cyanogen bromide has been researched along with 1,7-phenanthroline in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (40.00) | 18.7374 |
1990's | 1 (20.00) | 18.2507 |
2000's | 2 (40.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Appel, M; Klingenberg, M | 1 |
Joshi, S; Torok, K | 1 |
Bisaccia, F; Capobianco, L; Iacobazzi, V; Mazzeo, M; Palmieri, F; Zara, V | 1 |
Crouch, RK; Gelasco, A; Knapp, DR | 1 |
Fujimura, Y; Hamako, J; Hashimoto, K; Ito, M; Matsui, T; Matsumoto, M; Sakurai, Y; Suzuki, M; Titani, K | 1 |
5 other study(ies) available for cyanogen bromide and 1,7-phenanthroline
Article | Year |
---|---|
The uncoupling protein dimer can form a disulfide cross-link between the mobile C-terminal SH groups.
Topics: Animals; Binding Sites; Biological Transport; Carrier Proteins; Cricetinae; Cross-Linking Reagents; Cyanogen Bromide; Cysteine; Dipeptides; Disulfides; GTP-Binding Proteins; Guanosine Triphosphate; Ion Channels; Kinetics; Liposomes; Membrane Proteins; Mitochondrial Proteins; Oxidation-Reduction; Phenanthrolines; Trypsin; Uncoupling Agents; Uncoupling Protein 1 | 1989 |
Formation of an intramolecular disulfide bond in the mitochondrial adenine nucleotide translocase.
Topics: Animals; Cattle; Chemical Phenomena; Chemistry; Cyanogen Bromide; Cysteine; Disulfides; Mitochondria, Heart; Mitochondrial ADP, ATP Translocases; Nucleotidyltransferases; Peptide Fragments; Phenanthrolines; Proton-Translocating ATPases | 1985 |
The formation of a disulfide cross-link between the two subunits demonstrates the dimeric structure of the mitochondrial oxoglutarate carrier.
Topics: 1-Propanol; Acetone; Animals; Carrier Proteins; Cattle; Cross-Linking Reagents; Cyanogen Bromide; Diamide; Disulfides; Dithioerythritol; Electrophoresis, Polyacrylamide Gel; Ketoglutaric Acids; Kinetics; Liposomes; Macromolecular Substances; Membrane Transport Proteins; Mitochondria, Heart; Phenanthrolines; Proteolipids; Sulfhydryl Reagents | 1996 |
Intrahelical arrangement in the integral membrane protein rhodopsin investigated by site-specific chemical cleavage and mass spectrometry.
Topics: Amino Acid Sequence; Ascorbic Acid; Copper; Cyanogen Bromide; Cysteine; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Organometallic Compounds; Oxygen; Peptide Fragments; Phenanthrolines; Protein Structure, Secondary; Rhodopsin; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 2000 |
Complete amino acid sequence of kaouthiagin, a novel cobra venom metalloproteinase with two disintegrin-like sequences.
Topics: Amino Acid Motifs; Amino Acid Sequence; Animals; Binding Sites; Cyanogen Bromide; Disintegrins; Elapid Venoms; Enzyme Activation; Glycosylation; Humans; Hydrolysis; Metalloendopeptidases; Molecular Sequence Data; Peptide Fragments; Phenanthrolines; Platelet Aggregation; Protease Inhibitors; Protein Binding; Protein Structure, Tertiary; Repetitive Sequences, Amino Acid; von Willebrand Factor; Zinc | 2001 |