1-hydroxy-2-naphthoic acid has been researched along with salicylates 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 | 0 (0.00) | 29.6817 |
| 2010's | 4 (100.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Briganti, F; Bürger, S; Ferraroni, M; Matera, I; Reichert, S; Scozzafava, A; Steimer, L; Stolz, A | 1 |
| Jeong, KW; Ku, JM; Nam, TG; Park, MW; Park, SM; Yang, JE | 1 |
| Briganti, F; Bürger, S; Eppinger, E; Ferraroni, M; Peng, G; Steimer, L; Stolz, A | 1 |
| Coppotelli, BM; Macchi, M; Martinez, M; Morelli, IS; Tauil, RMN; Valacco, MP | 1 |
4 other study(ies) available for 1-hydroxy-2-naphthoic acid and salicylates
| Article | Year |
|---|---|
The salicylate 1,2-dioxygenase as a model for a conventional gentisate 1,2-dioxygenase: crystal structures of the G106A mutant and its adducts with gentisate and salicylate.
Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Catalytic Domain; Crystallography, X-Ray; Dioxygenases; Gentisates; Glycine; Hydrogen Bonding; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Naphthols; Phyllobacteriaceae; Protein Conformation; Salicylates; Substrate Specificity | 2013 |
Hydroxynaphthoic acids identified in a high throughput screening potently ameliorate endoplasmic reticulum stress as novel chemical chaperones.
Topics: DNA-Binding Proteins; Down-Regulation; Endoplasmic Reticulum; Endoplasmic Reticulum Chaperone BiP; Endoplasmic Reticulum Stress; Endoribonucleases; HEK293 Cells; Hep G2 Cells; Humans; Naphthols; Protein Serine-Threonine Kinases; Regulatory Factor X Transcription Factors; Salicylates; Structure-Activity Relationship; Transcription Factors; X-Box Binding Protein 1 | 2013 |
Function of different amino acid residues in the reaction mechanism of gentisate 1,2-dioxygenases deduced from the analysis of mutants of the salicylate 1,2-dioxygenase from Pseudaminobacter salicylatoxidans.
Topics: Alphaproteobacteria; Amino Acid Sequence; Amino Acids; Bacterial Proteins; Dioxygenases; Escherichia coli; Gene Expression; Gentisates; Kinetics; Molecular Sequence Data; Mutation; Naphthols; Oxidation-Reduction; Protein Conformation; Recombinant Proteins; Salicylates; Sequence Alignment; Sequence Homology, Amino Acid; Structure-Activity Relationship; Substrate Specificity | 2015 |
Insights into the genome and proteome of Sphingomonas paucimobilis strain 20006FA involved in the regulation of polycyclic aromatic hydrocarbon degradation.
Topics: Anthracenes; Bacterial Proteins; Biodegradation, Environmental; Computer Simulation; Dioxygenases; DNA, Bacterial; Fluorenes; Glucose; Hydroxybenzoates; Metabolic Networks and Pathways; Naphthols; Phenanthrenes; Polycyclic Aromatic Hydrocarbons; Proteome; Proteomics; Salicylates; Soil Microbiology; Soil Pollutants; Sphingomonas; Thiophenes; Trichloroacetic Acid; Whole Genome Sequencing | 2017 |