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Stadnyk V.V.,Institute of Animal Biology UAAS | Izyumova L.A.,Institute of Animal Biology UAAS | Rzhepetskiy Y.A.,Ukrainian Academy of Sciences | Mayor C.Y.,Institute of Animal Biology UAAS | Vlizlo V.V.,Institute of Animal Biology UAAS
Letters in Drug Design and Discovery | Year: 2010

The subject of this work was an inhibition of cellular prion expression in vitro and in vivo by antisense oligodeoxyribonucleotides, incorporated into cationic immunoliposomes. It was shown that asODNs are able to reduce the level of PrPc expression in vitro and in vivo. © 2010 Bentham Science Publishers Ltd.

Kaminska M.,Institute of Animal Biology UAAS | Huntchak A.,Institute of Animal Biology UAAS | Borowiec F.,Agricultural University of Krakow | Ratych I.,Institute of Animal Biology UAAS | Barteczko J.,Agricultural University of Krakow
Annals of Animal Science | Year: 2010

The main objective of the present study was to determine the characteristics of microflora composition of caecum and colon in hens and geese reared under standard conditions. Some similarities and differences in microflora composition in some parts of the gastrointestinal tract of birds were shown. The maximum total amount of microorganisms was determined in the layer hens' gastrointestinal tract, especially in the caecum content. Different groups of microorganisms decreased in the following order in hens: bifidobacteria, Lactobacillus, E. coli, Enterococcus, Streptococcus, Staphylococcus and fungi. A different order was typical of geese: bifidobacteria, E. coli, Lactobacillus, Streptococcus, Staphylococcus and fungi. The intestinal tracts of geese were characterized by the presence of moulds.

Stadnyk V.,Institute of Animal Biology UAAS | Mayor C.,Institute of Animal Biology UAAS | Izyumova L.,Institute of Animal Biology UAAS | Vlizlo V.,Institute of Animal Biology UAAS
Medical Hypotheses | Year: 2011

In this paper, we propose the hypothesis that the long incubation period of prion infections is dependent upon a low rate of pathological prion formation and accumulation. Reduced pathological prion formation might be caused by the high content of β-sheets in the molecule. β-Sheet folding appears to proceed more slowly than folding of α-helices; the former are a major component of the prion secondary structure. This hypothesis strongly agrees with the data about folding of the artificial protein l-polylysine. This protein exists in two subforms: a rapidly folding α-helix-enriched form and a β-sheet-rich form having a very slow speed of secondary and tertiary structure formation. According to our hypothesis, the limiting factor for prion infection propagation is the speed of β-sheet folding in molecules of pathological prion but not the speed of migration of this protein through the host organism. © 2011 Elsevier Ltd.

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