glycidyl nitrate has been researched along with formaldehyde in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (40.00) | 18.7374 |
1990's | 2 (40.00) | 18.2507 |
2000's | 1 (20.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Braun, V; Hantke, K | 1 |
Konvicková-Lamosová, M; Reich, J; Soska, J | 1 |
Bénédetti, H; Bouveret, E; Derouiche, R; Lazdunski, C; Lloubès, R; Rigal, A | 1 |
Bénédetti, H; Bouveret, E; Lazdunski, C; Rigal, A | 1 |
Corda, Y; Lazdunski, C; Walburger, A | 1 |
5 other study(ies) available for glycidyl nitrate and formaldehyde
Article | Year |
---|---|
Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the murein-lipoprotein of the Escherichia coli outer membrane.
Topics: Amides; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Carbon Isotopes; Chromatography, Thin Layer; Cysteine; Escherichia coli; Fatty Acids; Formaldehyde; Glycerides; Lipoproteins; Mass Spectrometry; Membranes; Palmitic Acids; Peptidoglycan; Sulfur Isotopes; Tritium | 1973 |
Autolysis of cells of Lactobacillus acidophilus induced by chloroform (effect of growth phase-murein).
Topics: Amino Acids; Bacteriolysis; Carbon Isotopes; Chloroform; Chromatography, Paper; Formaldehyde; Hydrogen-Ion Concentration; Iodine; Lactobacillus acidophilus; Oxidation-Reduction; Peptidoglycan; Temperature; Thymine; Tritium; Uracil | 1972 |
Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli.
Topics: Bacterial Outer Membrane Proteins; Bacterial Proteins; Cell Membrane; Cross-Linking Reagents; Escherichia coli; Escherichia coli Proteins; Formaldehyde; Genotype; Immunoblotting; Lipoproteins; Membrane Fusion; Membrane Proteins; Methionine; Molecular Weight; Peptidoglycan; Periplasmic Proteins; Phenotype; Plasmids; Proteoglycans; Sulfur Radioisotopes | 1995 |
The N-terminal domain of colicin E3 interacts with TolB which is involved in the colicin translocation step.
Topics: Alkaline Phosphatase; Antibodies, Bacterial; Bacterial Outer Membrane Proteins; Bacterial Proteins; beta-Lactamases; Blotting, Western; Cell Membrane; Colicins; Cytoplasm; Deoxycholic Acid; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Formaldehyde; Gene Expression Regulation, Bacterial; Lipoproteins; Microscopy, Electron; Peptides; Peptidoglycan; Periplasmic Proteins; Plasmids; Point Mutation; Precipitin Tests; Proteoglycans; Recombination, Genetic; Ribonucleases; Sodium Dodecyl Sulfate; Translocation, Genetic | 1997 |
The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB.
Topics: Bacterial Outer Membrane Proteins; Bacterial Proteins; Biological Transport; Cell Membrane; Colicins; Cross-Linking Reagents; Escherichia coli; Escherichia coli Proteins; Formaldehyde; Lipoproteins; Macromolecular Substances; Membrane Proteins; Mutagenesis; Peptidoglycan; Polymerase Chain Reaction; Protein Interaction Mapping; Protein Structure, Tertiary; Proteoglycans; Recombinant Fusion Proteins; Serine Endopeptidases; Sodium Dodecyl Sulfate; Two-Hybrid System Techniques | 2002 |