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

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

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (66.67)18.2507
2000's1 (33.33)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Corbin, J; Imagawa, T; Kaya, S; Kikkawa, U; Mårdh, S; Mori, M; Shimada, A; Taniguchi, K; Togawa, K1
Imagawa, T; Kanagawa, M; Kaya, S; Mårdh, S; Shimada, A; Taniguchi, K; Togawa, K; Umezu, H; Watanabe, S1
Casas, E; Francis, SA; Lynch, RD; McCarthy, KM; Schneeberger, EE; Thiele, C1

Other Studies

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

ArticleYear
Phosphorylation of Tyr7, Tyr10, and Ser27 of alpha-chain in H+,K(+)-ATPase by intrinsic and extrinsic kinases.
    Annals of the New York Academy of Sciences, 1997, Nov-03, Volume: 834

    Topics: Animals; Cholic Acids; Detergents; Gastric Mucosa; H(+)-K(+)-Exchanging ATPase; Kinetics; Macromolecular Substances; Phosphorylation; Phosphoserine; Phosphotyrosine; Protein Kinases; Serine; Swine; Tyrosine

1997
Direct evidence for in vivo reversible tyrosine phosphorylation of the N-terminal domain of the H/K-ATPase alpha-subunit in mammalian stomach cells.
    Journal of biochemistry, 1999, Volume: 126, Issue:2

    Topics: Animals; Cholic Acids; Culture Techniques; Detergents; H(+)-K(+)-Exchanging ATPase; Male; Phosphorylation; Phosphotyrosine; Protein-Tyrosine Kinases; Rabbits; Rats; Rats, Wistar; Recombinant Fusion Proteins; Stomach; Swine

1999
Cholesterol depletion alters detergent-specific solubility profiles of selected tight junction proteins and the phosphorylation of occludin.
    Experimental cell research, 2007, Jul-15, Volume: 313, Issue:12

    Topics: Animals; Cell Membrane; Cells, Cultured; Centrifugation; Cholesterol; Cholic Acids; Claudin-1; Detergents; Dogs; Electric Impedance; Epithelial Cells; Membrane Proteins; Occludin; Octoxynol; Palmitic Acid; Phosphorylation; Phosphothreonine; Phosphotyrosine; Solubility; Tight Junctions; Ultraviolet Rays

2007