urea has been researched along with i(3)so3-galactosylceramide in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (75.00) | 18.7374 |
| 1990's | 1 (25.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Joffe, S | 1 |
| Meeroff, JC | 1 |
| Buckelew, AR; Colacicco, G | 1 |
| Borgia, S; Hoffman, P; Huesca, M; Lingwood, CA | 1 |
1 review(s) available for urea and i(3)so3-galactosylceramide
| Article | Year |
|---|---|
[Chemical composition of gastric juice].
Topics: Animals; Bicarbonates; Blood Group Antigens; Blood Proteins; Calcium; Cats; Chlorides; Dogs; Gastric Juice; Gastric Mucosa; Gastrointestinal Hormones; Humans; Hydrogen-Ion Concentration; Lipase; Magnesium; Mucoproteins; Pepsin A; Peptide Hydrolases; Phosphates; Potassium; Rats; Sodium; Sulfoglycosphingolipids; Urea; Uric Acid; Water | 1972 |
3 other study(ies) available for urea and i(3)so3-galactosylceramide
| Article | Year |
|---|---|
Isolation of some properties of a succinylated protein-lipid complex derived from calf brain myelin.
Topics: Acylation; Animals; Brain Chemistry; Cattle; Centrifugation, Density Gradient; Cerebrosides; Cholesterol; Chromatography, Gel; Chromatography, Thin Layer; Circular Dichroism; Electrophoresis, Disc; Galactose; Lipids; Lipoproteins; Myelin Sheath; Phosphatidylethanolamines; Phosphatidylinositols; Phospholipids; Sphingomyelins; Succinates; Sulfoglycosphingolipids; Ultracentrifugation; Urea | 1971 |
Lipid monolayers: influence of lipid film and urea on the surface activity of staphylococcal alpha-toxin.
Topics: Adsorption; Bacterial Proteins; Buffers; Chemical Phenomena; Chemistry; Cholesterol; Gangliosides; Lipids; Membranes, Artificial; Muramidase; Phosphates; Phosphatidylcholines; Protein Denaturation; Ribonucleases; Staphylococcus; Streptolysins; Sulfoglycosphingolipids; Surface Properties; Surface Tension; Toxins, Biological; Urea | 1971 |
Acidic pH changes receptor binding specificity of Helicobacter pylori: a binary adhesion model in which surface heat shock (stress) proteins mediate sulfatide recognition in gastric colonization.
Topics: Adhesins, Bacterial; Antibodies, Blocking; Bacterial Adhesion; Bacterial Proteins; Binding Sites; Gastritis; Glycolipids; Heat-Shock Proteins; Helicobacter Infections; Helicobacter pylori; Humans; Hydrogen-Ion Concentration; In Vitro Techniques; Membrane Proteins; Models, Biological; Peptic Ulcer; Protein Synthesis Inhibitors; Stomach; Sulfoglycosphingolipids; Urea | 1996 |