n-(2-(1-maleimidyl)ethyl)-7-(diethylamino)coumarin-3-carboxamide has been researched along with cysteine in 3 studies
Studies (n-(2-(1-maleimidyl)ethyl)-7-(diethylamino)coumarin-3-carboxamide) | Trials (n-(2-(1-maleimidyl)ethyl)-7-(diethylamino)coumarin-3-carboxamide) | Recent Studies (post-2010) (n-(2-(1-maleimidyl)ethyl)-7-(diethylamino)coumarin-3-carboxamide) | Studies (cysteine) | Trials (cysteine) | Recent Studies (post-2010) (cysteine) |
---|---|---|---|---|---|
24 | 0 | 7 | 40,132 | 418 | 11,457 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (33.33) | 18.2507 |
2000's | 2 (66.67) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
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Brune, M; Corrie, JE; Haire, LL; Henrick, K; Hirshberg, M; Vasisht, N; Webb, MR | 1 |
Brune, M; Corrie, JE; Webb, MR | 1 |
Daunert, S; Deo, SK; Salins, LL | 1 |
3 other study(ies) available for n-(2-(1-maleimidyl)ethyl)-7-(diethylamino)coumarin-3-carboxamide and cysteine
Article | Year |
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Crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate.
Topics: Alanine; Amino Acid Substitution; Carrier Proteins; Computer Simulation; Coumarins; Crystallization; Crystallography, X-Ray; Cysteine; Escherichia coli; Fluorescent Dyes; Models, Molecular; Mutagenesis, Site-Directed; Phosphate-Binding Proteins; Phosphates; Stereoisomerism | 1998 |
A fluorescent sensor of the phosphorylation state of nucleoside diphosphate kinase and its use to monitor nucleoside diphosphate concentrations in real time.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Aspartic Acid; Binding Sites; Coumarins; Cysteine; Fluorescent Dyes; Guanosine Diphosphate; Humans; Kinetics; Mass Spectrometry; Mutagenesis, Site-Directed; Myosin Subfragments; Myxococcus xanthus; Nucleoside-Diphosphate Kinase; Phosphorylation; Purine Nucleotides; Rabbits; rho GTP-Binding Proteins; Solutions; Spectrometry, Fluorescence | 2001 |
Phosphate binding protein as the biorecognition element in a biosensor for phosphate.
Topics: Amino Acid Substitution; Bacterial Proteins; Biosensing Techniques; Coumarins; Cysteine; Environmental Monitoring; Escherichia coli; Fiber Optic Technology; Fluorescence; Ligands; Mutagenesis, Site-Directed; Mutation; Optical Fibers; Phosphate-Binding Proteins; Phosphates; Plasmids; Protein Conformation | 2004 |