n-(4-(7-(diethylamino)-4-methylcoumarin-3-yl))maleimide has been researched along with cysteine in 4 studies
Studies (n-(4-(7-(diethylamino)-4-methylcoumarin-3-yl))maleimide) | Trials (n-(4-(7-(diethylamino)-4-methylcoumarin-3-yl))maleimide) | Recent Studies (post-2010) (n-(4-(7-(diethylamino)-4-methylcoumarin-3-yl))maleimide) | Studies (cysteine) | Trials (cysteine) | Recent Studies (post-2010) (cysteine) |
---|---|---|---|---|---|
9 | 0 | 1 | 40,132 | 418 | 11,457 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 4 (100.00) | 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 |
---|---|
Aggeler, R; Capaldi, RA | 1 |
Colvert, KK; Mills, DA; Richter, ML | 1 |
Capaldi, RA; Turina, P | 2 |
4 other study(ies) available for n-(4-(7-(diethylamino)-4-methylcoumarin-3-yl))maleimide and cysteine
Article | Year |
---|---|
Cross-linking of the gamma subunit of the Escherichia coli ATPase (ECF1) via cysteines introduced by site-directed mutagenesis.
Topics: Adenosine Triphosphatases; Base Sequence; Blotting, Western; Coumarins; Cross-Linking Reagents; Cysteine; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Fluorescent Dyes; Maleimides; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Plasmids | 1992 |
Structural mapping of cysteine-63 of the chloroplast ATP synthase beta subunit.
Topics: Amino Acid Sequence; Binding Sites; Chloroplasts; Coumarins; Cysteine; Energy Transfer; Fluorescein; Fluoresceins; Fluorescence Polarization; Fluorescent Dyes; Kinetics; Maleimides; Molecular Sequence Data; Plants; Protein Conformation; Proton-Translocating ATPases; Spectrometry, Fluorescence | 1992 |
ATP binding causes a conformational change in the gamma subunit of the Escherichia coli F1ATPase which is reversed on bond cleavage.
Topics: Adenosine Triphosphate; Adenylyl Imidodiphosphate; Binding Sites; Coumarins; Cysteine; Escherichia coli; Fluorescent Dyes; Hydrolysis; Kinetics; Maleimides; Mutagenesis, Site-Directed; Protein Conformation; Proton-Translocating ATPases; Spectrometry, Fluorescence | 1994 |
ATP hydrolysis-driven structural changes in the gamma-subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues.
Topics: Adenosine Triphosphate; Coumarins; Cysteine; Escherichia coli; Fluorescence Polarization; Fluorescent Dyes; Hydrolysis; Kinetics; Maleimides; Mutation; Nucleotides; Protein Conformation; Proton-Translocating ATPases | 1994 |