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glycidyl nitrate and formaldehyde

glycidyl nitrate has been researched along with formaldehyde in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19902 (40.00)18.7374
1990's2 (40.00)18.2507
2000's1 (20.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Braun, V; Hantke, K1
Konvicková-Lamosová, M; Reich, J; Soska, J1
Bénédetti, H; Bouveret, E; Derouiche, R; Lazdunski, C; Lloubès, R; Rigal, A1
Bénédetti, H; Bouveret, E; Lazdunski, C; Rigal, A1
Corda, Y; Lazdunski, C; Walburger, A1

Other Studies

5 other study(ies) available for glycidyl nitrate and formaldehyde

ArticleYear
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.
    European journal of biochemistry, 1973, Volume: 34, Issue:2

    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).
    Folia biologica, 1972, Volume: 18, Issue:5

    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.
    The Journal of biological chemistry, 1995, May-12, Volume: 270, Issue:19

    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.
    Molecular microbiology, 1997, Volume: 23, Issue:5

    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.
    Molecular microbiology, 2002, Volume: 44, Issue:3

    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