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1
Content available remote

The presence of deoxyribonucleolytic activity in cytoplasmic ribosomes of rye (Secale cereale L) germs

100%
Siwecka M. A., Rytel M., Szarkowski J. W.
Acta Biochimica Polonica
|
1979
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vol. 26
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issue 1-2
97-101
2
Content available remote

Purification and some properties of a novel dsRNA degrading nuclease bound to rye germ ribosomes

99%
Siwecka M. A.
Acta Biochimica Polonica
|
1997
|
vol. 44
|
issue 1
61-68
3
Content available remote

Purification and characterization of nuclease I associated with rye germ ribosomes

88%
Siwecka M. A., Rytel M., Szarkowski J. W.
Acta Biochimica Polonica
|
1989
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vol. 36
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issue 1
45-62
4
Content available remote

Synthesis and anti-HIV properties of novel 6-phenylselenenyl-5-propyluracils

76%
Miazga A., Felczak K., Siwecka M. A., Lipniacki A., Piasek A., Kulikowski T.
|
2007
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vol. 54
|
issue 4
863-868
EN
Novel 6-phenylselenenyl-5-propyluracils were synthesized from 5-propyluracil with the use of regioselective synthesis to give 1-[(2-hydroxyethoxy)-methyl]-6-phenylselenenyl-5-propyluracil (6), 1-ethoxymethyl-6-phenylselenenyl-5-propyluracil (9) and 1-benzyloxymethyl-6-phenylselenenyl-5-propyluracil (10). Interaction of these compounds with recombinant HIV-1 reverse transcriptase (RT) was evaluated using a non-isotopic colorimetric method. Compounds 9 and 10 exerted potent HIV RT inhibition (IC50 0.06 and 0.05 µM respectively) while compound 6 showed moderate inhibition (IC50 = 3.5 µM). Potent anti-HIV-1 activity in MT-2 cells inoculated by a syncythia-inducing HIV-1 (cat #3 strain) laboratory isolate was exerted by compounds 9 and 10 (EC50 0.62 µM and 0.025 µM, respectively), while compound 6 showed only moderate activity (IC50 = 4.1 µM). In addition, compound 10 showed very good in vitro therapeutic index (TI > 2046), indicating that it is a potential anti-HIV/AIDS drug.
5
Content available remote

NTPase/helicase of Flaviviridae: inhibitors and inhibition of the enzyme.

76%
Borowski P., Niebuhr A., Schmitz H., Hosmane R. S., Bretner M., Siwecka M. A., Kulikowski T.
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2002
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vol. 49
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issue 3
597-614
EN
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 summarize 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
Content available remote

Inhibition of the helicase activity of HCV NTPase/helicase by 1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide-5'-triphosphate (ribavirin-TP).

64%
Borowski P., Lang M., Niebuhr A., Haag A., Schmitz H., Wiesch J. S. z., Choe J., Siwecka M. A., Kulikowski T.
|
2001
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vol. 48
|
issue 3
739-744
EN
In the presented study the ribavirin-TP - an established inhibitor of the NTPase activity of the superfamily NTPase/helicases II - was investigated as an inhibitor of the unwinding activity of the hepatitis C virus (HCV) NTPase/helicase. The kinetics of the reaction revealed that ribavirin-TP reduces the turnover number of the helicase reaction by a mechanism that does not correspond to that of the inhibition of the NTPase activity. Our results suggest that derivatives of ribavirin-TP with enhanced stability towards hydrolytic attack may be effective inhibitors of the enzyme.
7
Content available remote

ATP-binding domain of NTPase/helicase as a target for hepatitis C antiviral therapy.

64%
Borowski P., Mueller O., Niebuhr A., Kalitzky M., Hwang L.-H., Schmitz H., Siwecka M. A., Kulikowski T.
|
2000
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vol. 47
|
issue 1
173-180
EN
To enhance the inhibitory potential of 1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide (ribavirin) vs hepatitis C virus (HCV) NTPase/helicase, ribavirin-5'-triphosphate (ribavirin-TP) was synthesized and investigated. Ribavirin-TP was prepared with the use of modified Yoshikawa-Ludwig-Mishra-Broom procedure (cf. Mishra & Broom, 1991, J. Chem. Soc., Chem. Commun, 1276-1277) involving phosphorylation of unprotected nucleoside. Kinetic analysis revealed enhanced inhibitory potential of ribavirin-TP (IC50=40 μM) as compared to ribavirin (IC50 > 500 μM). Analysis of the inhibition type by means of graphical methods showed a competitive type of inhibition with respect to ATP. In view of the relatively low specificity towards nucleoside-5'-triphosphates (NTP) of the viral NTPase/helicases, it could not be ruled out that the investigated enzyme hydrolyzed the ribavirin-TP to less potent products. Investigations on non- hydrolysable analogs of ribavirin-TP or ribavirin-5'-diphosphate (ribavirin-DP) are currently under way.
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