Katrin Ingold
University of Bern
10 Papers
92 Citations
Katrin Ingold is an academic researcher from University of Bern. The author has contributed to research in topics: Echinococcus multilocularis & Metacestode. The author has an hindex of 7, co-authored 9 publications.
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Papers
Efficacies of Albendazole Sulfoxide and Albendazole Sulfone against In Vitro-Cultivated Echinococcus multilocularis Metacestodes
Katrin Ingold,Peter Bigler,Wolfgang Thormann,Tania Cavaliero,Bruno Gottstein,Andrew Hemphill +5 more
TL;DR: The in vitro cultivation model presented here provides an ideal first-round test system for screening of antiparasite drugs and Transmission electron microscopic investigation of parasite tissues and nuclear magnetic resonance spectroscopy of vesicle fluids demonstrated that albendazole sulfoxide and albendsole sulfone had similar effects with respect to parasite ultrastructure and changes in metabolites in vesicles fluids.
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Detection of surface-associated and intracellular glycoconjugates and glycoproteins in Neospora caninum tachyzoites.
TL;DR: Data is presented which strongly suggest that the surface of N. caninum tachyzoites is glycosylated, and glycoproteins reacted specifically with the lectins Con A, wheat germ agglutinin, Jacalin and soy bean agglUTinin.
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An outbreak of hepatitis A virus infection in a secondary school in England with no undetected asymptomatic transmission among students
Adrian Wensley,Elizabeth Smout,Siew Lin Ngui,Koye Balogun,Paula Blomquist,Michael Edelstein,R. Greenwood,S Coles,Katrin Ingold,L. R. Sargeant,M Gent,Simon Padfield,Gareth Hughes +12 more
TL;DR: In this article , the Health Protection Team in Yorkshire and Humber, England, was notified of cases of hepatitis A virus (HAV) infection in staff at a secondary school.
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Conservation of calnexin in the early branching protozoan Tritrichomonas suis.
TL;DR: Demonstration of a structurally conserved calnexin in the amitochondriate protist T. suis indicates the very early evolutionary origin of the machinery for quality control of protein folding in the endoplasmic reticulum and the molecules involved hereby.
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