dithionitrobenzoic acid has been researched along with 11-cis-retinal in 7 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 6 (85.71) | 18.7374 |
| 1990's | 1 (14.29) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Chizhevich, EP; Korchagin, VP; Shukoliukov, SA | 1 |
| Bonting, SL; Daemen, FJ; de Grip, WJ; Regan, CM | 1 |
| McDowell, JH; Williams, TP | 1 |
| Bonting, SL; Daemen, FJ; Jansen, PA; Van Breugel, PJ | 1 |
| Bonting, SL; Daemen, FJ; De Grip, WJ | 1 |
| Hofmann, KP; Reichert, J | 1 |
| van Kuijk, FJ | 1 |
7 other study(ies) available for dithionitrobenzoic acid and 11-cis-retinal
| Article | Year |
|---|---|
[Accessibility of sulfhydryl groups to 5,5'-dithiobis-2-nitrobenzoic acid and acid-base properties of bovine and walleye pollock rhodopsin preparations].
Topics: Animals; Cattle; Cetrimonium Compounds; Chemical Phenomena; Chemistry; Digitonin; Dithionitrobenzoic Acid; Fishes; Hydrogen-Ion Concentration; Light; Nitrobenzoates; Papain; Photoreceptor Cells; Polyethylene Glycols; Retinal Pigments; Rhodopsin; Sodium Dodecyl Sulfate; Sulfhydryl Compounds | 1978 |
Biochemical aspects of the visual process. XXXIX. Sulfhydryl group reactivity as a probe of transient protein conformational changes during rhodopsin photolysis.
Topics: Animals; Cattle; Cell Membrane; Dithionitrobenzoic Acid; Light; Photolysis; Photoreceptor Cells; Protein Binding; Protein Conformation; Retinal Pigments; Rhodopsin; Vision, Ocular | 1978 |
Oxidation states of four sulfurs of rhodopsin before and after bleaching.
Topics: Animals; Darkness; Disulfides; Dithionitrobenzoic Acid; Hot Temperature; Kinetics; Light; Oxidation-Reduction; Protein Binding; Retinal Pigments; Rhodopsin; Sulfhydryl Compounds | 1976 |
Biochemical aspects of the visual process. XXXIV. Relation between sulfhydryl groups and properties of rhodopsin studied by means of methylmercuric iodide.
Topics: Animals; Binding Sites; Cattle; Cell Membrane; Dithionitrobenzoic Acid; Methylmercury Compounds; Photolysis; Photoreceptor Cells; Retinal Pigments; Rhodopsin; Spectrophotometry; Sulfhydryl Compounds | 1976 |
Biochemical aspects of the visual process. XXVIII. Classification of sulfhydryl groups in phodopsin and other photoreceptor membrane proteins.
Topics: Animals; Binding Sites; Cattle; Cell Membrane; Chloromercuribenzoates; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Ethylmaleimide; Kinetics; Nerve Tissue Proteins; Photoreceptor Cells; Protein Binding; Retinal Pigments; Rhodopsin; Sulfhydryl Compounds; Time Factors; Ultracentrifugation; Vision, Ocular | 1975 |
Chemical probing of the light-induced interaction between rhodopsin and G-protein. Near-infrared light-scattering and sulfhydryl modifications.
Topics: Animals; Cattle; Dithionitrobenzoic Acid; Electrophoresis, Polyacrylamide Gel; Ethylmaleimide; GTP-Binding Proteins; Guanosine Diphosphate; Guanosine Triphosphate; Infrared Rays; Light; Photoreceptor Cells; Retinal Pigments; Rhodopsin; Rod Cell Outer Segment; Scattering, Radiation | 1985 |
4-Hydroxynonenal interaction with rhodopsin.
Topics: Aldehydes; Animals; Binding Sites; Cattle; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Dithionitrobenzoic Acid; Mass Spectrometry; Peptide Fragments; Rhodopsin; Sulfhydryl Compounds; Trypsin | 1997 |