erythrosine has been researched along with 1,5-i-aedans in 19 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 8 (42.11) | 18.7374 |
| 1990's | 8 (42.11) | 18.2507 |
| 2000's | 3 (15.79) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Dobryszycki, P; Kochman, M; Sakowicz, R | 1 |
| Seifried, SE; von Hippel, PH; Wang, Y | 1 |
| Baba, A; Kawakita, M; Nakamura, T | 1 |
| Bigelow, DJ; Garcia de Ancos, J; Inesi, G; Squier, TC | 1 |
| Gorman, JJ | 1 |
| Chung, DG; Lewis, PN | 1 |
| Bucci, E; Kowalczyk, J; Sassaroli, M | 1 |
| Lowey, S; Marsh, DJ | 1 |
| Cittanova, N; Evrain, C; Jayle, MF; Rajkowski, KM | 1 |
| Duong, AM; Reisler, E | 1 |
| dos Remedios, CG; Moens, PD; Yee, DJ | 1 |
| Alvear, M; Cardemil, E; Encinas, MV; Herrera, L | 1 |
| Baker, KJ; East, JM; Lee, AG | 1 |
| Avrova, SV; Chacko, S; Horiuchi, KY | 1 |
| dos Remedios, CG; Funatsu, T; Ishiwata, S; Miki, M; Shin, I; Yasuda, K | 1 |
| Hild, G; Nyitrai, M; Somogyi, B | 1 |
| Lubsen, NH; Prat, K; Putilina, T; Skouri-Panet, F; Tardieu, A | 1 |
| Cowan, JA; Nuth, M | 1 |
| Prochniewicz, E; Thomas, DD | 1 |
19 other study(ies) available for erythrosine and 1,5-i-aedans
| Article | Year |
|---|---|
Site-specific modification or rabbit muscle aldolase with fluorescent probes.
Topics: Animals; Fluoresceins; Fluorescent Dyes; Fructose-Bisphosphate Aldolase; Naphthalenesulfonates; p-Dimethylaminoazobenzene; Rabbits; Spectrometry, Fluorescence | 1990 |
Fluorescent modification of the cysteine 202 residue of Escherichia coli transcription termination factor rho.
Topics: Adenosine Triphosphatases; Chemical Phenomena; Chemistry; Cross-Linking Reagents; Cysteine; Energy Transfer; Escherichia coli; Fluoresceins; Fluorescent Dyes; Macromolecular Substances; Naphthalenesulfonates; Rho Factor; RNA; Spectrophotometry; Sulfhydryl Reagents; Transcription Factors; Transcription, Genetic | 1988 |
Chemical modification and fluorescence labeling study of Ca2+,Mg2+-adenosine triphosphatase of sarcoplasmic reticulum using iodoacetamide and its N-substituted derivatives.
Topics: Adenosine Diphosphate; Animals; Binding Sites; Ca(2+) Mg(2+)-ATPase; Calcium; Calcium-Transporting ATPases; Chemical Phenomena; Chemistry; Fluoresceins; Fluorescent Dyes; Iodoacetamide; Iodoacetates; Naphthalenesulfonates; Nucleotides; Peptide Fragments; Protein Conformation; Rabbits; Sarcoplasmic Reticulum; Sulfhydryl Compounds; Thionucleotides; Trypsin | 1986 |
Localization of site-specific probes on the Ca-ATPase of sarcoplasmic reticulum using fluorescence energy transfer.
Topics: Adenosine Monophosphate; Affinity Labels; Animals; Binding Sites; Calcium-Transporting ATPases; Energy Transfer; Fluorescein-5-isothiocyanate; Fluoresceins; In Vitro Techniques; Naphthalenesulfonates; Rabbits; Sarcoplasmic Reticulum; Spectrometry, Fluorescence; Sulfhydryl Compounds; Thiocyanates | 1987 |
Fluorescent labeling of cysteinyl residues to facilitate electrophoretic isolation of proteins suitable for amino-terminal sequence analysis.
Topics: Amino Acid Sequence; Animals; Cattle; Cysteine; Electrophoresis, Polyacrylamide Gel; Fluoresceins; Fluorescence; Naphthalenesulfonates; Proteins; Serum Albumin, Bovine; Sodium Dodecyl Sulfate | 1987 |
Internal architecture of the core nucleosome: fluorescence energy transfer studies at methionine-84 of histone H4.
Topics: Animals; Chickens; DNA; Energy Transfer; Fluoresceins; Fluorescent Dyes; Histones; Naphthalenesulfonates; Nucleosomes; Osmolar Concentration; Spectrometry, Fluorescence | 1986 |
Probe dependence of correlation times in heme-free extrinsically labeled human hemoglobin.
Topics: Anilino Naphthalenesulfonates; Apoproteins; Fluoresceins; Fluorescent Dyes; Hemoglobins; Humans; Hydrogen-Ion Concentration; Naphthalenesulfonates; Pyridoxal Phosphate; Spectrometry, Fluorescence; Viscosity | 1986 |
Fluorescence energey transfer in myosin subfragment-1.
