5-((2-aminoethyl)amino)naphthalene-1-sulfonic acid has been researched along with cysteine in 3 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (33.33) | 18.2507 |
2000's | 1 (33.33) | 29.6817 |
2010's | 1 (33.33) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Kanazawa, T; Nakamura, S; Suzuki, H | 1 |
Cui, Y; Fan, Z; Wang, W | 1 |
Miller, C; Nathanson, JT; Stockbridge, RB; Street, TO; Turman, DL | 1 |
3 other study(ies) available for 5-((2-aminoethyl)amino)naphthalene-1-sulfonic acid and cysteine
Article | Year |
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Effects of divalent cations bound to the catalytic site on ATP-induced conformational changes in the sarcoplasmic reticulum Ca(2+)-ATPase: stopped-flow analysis of the fluorescence of N-acetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine attached to cysteine-67
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Binding Sites; Calcium-Transporting ATPases; Catalysis; Cations, Divalent; Cysteine; Ethylmaleimide; Fluorescent Dyes; Kinetics; Muscles; Naphthalenesulfonates; Protein Conformation; Rabbits; Sarcoplasmic Reticulum; Spectrometry, Fluorescence | 1994 |
Cytoplasmic vestibule of the weak inward rectifier Kir6.2 potassium channel.
Topics: Adenosine Triphosphate; Animals; Cells, Cultured; COS Cells; Cysteine; Cytoplasm; DNA, Complementary; Dose-Response Relationship, Drug; Ethyl Methanesulfonate; Immunohistochemistry; Isoleucine; Mesylates; Models, Biological; Models, Chemical; Mutagenesis, Site-Directed; Naphthalenesulfonates; Patch-Clamp Techniques; Potassium; Potassium Channels, Inwardly Rectifying; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Recombinant Fusion Proteins; Serine; Spermine; Sulfhydryl Reagents; Transfection | 2002 |
Two-sided block of a dual-topology F- channel.
Topics: Anisotropy; Antibodies, Monoclonal; Bacterial Proteins; Binding Sites; Cysteine; Dose-Response Relationship, Drug; Epitopes; Fluorescence Polarization; Fluorine; Ion Channels; Kinetics; Lipid Bilayers; Microscopy, Fluorescence; Models, Theoretical; Mutation; Naphthalenesulfonates; Protein Binding; Static Electricity | 2015 |