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Wyszukujesz frazę "Gołos, Barbara" wg kryterium: Autor


Wyświetlanie 1-7 z 7
Tytuł:
Synthesis and interaction with thymidylate synthase of 5'-dithiophosphate and 5'-fluorothiophosphate of thymidine
Autorzy:
Gołos, Barbara
Misiura, Konrad
Olesiak, Magdalena
Okruszek, Andrzej
Rode, Wojciech J.
Powiązania:
https://bibliotekanauki.pl/articles/1044856.pdf
Data publikacji:
1998
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1998, 45, 1; 83-86
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The effect of Arg209 to Lys mutation in mouse thymidylate synthase.
Autorzy:
Cieśla, Joanna
Gołos, Barbara
Wałajtys-Rode, Elżbieta
Jagielska, Elżbieta
Płucienniczak, Andrzej
Rode, Wojciech
Powiązania:
https://bibliotekanauki.pl/articles/1043728.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
nucleotide's phosphate binding
thymidylate synthase
mutation
Opis:
Mouse thymidylate synthase R209K (a mutation corresponding to R218K in Lactobacillus casei), overexpressed in thymidylate synthase-deficient Escherichia coli strain, was poorly soluble and with only feeble enzyme activity. The mutated protein, incubated with FdUMP and N5,10-methylenetetrahydrofolate, did not form a complex stable under conditions of SDS/polyacrylamide gel electrophoresis. The reaction catalyzed by the R209K enzyme (studied in a crude extract), compared to that catalyzed by purified wild-type recombinant mouse thymidylate synthase, showed the Km value for dUMP 571-fold higher and Vmax value over 50-fold (assuming that the mutated enzyme constituted 20% of total crude extract protein) lower. Thus the ratios kcat, R209K/kcat, 'wild' and (kcat, R209K/Km, R209KdUMP)/( kcat, 'wild'/Km, 'wild'dUMP) were 0.019 and 0.000032, respectively, documenting that mouse thymidylate synthase R209, similar to the corresponding L. casei R218, is essential for both dUMP binding and enzyme reaction.
Źródło:
Acta Biochimica Polonica; 2002, 49, 3; 651-658
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Effect of cyclosporin A on immunological response in lungs of guinea pigs infected with Trichinella spiralis.
Autorzy:
Dzik, Jolanta
Zieliński, Zbigniew
Gołos, Barbara
Jagielska, Elżbieta
Wranicz, Mariusz
Wałajtys-Rode, Elżbieta
Powiązania:
https://bibliotekanauki.pl/articles/1043834.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
bronchoalveolar lavage
cyclosporin A
Trichinella
lungs
trichinellosis
nitric oxide
superoxide
Opis:
The effects of cyclosporin A (CsA), a potent immunosuppressive drug with antiparasitic activity, on the innate immunological response in guinea pig lungs during an early period (6th and 14th days) after T. spiralis infection were studied. CsA treatment of T. spiralis-infected guinea pigs caused a significant attenuation of immunological response in lungs by decreasing lymphocyte infiltration into pulmonary alveolar space, inhibiting alveolar macrophage superoxide anion production and lowering both the production of NO metabolites measured in bronchoalveolar lavage fluid and expression of the iNOS protein in lung homogenates, allowing us to speculate that the T. spiralis-dependent immunological response is dependent on lymphocyte T function. Interestingly, CsA itself had a pro-inflammatory effect, promoting leucocyte accumulation and macrophage superoxide production in guinea pig lungs. This observation may have a relevance to the situation in patients undergoing CsA therapy. Macrophage expression of the iNOS protein, evaluated by immunoblotting was not influenced by treatment of animals with CsA or anti-TGF-antibody, indicating different regulation of the guinea pig and murine enzymes.
Źródło:
Acta Biochimica Polonica; 2002, 49, 1; 233-247
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Sulfamide antifolates inhibiting thymidylate synthase: synthesis, enzyme inhibition and cytotoxicity.
