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1

Existing and future therapeutic options for hepatitis C virus infection

100%
Bretner M.
Acta Biochimica Polonica
|
2005
|
tom 52
|
nr 1
Hepatitis C virus (HCV) infection is an important cause of chronic hepatitis, cirrhosis, hepatocellular carcinoma and liver failure worldwide. Chronic hepatitis C virus infection is treated with interferon-alpha (IFN-alpha), pegylated interferon-alpha (PEG-IFNalpha) alone or in combination with ribavirin; however, a significant fraction of patients either fail to respond or relapse after cessation of therapy. Efforts to identify and develop highly specific and potent HCV inhibitors have intensified recently. Each of the virally encoded replication enzymes has been a focus of studies as well as viral receptors and the host immune system. This review summarizes recent progress in the search for novel anti-HCV agents.
2

Nowe inhibitory cyklu rozwojowego wirusow rodziny Flaviviridae.

51%
Bretner M., Felczak K., Siwecka M. A., Kulikowski T.
Działalność Naukowa PAN. Wybrane Zagadnienia
|
2002
|
tom 14
50-52
3

Selectivity of 4,5,6,7-tetrabromobenzimidazole [TBBZ] as an ATP-competitive potent inhibitor of protein kinase CK2 from various sources

45%
Zien P., Bretner M., Zastapilo K., Szyszka R., Shugar D.
Cellular and Molecular Biology Letters
|
2003
|
tom 08
|
nr 2A
4

Tetrabromobenzotriazole [TBBt] and tetrabromobenzimidazole [TBBz]: selective inhibitors of protein kinase CK2, and their influence on activities of different forms of human CK2, and on the cells

39%
Zien P., Litchfield D. W., Duncan J., Skierski J., Bretner M., Shugar D.
Cellular and Molecular Biology Letters
|
2005
|
tom 10
|
nr Suppl.2
5

NTPase-helicase of Flaviviridae: inhibitors and inhibition of the enzyme

39%
Borowski P., Niebuhr A., Schmitz H., Hosmane R. S., Bretner M., Siwecka M. A., Kulikowski T.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 3
RNA nucleoside triphosphatases (NTPase)/helicases represent a large family of pro­teins that are ubiquitously distributed over a wide range of organisms. The enzymes play essential role in cell development and differentiation, and some of them are in­volved in transcription and replication of viral single-stranded RNA genomes. The en­zymatic activities of a NTPase/helicase were also detected in the carboxyl-terminal non-structural protein 3 (NS3) of members of the Flaviviridae family. The crucial role of the enzyme for the virus life cycle was demonstrated in knock out experiments and by using NTPase/helicase specific inhibitors. This makes the enzyme an attractive tar­get for development of Flaviviridae-specific antiviral therapies. This review will sum-marize our knowledge about the function and structure of the enzyme, update the spectrum of inhibitors of the enzymatic activities of the NTPase/helicase and describe the different mechanisms by which the compounds act. Some of the compounds reviewed herein could show potential utility as antiviral agents against Flaviviridae viruses.
6

Different properties of four molecular forms of protein kinase CK2 from Saccharomyces cerevisiae

39%
Domanska K., Zielinski R., Kubinski K., Sajnaga E., Maslyk M., Bretner M., Szyszka R.
Acta Biochimica Polonica
|
2005
|
tom 52
|
nr 4
CK2 is a pleiotropic constitutively active serine/threonine protein kinase composed of two catalytic α- and two regulatory β-subunits, whose regulation is still not well understood. It seems to play an essential role in regulation of many cellular processes. Four active forms of CK2, composed of αα'ββ', α2ββ', α'2ββ', and a free α'-subunit were isolated from wild-type yeast and strains containing a single deletion of the catalytic subunit. Each species exhibits properties typical for CK2, but they differ in substrate specificity and sensitivity to inhibitors. This suggests that each CK2 isomer may regulate different process or may differ in the way of its regulation.
7

Acyclic analogues of 5-fluoro-dUMP and 5-fluoro-2'-deoxyuridine: Synthesis and inhibition of thymidylate synthase and tumour cell growth

39%
Felczak K., Golos B., Dzik J., Rode W., Bretner M., Shugar D., Kulikowski T.
Acta Biochimica Polonica
|
1998
|
tom 45
|
nr 1
1-[(2-Hydroxyethoxy)methyl]-5-fluorouracil (HEMFU) and 1-[(1,3-dihydroxy-2-propoxy)methyl]-5-fluorouracil (DHPFU) were prepared by alkylation of the di-O-TMS derivative of 5-fluorouracil and phosphorylated with the use of the wheat shoot phosphotransferase system to their monophosphates, HEMFUMP and DHPFUMP. 1-(2-Phosphonylmethoxyethyl)-5-fluorouracil (PMEFU) was obtained by condensation of diethyl-2-chloroethoxymethanephosphonate with 5-fluorouracil and cleavage of the alkylphosphoester with trimethylbromosilane. Inhibition of highly purified thymidylate synthase from mouse tumour Ehrlich carcinoma and leukemia L1210 cells by each of the nucleotide analogues, DHPFUMP, PMEFU and HEMFUMP, and of L5178Y mouse leukemia cell growth by the nucleoside (HEMFU) analogue, were studied. DHPFUMP proved to be the strongest inhibitor, non-competitive vs dUMP, with Kiapp 2.8 μM for time-independent interaction with the enzyme and N5,N10-methylenetetrahydrofolate (CH2H4PteGlu). In the presence of CH2H4PteGlu, DHPFUMP exhibited time-dependent inactivation of the enzyme, the inactivation rate plots being biphasic and pointing to Ki values in the μM range (103-fold higher than for 5-fluoro-dUMP). HEMFUMP and PMEFU were much weaker inhibitors of the enzyme, with Kiapp values of 0.26 μM (non-competitive vs dUMP) and 30 mM (non-competitive vs dUMP), respectively. HEMFU, despite the weak interaction of its nucleotide analogue with the enzyme, proved to be a strong cell (L5178Y) growth inhibitor, with IC50 in the range 10-5 M.
8

Expression and structural studies on hepatitis C virus helicase and its inhibitors

33%
Stankiewicz A., Strokovskaya L., Poznanski J., Zhukov I., Gozdek A., Bretner M., Zagorska-Ostoja W., Boguszewska-Chachulska A.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
9

Fluorescent hepatitis C virus (HCV) helicase assay

33%
Krawczyk M., Stankiewicz A., Strokovskaya L., Gozdek A., Galitonov G., Bretner M., Haenni A.-L., Zagorski W., Boguszewska-Chachulska A.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
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