dicyclohexylcarbodiimide has been researched along with serine in 6 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 4 (66.67) | 18.7374 |
1990's | 1 (16.67) | 18.2507 |
2000's | 1 (16.67) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Fillingame, RH; Fraga, D; Oldenburg, M | 1 |
Cox, GB; Gibson, F; Howitt, SM | 1 |
Asghar, SS; Harold, FM; Levin, E | 1 |
Polgár, L | 1 |
Fridkin, M; Goren, HJ | 1 |
Ahmad, Z; Brudecki, LE; Li, W; Senior, AE | 1 |
6 other study(ies) available for dicyclohexylcarbodiimide and serine
Article | Year |
---|---|
Mutation of alanine 24 to serine in subunit c of the Escherichia coli F1F0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide.
Topics: Alanine; Amino Acid Sequence; Base Sequence; Dicyclohexylcarbodiimide; DNA Mutational Analysis; DNA, Bacterial; Drug Resistance, Microbial; Escherichia coli; Genetic Complementation Test; Genetic Vectors; Molecular Sequence Data; Proton-Translocating ATPases; Sequence Alignment; Serine; Structure-Activity Relationship; Venturicidins | 1991 |
The proton pore of the F0F1-ATPase of Escherichia coli: Ser-206 is not required for proton translocation.
Topics: Alanine; Amino Acid Sequence; Asparagine; Base Sequence; Dicyclohexylcarbodiimide; DNA Restriction Enzymes; DNA, Bacterial; Escherichia coli; Fluorescence; Glutamine; Ion Channels; Oxidative Phosphorylation; Proton-Translocating ATPases; Protons; Quinacrine; Serine | 1988 |
Accumulation of neutral amino acids by Streptococcus faecalis. Energy coupling by a proton-motive force.
Topics: Alanine; Amino Acids; Anti-Bacterial Agents; Biological Transport, Active; Carbon Radioisotopes; Carboxylic Acids; Cycloserine; Dicyclohexylcarbodiimide; Energy Metabolism; Enterococcus faecalis; Glycine; Glycolysis; Hydrogen-Ion Concentration; Kinetics; Membrane Potentials; Models, Biological; Mutation; Polycyclic Compounds; Potassium; Serine; Sodium; Threonine; Time Factors; Valinomycin | 1973 |
Symmetry and asymmetry in the mechanisms of hydrolysis by serine proteases and their thiol analogues.
Topics: Binding Sites; Chymotrypsin; Cinnamates; Dicyclohexylcarbodiimide; Endopeptidases; Esters; Hydrogen-Ion Concentration; Kinetics; Mercuribenzoates; Nitrophenols; Protein Binding; Serine; Structure-Activity Relationship; Subtilisins; Sulfhydryl Compounds | 1972 |
Synthesis and catalytic properties of the heptapeptide L-seryl-L-prolyl-L-cysteinyl-L-steryl-alpha-L-glutamyl-L-threonyl-L-tyrosine.
Topics: Acetates; Carboxypeptidases; Chromatography, Gel; Chromatography, Thin Layer; Cysteine; Dicyclohexylcarbodiimide; Esters; Glutamates; Hydrogen-Ion Concentration; Kinetics; Mathematics; Nitrophenols; Oligopeptides; Optical Rotation; Proline; Serine; Spectrophotometry; Spectrophotometry, Ultraviolet; Sulfhydryl Compounds; Threonine; Tyrosine | 1974 |
Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.
Topics: 4-Chloro-7-nitrobenzofurazan; Amino Acid Sequence; Animals; ATP Synthetase Complexes; Base Sequence; Catalytic Domain; Dicyclohexylcarbodiimide; Dithiothreitol; Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Glycine; Humans; Molecular Conformation; Molecular Sequence Data; Mutation; Protein Subunits; Sequence Alignment; Serine | 2009 |