3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate has been researched along with Alzheimer Disease in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (33.33) | 18.2507 |
| 2000's | 2 (66.67) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Beyreuther, K; Czech, C; De Strooper, B; Dotti, CG; Hartmann, T; Ida, N; Ikonen, E; Masters, CL; Multhaup, G; Simons, M; Tienari, PJ; Van Leuven, F; Weidemann, A | 1 |
| DiMuzio-Mower, J; Gardell, SJ; Huang, Q; Lai, MT; Li, YM; Sardana, MK; Shafer, JA; Shi, XP; Xu, M; Yin, KC | 1 |
| Selkoe, DJ; Wolfe, MS | 1 |
3 other study(ies) available for 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate and Alzheimer Disease
| Article | Year |
|---|---|
The beta-amyloid domain is essential for axonal sorting of amyloid precursor protein.
Topics: Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Protein Precursor; Amyloidosis; Animals; Axonal Transport; Axons; Cell Membrane; Cell Polarity; Cells, Cultured; Cholic Acids; Detergents; Epitopes; Glycosylation; Hemagglutinins, Viral; Hippocampus; Humans; Molecular Sequence Data; Neurons; Proto-Oncogene Proteins c-myc; Rats; Recombinant Fusion Proteins; Semliki forest virus; Sequence Deletion; Solubility; Tunicamycin | 1996 |
Presenilin 1 is linked with gamma-secretase activity in the detergent solubilized state.
Topics: Alzheimer Disease; Amyloid beta-Protein Precursor; Amyloid Precursor Protein Secretases; Aspartic Acid Endopeptidases; Carbamates; Cell Fractionation; Cell Membrane; Cholic Acids; Detergents; Dipeptides; Endopeptidases; HeLa Cells; Humans; Membrane Proteins; Neoplasm Proteins; Pepstatins; Presenilin-1; Protease Inhibitors; Recombinant Fusion Proteins; Solubility; Substrate Specificity | 2000 |
In search of gamma-secretase: presenilin at the cutting edge.
Topics: Alzheimer Disease; Amyloid beta-Protein Precursor; Amyloid Precursor Protein Secretases; Aspartic Acid Endopeptidases; Binding Sites; Cholic Acids; Detergents; Dimerization; Endopeptidases; Endoribonucleases; HeLa Cells; Humans; Macromolecular Substances; Membrane Proteins; Models, Biological; Nerve Tissue Proteins; Presenilin-1; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Receptors, Notch; Substrate Specificity | 2000 |