adenosine diphosphate has been researched along with dodecyldimethylamine oxide in 7 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (42.86) | 18.2507 |
| 2000's | 1 (14.29) | 29.6817 |
| 2010's | 2 (28.57) | 24.3611 |
| 2020's | 1 (14.29) | 2.80 |
| Authors | Studies |
|---|---|
| Allison, WS; Jault, FM; Jault, JM; Kagawa, Y; Kaibara, C; Matsui, T; Muneyuki, E; Yoshida, M | 1 |
| Allison, WS; Dou, C; Honda, M; Matsui, T; Muneyuki, E; Yoshida, M | 1 |
| Allison, WS; Dou, C; Fortes, PA | 1 |
| Allison, WS; Ren, H | 1 |
| Bordignon, E; Goetz, BA; Jeschke, G; Joseph, B; Locher, KP | 1 |
| Milgrom, YM | 1 |
| Duncan, TM; Milgrom, YM | 1 |
7 other study(ies) available for adenosine diphosphate and dodecyldimethylamine oxide
| Article | Year |
|---|---|
The alpha 3 beta 3 gamma complex of the F1-ATPase from thermophilic Bacillus PS3 containing the alpha D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Bacillus; Base Sequence; Binding Sites; Dimethylamines; Enzyme Activation; Hydrolysis; Kinetics; Molecular Sequence Data; Mutation; Protein Conformation; Proton-Translocating ATPases; Rhodamines; Structure-Activity Relationship | 1995 |
Catalytic activity of the alpha3beta3gamma complex of F1-ATPase without noncatalytic nucleotide binding site.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Bacillus; Binding Sites; Dimethylamines; Fluorescent Dyes; Kinetics; Peptide Mapping; Protein Conformation; Proton-Translocating ATPases; Structure-Activity Relationship; Surface-Active Agents | 1997 |
The alpha 3(beta Y341W)3 gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Azides; Bacillus; Binding Sites; Catalysis; Cattle; Cross-Linking Reagents; Detergents; Dimethylamines; Fluorescence Polarization; Hydrolysis; Kinetics; Mutagenesis, Site-Directed; Proton-Translocating ATPases; Spectrometry, Fluorescence; Tryptophan; Tyrosine | 1998 |
Substitution of betaGlu(201) in the alpha(3)beta(3)gamma subcomplex of the F(1)-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Substitution; Animals; Bacillus; Binding Sites; Catalytic Domain; Cattle; Detergents; Dimethylamines; Hydrogen Bonding; Kinetics; Macromolecular Substances; Magnesium; Mutagenesis, Site-Directed; Proton-Translocating ATPases; Recombinant Proteins | 2000 |
Transmembrane gate movements in the type II ATP-binding cassette (ABC) importer BtuCD-F during nucleotide cycle.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; ATP-Binding Cassette Transporters; Cell Membrane; Cysteine; Cytoplasm; Detergents; Dimethylamines; Electron Spin Resonance Spectroscopy; Escherichia coli; Escherichia coli Proteins; Liposomes; Models, Molecular; Movement; Periplasmic Binding Proteins; Protein Conformation; Spin Labels; Vitamin B 12 | 2011 |
Characteristics of protection by MgADP and MgATP of α3β3γ subcomplex of thermophilic Bacillus PS3 βY341W-mutant F1-ATPase from inhibition by 7-chloro-4-nitrobenz-2-oxa-1,3-diazole support a bi-site mechanism of catalysis.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Bacillus; Bacterial Proton-Translocating ATPases; Binding Sites; Catalysis; Catalytic Domain; Dimethylamines; Kinetics; Mutant Proteins; Nitrobenzenes; Oxazoles; Protein Subunits | 2011 |
F-ATP-ase of Escherichia coli membranes: The ubiquitous MgADP-inhibited state and the inhibited state induced by the ε-subunit's C-terminal domain are mutually exclusive.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Cell Membrane; Dimethylamines; Enzyme Activation; Escherichia coli; Hydrolysis; Protein Domains; Protein Subunits; Proton-Translocating ATPases; Selenious Acid; Solubility | 2020 |