Results 181 to 190 of about 8,808 (199)
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Acanthamoeba castellanii: Specificity of immobilization test
Experimental Parasitology, 1969Recognizable changes in the structure of Acanthamoeba castellanii (Neff strain)1 during antiserum immobilization are described and documented with phase-contrast photomicrographs. Antisera against A. castellanii used in this test failed to react with cultures of A. polyphaga, A. astronyxis, and A. palestinensis.
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Preparation of an immunotoxin for Acanthamoeba castellanii
Biochemical and Biophysical Research Communications, 1984Acanthamoeba castellanii (Neff) is a small free-living amoeba which is closely related to pathogenic organisms that produce almost invariably fatal human infections (1). The f(ab)' fragment of a monoclonal antibody (designated A9) specifically reactive to the A. castellanii cell surface, was covalently linked to the A chain of diphtheria toxin.
C L, Villemez, P L, Carlo
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Acanthamoeba castellanii: Characterization of an Adhesin Molecule
Experimental Parasitology, 1999Acanthamoeba castellanii is a free-living protozoan that causes keratitis in humans and has been associated with pneumonia and granulomatous amebic encephalitis in dogs, sheep, and other species. Adherence of the Acanthamoeba to epithelial cells is critical to the pathogenesis of this disease.
M J, Kennett +3 more
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Encystment in Acanthamoeba castellanii: A review
Experimental Parasitology, 2014Differentiation of Acanthamoeba castellanii trophozoites involves massive turnover of cellular components and remodelling of organelle structure and function so as to produce a cryptobiotic cell, resistant to desiccation, heat, freezing, and chemical treatments.
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Mechanisms associated with Acanthamoeba castellanii (T4) phagocytosis
Parasitology Research, 2005Using fluorescein isothiocyanate (FITC)-labelled Escherichia coli, phagocytosis in Acanthamoeba is studied. This assay is based on the quenching effect of trypan blue on FITC-labelled E. coli. Only intracellular E. coli retain their fluorescence, which are easily discriminated from non-fluorescent adherent bacteria. Acanthamoeba uptake of E.
Selwa, Alsam +3 more
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Migration of Acanthamoeba castellanii Through Legionella Biofilms
2019The amoeba-resistant bacterium Legionella pneumophila infects humans through aerosols and thereby can cause a life-threatening pneumonia termed Legionnaires' disease. In the environment L. pneumophila forms and colonizes biofilms, which usually comprise complex multispecies communities. In these biofilms L.
Hochstrasser, R, Hilbi, H
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Ribosomal Phosphoproteins in Acanthamoeba castellanii
European Journal of Biochemistry, 1981Ribosomes and subunits from Acanthamoeba castellanii were purified. The pattern of ribosomal proteins was analysed by two‐dimensional get electrophoresis. The small subunit of cytoplasmic ribosomes contains 25 and the large 40 proteins. After incubation of exponentially growing cells with ortho[33P]phosphate for 1 j, one basic protein of the small ...
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[32] Myosins from Acanthamoeba castellanii
1982Publisher Summary This chapter presents procedure for purification of myosins from Acanthamoeba castellanii and it assay methods. Acanthamoeba castellanii contains three myosin isoenzymes referred to as myosins IA, IB, and II. Purification of Myosins IA and IB include extraction of approximately 1 kg of cells is extracted with 2 volumes of buffer
Edward D. Korn +2 more
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In vitro Characterization of Acanthamoeba castellanii Cytopathic Effect
The Journal of Parasitology, 1995This study examined the mechanism of the cytopathic effect (CPE) of Acanthamoeba castellanii on human target cells. Pathogenic Acanthamoeba trophozoites were incubated with human ocular melanoma (OCM1) cells for 30 min, 1 hr, and 3 hr. The amoebae were treated with a calcium ionophore (A23187), phorbol myristate ester (PMA), calcium channel blocker ...
W M, Taylor +3 more
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Metabolismus mědi u Acanthamoeba castellanii
2023Copper is an essential element that, due to its redox properties, is involved as a cofactor in many enzymes, the most well-known example is the cytochrome c oxidase. At the same time, in higher concentrations, this element shows toxic effects on several levels, it can disrupt iron-sulfur clusters, damage proteins and lead to cell death.
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