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Wyszukujesz frazę "Niebuhr, Andreas" wg kryterium: Autor


Wyświetlanie 1-3 z 3
Tytuł:
NTPase/helicase of Flaviviridae: inhibitors and inhibition of the enzyme.
Autorzy:
Borowski, Peter
Niebuhr, Andreas
Schmitz, Herbert
Hosmane, Ramachandra
Bretner, Maria
Siwecka, Maria
Kulikowski, Tadeusz
Powiązania:
https://bibliotekanauki.pl/articles/1043721.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
NTPase/helicase inhibitors
Flaviviridae
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2002, 49, 3; 597-614
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
ATP-binding domain of NTPase/helicase as a target for hepatitis C antiviral therapy.
Autorzy:
Borowski, Peter
Mueller, Oliver
Niebuhr, Andreas
Kalitzky, Matthias
Hwang, Lih-Hwa
Schmitz, Herbert
Siwecka, Maria
Kulikowski, Tadeusz
Powiązania:
https://bibliotekanauki.pl/articles/1044428.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
ribavirin-5'-triphosphate
enzyme inhibition
HCV NTPase/helicase
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2000, 47, 1; 173-180
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Inhibition of the helicase activity of HCV NTPase/helicase by 1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide-5-triphosphate (ribavirin-TP).
Autorzy:
Borowski, Peter
Lang, Melanie
Niebuhr, Andreas
Haag, Annemarie
Schmitz, Herbert
Schulze zur Wiesch, Julian
Choe, Joonho
Siwecka, Maria
Kulikowski, Tadeusz
Powiązania:
https://bibliotekanauki.pl/articles/1044103.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
ribavirin-5'-triphosphate
enzyme inhibition
HCV helicase
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2001, 48, 3; 739-744
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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