ethyldimethylaminopropyl carbodiimide has been researched along with adenosine diphosphate in 9 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (22.22) | 18.7374 |
1990's | 1 (11.11) | 18.2507 |
2000's | 6 (66.67) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Capaldi, RA; Mendel-Hartvig, J | 1 |
Greene, LE; King, RT | 1 |
Arata, T | 1 |
Fujisawa, T; Iwamoto, H; Oiwa, K; Suzuki, T | 1 |
Karczewska, E; Pliszka, B | 1 |
Barman, T; Belus, A; Candau, R; Iorga, B; Lionne, C; Piroddi, N; Travers, F; Webb, MR | 1 |
Chiu, HJ; Einsle, O; Howard, JB; Rees, DC; Schmid, B; Willing, A; Yoshida, M | 1 |
Ballweber, E; Kiessling, P; Mannherz, HG; Manstein, D | 1 |
Karczewska, E; Martin, BM; Pliszka, B | 1 |
9 other study(ies) available for ethyldimethylaminopropyl carbodiimide and adenosine diphosphate
Article | Year |
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Nucleotide-dependent and dicyclohexylcarbodiimide-sensitive conformational changes in the epsilon subunit of Escherichia coli ATP synthase.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Dicyclohexylcarbodiimide; Egtazic Acid; Escherichia coli; Ethyldimethylaminopropyl Carbodiimide; Kinetics; Macromolecular Substances; Proton-Translocating ATPases; Trypsin | 1991 |
The conformation of cross-linked actin.S-1 in the presence and absence of ATP.
Topics: Actins; Adenosine Diphosphate; Adenosine Triphosphate; Animals; Ethyldimethylaminopropyl Carbodiimide; Ethylmaleimide; Maleimides; Microscopy, Electron; Peptide Fragments; Protein Conformation; Rabbits | 1987 |
Chemical crosslinking of myosin subfragment-1 to F-actin in the presence of nucleotide.
Topics: Actins; Adenine Nucleotides; Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Animals; Ca(2+) Mg(2+)-ATPase; Carbodiimides; Ethyldimethylaminopropyl Carbodiimide; Kinetics; Muscles; Myosin Subfragments; Myosins; Osmolar Concentration; Peptide Fragments; Potassium Chloride; Rabbits | 1984 |
X-ray diffraction evidence for the lack of stereospecific protein interactions in highly activated actomyosin complex.
Topics: Actins; Actomyosin; Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Calcium; Cross-Linking Reagents; Enzyme Activation; Ethyldimethylaminopropyl Carbodiimide; Kinetics; Models, Molecular; Muscle Fibers, Skeletal; Muscle, Skeletal; Myosin Subfragments; Phosphates; Protein Binding; Protein Structure, Quaternary; Rabbits; Stereoisomerism; Substrate Specificity; X-Ray Diffraction | 2001 |
Changes at the interface of the N- and C-terminal parts of the heavy chain of myosin subfragment 1.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Animals; Electrophoresis, Polyacrylamide Gel; Ethyldimethylaminopropyl Carbodiimide; Myosin Heavy Chains; Myosin Subfragments; Rabbits; Trypsin | 2002 |
Evidence that phosphate release is the rate-limiting step on the overall ATPase of psoas myofibrils prevented from shortening by chemical cross-linking.
Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Calibration; Cross-Linking Reagents; Ethyldimethylaminopropyl Carbodiimide; Isometric Contraction; Kinetics; Models, Biological; Myofibrils; Phosphates; Psoas Muscles; Rabbits; Spectrometry, Fluorescence; Temperature; Time Factors | 2002 |
Biochemical and structural characterization of the cross-linked complex of nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure.
Topics: Adenosine Diphosphate; Aluminum Compounds; Azotobacter vinelandii; Cross-Linking Reagents; Crystallography, X-Ray; Enzyme Stability; Ethyldimethylaminopropyl Carbodiimide; Fluorides; Glycine; Molybdoferredoxin; Multienzyme Complexes; Nitrogenase; Nonheme Iron Proteins; Protein Binding; Static Electricity | 2002 |
Interaction of myosin subfragment 1 with forms of monomeric actin.
Topics: Actins; Adenosine Diphosphate; Adsorption; Animals; Binding, Competitive; Cattle; Chromatography, Affinity; Cross-Linking Reagents; Deoxyribonuclease I; Dictyostelium; Enzymes, Immobilized; Ethyldimethylaminopropyl Carbodiimide; Hydrolysis; Magnesium; Myosin Subfragments; ortho-Aminobenzoates; Osmolar Concentration; Protozoan Proteins; Pyrenes; Rabbits; Spectrometry, Fluorescence; Titrimetry; Trypsin; Vitamin D-Binding Protein | 2003 |
Effect of nucleotide on interaction of the 567-578 segment of myosin heavy chain with actin.
Topics: Actins; Adenosine Diphosphate; Amino Acid Sequence; Animals; Cross-Linking Reagents; Ethyldimethylaminopropyl Carbodiimide; Myosin Heavy Chains; Myosin Subfragments; Peptide Fragments; Protein Interaction Mapping; Rabbits; Single-Strand Specific DNA and RNA Endonucleases | 2006 |