; Protein Binding; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrophotometry; Substrate Specificity; Temperature; Time Factors | 2003 |
Characterization of catechol 2,3-dioxygenase from Planococcus sp. strain S5 induced by high phenol concentration.
Topics: Bacterial Proteins; Base Sequence; Biodegradation, Environmental; Catechol 2,3-Dioxygenase; Catechols; Culture Media; Enzyme Activation; Enzyme Stability; Genes, Bacterial; Hydrogen-Ion Concentration; Molecular Sequence Data; Phenol; Planococcus Bacteria; Sequence Alignment; Sequence Homology; Species Specificity; Substrate Specificity; Time Factors | 2012 |
Formate-assisted analytical pyrolysis of kraft lignin to phenols.
Topics: Catalysis; Catechols; Formates; Lignin; Pyrolysis | 2019 |
Expression and characterization of catechol 1,2-dioxygenase from Oceanimonas marisflavi 102-Na3.
Topics: Aeromonadaceae; Amino Acid Sequence; Bacterial Proteins; Catechol 1,2-Dioxygenase; Catechols; Cloning, Molecular; Escherichia coli; Gene Expression; Genetic Vectors; Hydrogen-Ion Concentration; Kinetics; Molecular Weight; Phylogeny; Protein Multimerization; Pyrogallol; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity | 2021 |