octyl glucoside has been researched along with dimyristoylphosphatidylcholine in 6 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (33.33) | 18.7374 |
1990's | 2 (33.33) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 2 (33.33) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Bayerl, TM; Sackmann, E; Werner, GD | 1 |
Horváth, LI; Marsh, D; Ryba, NJ; Watts, A | 1 |
Blume, A; Keller, M; Kerth, A | 1 |
Getmanova, EV; Khorana, HG; Klein-Seetharaman, J; Loewen, MC; Reeves, PJ | 1 |
Ando, T; Angsuthanasombat, C; Aroonkesorn, A; Kanchanawarin, C; Sakdee, S; Sriwimol, W; Uchihashi, T | 1 |
Atkinson, D; Herscovitz, H; Liu, M; Mei, X | 1 |
6 other study(ies) available for octyl glucoside and dimyristoylphosphatidylcholine
Article | Year |
---|---|
Solubilization of DMPC and DPPC vesicles by detergents below their critical micellization concentration: high-sensitivity differential scanning calorimetry, Fourier transform infrared spectroscopy and freeze-fracture electron microscopy reveal two interac
Topics: 1,2-Dipalmitoylphosphatidylcholine; Calorimetry, Differential Scanning; Cholic Acid; Cholic Acids; Deoxycholic Acid; Detergents; Dimyristoylphosphatidylcholine; Fourier Analysis; Freeze Fracturing; Glucosides; Micelles; Microscopy, Electron; Models, Theoretical; Spectrophotometry, Infrared | 1989 |
Molecular exchange at the lipid-rhodopsin interface: spin-label electron spin resonance studies of rhodopsin-dimyristoylphosphatidylcholine recombinants.
Topics: Animals; Cattle; Cyclic N-Oxides; Dimyristoylphosphatidylcholine; Electron Spin Resonance Spectroscopy; Glucosides; Lipid Bilayers; Molecular Conformation; Protein Conformation; Retinal Pigments; Rhodopsin; Rod Cell Outer Segment; Thermodynamics | 1987 |
Thermodynamics of interaction of octyl glucoside with phosphatidylcholine vesicles: partitioning and solubilization as studied by high sensitivity titration calorimetry.
Topics: 1,2-Dipalmitoylphosphatidylcholine; Calorimetry; Dimyristoylphosphatidylcholine; Glucosides; Light; Lipid Bilayers; Liposomes; Micelles; Phosphatidylcholines; Scattering, Radiation; Solubility; Surface-Active Agents; Temperature; Thermodynamics | 1997 |
NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: applicability of solution (19)F NMR.
Topics: Amino Acid Sequence; Animals; Cattle; Cell Line, Transformed; Cysteine; Darkness; Detergents; Dimyristoylphosphatidylcholine; Fluorine Radioisotopes; Glucosides; Light; Memantine; Molecular Sequence Data; Mutagenesis; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Rhodopsin; Solutions | 1999 |
Potential Prepore Trimer Formation by the Bacillus thuringiensis Mosquito-specific Toxin: MOLECULAR INSIGHTS INTO A CRITICAL PREREQUISITE OF MEMBRANE-BOUND MONOMERS.
Topics: Aedes; Animals; Bacillus thuringiensis; Bacillus thuringiensis Toxins; Bacterial Proteins; Bacterial Toxins; Dimyristoylphosphatidylcholine; Endotoxins; Escherichia coli; Gene Expression; Glucosides; Hemolysin Proteins; Insect Proteins; Insecticides; Liposomes; Micelles; Molecular Dynamics Simulation; Pest Control, Biological; Protein Conformation; Protein Multimerization; Receptors, Cell Surface; Recombinant Proteins; Sf9 Cells; Spodoptera; Sulfonic Acids | 2015 |
Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation.
Topics: Amino Acid Sequence; Animals; Apolipoprotein A-I; Cholesterol; Circular Dichroism; Dimyristoylphosphatidylcholine; Glucosides; HEK293 Cells; Humans; Hydrophobic and Hydrophilic Interactions; Lipoproteins, HDL; Mice; Models, Molecular; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Solutions | 2016 |