Autorzy:
Pawełczak, Krzysztof
Makowski, Maciej
Kempny, Michał
Dzik, Jolanta
Gołos, Barbara
Rode, Wojciech
Rzeszotarska, Barbara
Powiązania:
https://bibliotekanauki.pl/articles/1043769.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
thymidylate synthase inhibitors
antifolate analogues
antifolates
p-aminobenzenesulfonic acid
Opis:
Synthesis and biological evaluation are described of seven new analogues (3-9) of two potent thymidylate synthase inhibitors, 10-propargyl-5,8-dideazafolate (1) and its 2-methyl-2-deamino congener ICI 198583 (2). While the new compunds 3 and 4 were analogues of 1 and 2, respectively, containing a p-aminobenzenesulfonyl residue in place of the p-aminobenzoic acid residue, the remaining 5 new compounds were analogues of 4 with the L-glutamic acid residue replaced by glycine (5), L-valine (6), L-alanine (7), L-phenylglycine (8) or L-norvaline (9). The new analogues were tested as inhibitors of thymidylate synthases isolated from tumour (Ehrlich carcinoma), parasite (Hymenolepis diminuta) and normal tissue (regenerating rat liver) and found to be weaker inhibitors than the parent 10-propargyl-5,8-dideazafolic acid. Selected new analogues, tested as inhibitors of growth of mouse leukemia L 5178Y cells, were less potent than the parent 10-propargyl-5,8-dideazafolic acid. Substitution of the glutamyl residue in compound 4 with l-norvaline (9) resulted in only a 5-fold stronger thymidylate synthase inhibitor, but a 40-fold weaker cell growth inhibitor.
Źródło:
Acta Biochimica Polonica; 2002, 49, 2; 407-420
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Acyclic analogues of 5-fluoro-dUMP and 5-fluoro-2-deoxyuridine: Synthesis and inhibition of thymidylate synthase and tumour cell growth
Autorzy:
Felczak, Krzysztof
Gołos, Barbara
Dzik, Jolanta
Rode, Wojciech
Bretner, Maria
Shugar, David
Kulikowski, Tadeusz
Powiązania:
https://bibliotekanauki.pl/articles/1044855.pdf
Data publikacji:
1998
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1998, 45, 1; 75-82
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Synthesis and biological activity of Nα-[4-[N-[(3,4-dihydro-2-methyl-4-oxo-6-quinazolinyl)methyl]-N-propargylamino]phenyl-acetyl]-L-glutamic acid.
Autorzy:
Kusakiewicz-Dawid, Anna
Bugaj, Marta
Dzik, Jolanta
Gołos, Barbara
Wińska, Patrycja
Pawełczak, Krzysztof
Rzeszotarska, Barbara
Rode, Wojciech
Powiązania:
https://bibliotekanauki.pl/articles/1043826.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
ICI 198583 analogue
inhibition
thymidylate synthase
Opis:
2-Deamino-2-methyl-N10-propargyl-5,8-dideazafolic acid (ICI 198583) is a potent inhibitor of thymidylate synthase. Its analogue, Nα-[4-[N-[(3,4-dihydro-2-methyl-4-oxo-6-quinazolinyl)methyl]-N-propargylamino]phenylacetyl]-L-glutamic acid, containing p-aminophenylacetic acid residue substituting p-aminobenzoic acid residue, was synthesized. The new analogue exhibited a moderately potent thymidylate synthase inhibition, of linear mixed type vs. the cofactor, N5,10 -methylenetetrahydrofolate. The Ki value of 0.34 μM, determined with a purified recombinant rat hepatoma enzyme, was about 30-fold higher than that reported for inhibition of thymidylate synthase from mouse leukemia L1210 cells by ICI 198583 (Hughes et al., 1990, J. Med. Chem. 33, 3060). Growth of mouse leukemia L5178Y cells was inhibited by the analogue (IC50 = 1.26 μM) 180-fold weaker than by ICI 198583 (IC50 = 6.9 μM).
Źródło:
Acta Biochimica Polonica; 2002, 49, 1; 197-202
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-7 z 7

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