Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Susan Wimer-Mackin"'
Publikováno v:
Infection and Immunity. 68:6487-6492
Culture supernatants prepared from reactogenic strains of Vibrio cholerae cause a decrease in the transcellular epithelial resistance of T84 intestinal cells. This decrease correlates with the presence of hemagglutinin/protease but not with the prese
Publikováno v:
Infection and Immunity. 68:6487-6492
Publikováno v:
Infection and Immunity. 67:3026-3030
We examined the entry of anthrax edema toxin (EdTx) into polarized human T84 epithelial cells using cyclic AMP-regulated Cl − secretion as an index of toxin entry. EdTx is a binary A/B toxin which self assembles at the cell surface from anthrax ede
Autor:
Margaret Ferguson-Maltzman, Michael G. Jobling, Wayne I. Lencer, J. L. Madara, Susan Wimer-Mackin, Anne A. Wolf, Randall K. Holmes
Publikováno v:
The Journal of Cell Biology
In polarized cells, signal transduction by cholera toxin (CT) requires apical endocytosis and retrograde transport into Golgi cisternae and perhaps ER (Lencer, W.I., C. Constable, S. Moe, M. Jobling, H.M. Webb, S. Ruston, J.L. Madara, T. Hirst, and R
Autor:
Bruce L. Granger, Susan Wimer-Mackin
Publikováno v:
Biochemical and Biophysical Research Communications. 229:472-478
The lgp/LAMP family of mammalian and avian lysosomal type I membrane glycoproteins features short, conserved, cytosolic tails that possess lysosomal targeting information. The sequences of the adjacent transmembrane domains are also highly conserved,
Publikováno v:
Infection and immunity. 69(12)
Escherichia colitype IIa heat-labile enterotoxin (LTIIa) binds in vitro with highest affinity to ganglioside GD1b. It also binds in vitro with lower affinity to several other oligosialogangliosides and to ganglioside GM1, the functional receptor for
Autor:
Heini M. Miettinen, John S. Mills, Michael J. Vlases, Susan Wimer-Mackin, Edward A. Dratz, David R. Barnidge, Jan Sunner, Algirdas J. Jesaitis
Publikováno v:
The Journal of biological chemistry. 273(17)
A novel fluorescent photoaffinity cross-linking probe, formyl-Met-p-benzoyl-L-phenylalanine-Phe-Tyr-Lys-epsilon-N-fluorescei n (fMBpaFYK-fl), was synthesized and used to identify binding site residues in recombinant human phagocyte chemoattractant fo
Publikováno v:
Gastroenterology. 120:A700-A700