dicyclohexylcarbodiimide has been researched along with tryptophan in 4 studies
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 |
---|---|
Grell, E; Senior, AE; Weber, J; Wilke-Mounts, S | 1 |
Peerce, BE | 1 |
Senior, AE; Weber, J | 1 |
Josse, D; Lockridge, O; Masson, P; Renault, F; Rochu, D; Schopfer, LM; Xie, W | 1 |
4 other study(ies) available for dicyclohexylcarbodiimide and tryptophan
Article | Year |
---|---|
Tryptophan-free Escherichia coli F1-ATPase.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Aurovertins; Azides; Base Sequence; Dicyclohexylcarbodiimide; Escherichia coli; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oxidative Phosphorylation; Proton-Translocating ATPases; Spectrometry, Fluorescence; Tryptophan | 1994 |
Molecular mechanism of two noncompetitive inhibitors of Na(+)-glucose cotransporter: comparison of DCCD and PCMB.
Topics: Chloromercuribenzoates; Dicyclohexylcarbodiimide; Fluorescein-5-isothiocyanate; Fluorescence; Molecular Conformation; Monosaccharide Transport Proteins; p-Chloromercuribenzoic Acid; Sodium; Tryptophan | 1993 |
Effects of the inhibitors azide, dicyclohexylcarbodiimide, and aurovertin on nucleotide binding to the three F1-ATPase catalytic sites measured using specific tryptophan probes.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Aurovertins; Catalytic Domain; Dicyclohexylcarbodiimide; Enzyme Inhibitors; Molecular Probes; Protein Binding; Proton-Translocating ATPases; Sodium Azide; Spectrometry, Fluorescence; Tryptophan | 1998 |
Identification of residues essential for human paraoxonase (PON1) arylesterase/organophosphatase activities.
Topics: Amino Acids; Animals; Aryldialkylphosphatase; Aspartic Acid; Binding Sites; Bromosuccinimide; Calcium Radioisotopes; Cell Line; Dicyclohexylcarbodiimide; Diethyl Pyrocarbonate; Enzyme Activation; Enzyme Inhibitors; Esterases; Glutamic Acid; Glycosylation; Histidine; Humans; Indicators and Reagents; Kidney; Kinetics; Mutagenesis, Site-Directed; Protein Conformation; Rabbits; Recombinant Proteins; Spectrometry, Fluorescence; Terbium; Tryptophan | 1999 |