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Wyszukujesz frazę "Pietrzak, Robert" wg kryterium: Autor


Wyświetlanie 1-2 z 2
Tytuł:
Influence of silver nanoparticles on metabolism and toxicity of moulds
Autorzy:
Pietrzak, Katarzyna
Twarużek, Magdalena
Czyżowska, Agata
Kosicki, Robert
Gutarowska, Beata
Powiązania:
https://bibliotekanauki.pl/articles/1038932.pdf
Data publikacji:
2015
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
silver nanoparticles
moulds
mycotoxins
cytotoxicity
MTT
organic acids
extracellular enzymes
Opis:
The unique antimicrobial features of silver nanoparticles (AgNPs) are commonly applied in innumerable products. The lack of published studies on the mechanisms of AgNPs action on fungi resulted in identification of the aim of this study, which was: the determination of the influence of AgNPs on the mould cytotoxicity for swine kidney cells (MTT test) and the production of selected mycotoxins, organic acids, extracellular enzymes by moulds. The conducted study had shown that silver nanoparticles can change the metabolism and toxicity of moulds. AgNPs decrease the mycotoxin production of Aspergillus sp. (81-96%) and reduce mould cytotoxicity (50-75%). AgNPs influence the organic acid production of A. niger and P. chrysogenum by decreasing their concentration (especially of the oxalic and citric acid). Also, a change in the extracellular enzyme profile of A. niger and P. chrysogenum was observed, however, the total enzymatic activity was increased.
Źródło:
Acta Biochimica Polonica; 2015, 62, 4; 851-857
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Interaction of three Caenorhabditis elegans isoforms of translation initiation factor eIF4E with mono- and trimethylated mRNA 5 cap analogues.
Autorzy:
Stachelska, Alicja
Wieczorek, Zbigniew
Ruszczyńska, Katarzyna
Stolarski, Ryszard
Pietrzak, Monika
Lamphear, Barry
Rhoads, Robert
Darżynkiewicz, Edward
Jankowska-Anyszka, Marzena
Powiązania:
https://bibliotekanauki.pl/articles/1043732.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
fluorescence quenching
eIF4E
Caenorhabditis elegans
mRNA 5' cap
translation initiation
Opis:
Translation initiation factor eIF4E binds the m7G cap of eukaryotic mRNAs and mediates recruitment of mRNA to the ribosome during cap-dependent translation initiation. This event is the rate-limiting step of translation and a major target for translational control. In the nematode Caenorhabditis elegans, about 70% of genes express mRNAs with an unusual cap structure containing m32,2,7G, which is poorly recognized by mammalian eIF4E. C. elegans expresses five isoforms of eIF4E (IFE-1, IFE-2, etc.). Three of these (IFE-3, IFE-4 and IFE-5) were investigated by means of spectroscopy and structural modelling based on mouse eIF4E bound to m7GDP. Intrinsic fluorescence quenching of Trp residues in the IFEs by iodide ions indicated structural differences between the apo and m7G cap bound proteins. Fluorescence quenching by selected cap analogues showed that only IFE-5 forms specific complexes with both m7G- and m32,2,7G-containing caps (Kas 2×106 M-1 to 7×106 M-1) whereas IFE-3 and IFE-4 discriminated strongly in favor of m7G-containing caps. These spectroscopic results quantitatively confirm earlier qualitative data derived from affinity chromatography. The dependence of Kas on pH indicated optimal cap binding of IFE-3, IFE-4 and IFE-5 at pH 7.2, lower by 0.4 pH units than that of eIF4E from human erythrocytes. These results provide insight into the molecular mechanism of recognition of structurally different caps by the highly homologous IFEs.
Źródło:
Acta Biochimica Polonica; 2002, 49, 3; 671-682
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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