Page last updated: 2024-08-17

1-hydroxy-2-naphthoic acid and 2,5-dihydroxybenzoic acid

1-hydroxy-2-naphthoic acid has been researched along with 2,5-dihydroxybenzoic acid in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	1 (50.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Hanna, K	1
Briganti, F; Bürger, S; Eppinger, E; Ferraroni, M; Peng, G; Steimer, L; Stolz, A	1

Other Studies

2 other study(ies) available for 1-hydroxy-2-naphthoic acid and 2,5-dihydroxybenzoic acid

Article	Year
Sorption of two aromatic acids onto iron oxides: experimental study and modeling. Journal of colloid and interface science, 2007, May-15, Volume: 309, Issue:2 Topics: Adsorption; Calcium Chloride; Ferric Compounds; Gentisates; Hydrogen-Ion Concentration; Models, Chemical; Naphthols; Osmolar Concentration; Surface Properties	2007
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. Biochimica et biophysica acta, 2015, Volume: 1854, Issue:10 Pt A 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

Article

Year

Sorption of two aromatic acids onto iron oxides: experimental study and modeling.

Journal of colloid and interface science, 2007, May-15, Volume: 309, Issue:2

Topics: Adsorption; Calcium Chloride; Ferric Compounds; Gentisates; Hydrogen-Ion Concentration; Models, Chemical; Naphthols; Osmolar Concentration; Surface Properties

2007

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.

Biochimica et biophysica acta, 2015, Volume: 1854, Issue:10 Pt A

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