prodan has been researched along with 1-anilino-8-naphthalenesulfonate in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (25.00) | 18.2507 |
2000's | 1 (25.00) | 29.6817 |
2010's | 2 (50.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bhattacharyya, B; Mazumdar, M; Parrack, PK | 1 |
Bhattacharya, S; Bhattacharyya, M; Chakrabarti, A; Ray, S | 1 |
Chakrabarti, A; Mitra, M; Mukhopadhyay, C; Patra, M | 1 |
Andreeva, TV; Ayvazyan, NM; Ghazaryan, NA; Ghulikyan, L; Kishmiryan, A; Lomonte, B; Tsetlin, VI; Utkin, YN | 1 |
4 other study(ies) available for prodan and 1-anilino-8-naphthalenesulfonate
Article | Year |
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Interaction of Prodan with tubulin. A fluorescence spectroscopic study.
Topics: 2-Naphthylamine; Anilino Naphthalenesulfonates; Binding Sites; Binding, Competitive; Fluorescence Polarization; Fluorescent Dyes; Protein Binding; Spectrometry, Fluorescence; Tubulin | 1992 |
Chaperone activity and prodan binding at the self-associating domain of erythroid spectrin.
Topics: 2-Naphthylamine; Alcohol Dehydrogenase; Alkaline Phosphatase; alpha-Glucosidases; Amino Acid Sequence; Anilino Naphthalenesulfonates; Animals; Binding Sites; Cattle; Dimerization; Dose-Response Relationship, Drug; Edetic Acid; Erythrocytes; Escherichia coli Proteins; Heat-Shock Proteins; Horses; Hot Temperature; HSP40 Heat-Shock Proteins; HSP90 Heat-Shock Proteins; Humans; Insulin; Kinetics; Molecular Chaperones; Molecular Sequence Data; Mutation; Pancreas; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrin; Spectrometry, Fluorescence; Temperature; Time Factors | 2004 |
Binding of polarity-sensitive hydrophobic ligands to erythroid and nonerythroid spectrin: fluorescence and molecular modeling studies.
Topics: 2-Naphthylamine; Anilino Naphthalenesulfonates; Animals; Carrier Proteins; Erythrocytes; Fluorescent Dyes; Goats; Hydrophobic and Hydrophilic Interactions; Microfilament Proteins; Molecular Docking Simulation; Protein Interaction Domains and Motifs; Protein Multimerization; Pyrenes; Sheep; Spectrin; Spectrometry, Fluorescence; Thermodynamics | 2014 |
Phospholipases a2 from Viperidae snakes: Differences in membranotropic activity between enzymatically active toxin and its inactive isoforms.
Topics: 2-Naphthylamine; Amino Acid Substitution; Anilino Naphthalenesulfonates; Animals; Aspartic Acid; Biological Transport; Brain Chemistry; Catalytic Domain; Fluorescent Dyes; Laurates; Lipid Bilayers; Lysine; Male; Membrane Fluidity; Phospholipases A2; Rats; Reptilian Proteins; Serine; Snake Venoms; Structure-Activity Relationship; Unilamellar Liposomes; Viperidae; Water | 2015 |