3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate and Amyloidosis

3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate has been researched along with Amyloidosis in 1 studies

Research

Studies (1)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (100.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

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

Other Studies

1 other study(ies) available for 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate and Amyloidosis

Article	Year
The beta-amyloid domain is essential for axonal sorting of amyloid precursor protein. The EMBO journal, 1996, Oct-01, Volume: 15, Issue:19 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

Article

Year

The beta-amyloid domain is essential for axonal sorting of amyloid precursor protein.

The EMBO journal, 1996, Oct-01, Volume: 15, Issue:19

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