Topics: Adenosine Triphosphatases; Adenosine Triphosphate; Amino Acids; Animals; Energy Transfer; Fluoresceins; Iodoacetamide; Magnesium; Muscles; Myosins; Naphthalenesulfonates; Protein Binding; Rabbits; Spectrometry, Fluorescence | 1980 |
The preparation of three fluorescence-labeled derivatives of testosterone.
Topics: Chemical Phenomena; Chemistry; Cysteamine; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescent Antibody Technique; Iodoacetamide; Naphthalenesulfonates; Spectrophotometry, Ultraviolet; Testosterone; Thiocyanates | 1980 |
C-terminus on actin: spectroscopic and immunochemical examination of its role in actomyosin interactions.
Topics: Actins; Actomyosin; Animals; Aziridines; Cysteine; Dansyl Compounds; Fluorescein; Fluoresceins; Fluorescent Dyes; Immunoglobulin G; Myosin Subfragments; Naphthalenesulfonates; Peptide Fragments; Rabbits; Spectrometry, Fluorescence | 1994 |
Determination of the radial coordinate of Cys-374 in F-actin using fluorescence resonance energy transfer spectroscopy: effect of phalloidin on polymer assembly.
Topics: Actins; Amino Acid Sequence; Animals; Cysteine; Electrophoresis, Polyacrylamide Gel; Energy Transfer; Fluoresceins; Fluorescent Dyes; Models, Chemical; Molecular Sequence Data; Muscle, Skeletal; Naphthalenesulfonates; Phalloidine; Polymers; Rabbits; Reference Standards; Spectrometry, Fluorescence; Sulfhydryl Reagents | 1994 |
Resonance energy transfer determination of the distance between the four cysteine-364 residues in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase.
Topics: Amino Acid Sequence; Binding Sites; Chemical Phenomena; Chemistry, Physical; Cross-Linking Reagents; Cysteine; Energy Transfer; Fluoresceins; Fluorescent Dyes; Macromolecular Substances; Molecular Sequence Data; Naphthalenesulfonates; Oxadiazoles; Phosphoenolpyruvate Carboxykinase (GTP); Saccharomyces cerevisiae; Spectrometry, Fluorescence; Spectrophotometry; Sulfhydryl Reagents | 1994 |
Localization of the hinge region of the Ca(2+)-ATPase of sarcoplasmic reticulum using resonance energy transfer.
Topics: Binding Sites; Calcium-Transporting ATPases; Energy Transfer; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescent Dyes; Muscles; Naphthalenesulfonates; Phospholipids; Protein Conformation; Sarcoplasmic Reticulum; Spectrometry, Fluorescence; Water | 1994 |
Modulation of actin conformation and inhibition of actin filament velocity by calponin.
Topics: Actins; Animals; Calcium-Binding Proteins; Calponins; Chickens; Fluorescein; Fluoresceins; Fluorescence Polarization; Fluorescent Dyes; Maleimides; Microfilament Proteins; Muscle Contraction; Muscle, Skeletal; Muscle, Smooth; Myosin Subfragments; Naphthalenesulfonates; Phalloidine; Phosphorylation; Protein Binding; Protein Conformation; Rhodamines | 1996 |
Interhead distances in myosin attached to F-actin estimated by fluorescence energy transfer spectroscopy.
Topics: Actins; Animals; Energy Transfer; Fluoresceins; Fluorescent Dyes; Kinetics; Models, Chemical; Models, Structural; Muscle, Skeletal; Myosin Subfragments; Myosins; Naphthalenesulfonates; Rabbits; Spectrometry, Fluorescence; Sulfhydryl Compounds | 1997 |
Intermonomer flexibility of Ca- and Mg-actin filaments at different pH values.
Topics: Actin Cytoskeleton; Actins; Animals; Calcium; Fluoresceins; Hydrogen-Ion Concentration; Magnesium; Muscle, Skeletal; Naphthalenesulfonates; Rabbits; Spectrum Analysis | 2002 |
Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins.
Topics: alpha-Crystallins; Animals; beta-Crystallins; Binding Sites; Blotting, Western; Cattle; Chromatography, Gel; Fluoresceins; Fluorescence Resonance Energy Transfer; gamma-Crystallins; Lens, Crystalline; Molecular Chaperones; Naphthalenesulfonates; Protein Binding; Scattering, Radiation; Spectrometry, Fluorescence; Sulfhydryl Reagents; Temperature; Time Factors; X-Rays | 2003 |
Iron-sulfur cluster biosynthesis: characterization of IscU-IscS complex formation and a structural model for sulfide delivery to the [2Fe-2S] assembly site.
Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Calorimetry; Carbon-Sulfur Lyases; Cell Line; Fluoresceins; Fluorescence Resonance Energy Transfer; Iron; Iron-Sulfur Proteins; Models, Molecular; Mutation; Naphthalenesulfonates; Protein Binding; Protein Conformation; Protein Stability; Staining and Labeling; Substrate Specificity; Sulfides; Sulfur; Thermotoga maritima | 2009 |
Differences in structural dynamics of muscle and yeast actin accompany differences in functional interactions with myosin.
Topics: Actins; Animals; Calcium; Energy Transfer; Enzyme Activation; Erythrosine; Fluorescent Dyes; Magnesium; Muscle, Skeletal; Myosins; Naphthalenesulfonates; Rabbits; Structure-Activity Relationship; Yeasts | 1999 |