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

Standard

Inhibition of the helicase activity of HCV NTPase/helicase by 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide-5 '-triphosphate (ribavirin-TP). / Borowski, P; Lang, M; Niebuhr, A; Haag, A; Schmitz, H; Schulze zur Wiesch, J; Choe, J; Siwecka, M A; Kulikowski, T.

In: ACTA BIOCHIM POL, Vol. 48, No. 3, 2001, p. 739-44.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Borowski, P, Lang, M, Niebuhr, A, Haag, A, Schmitz, H, Schulze zur Wiesch, J, Choe, J, Siwecka, MA & Kulikowski, T 2001, 'Inhibition of the helicase activity of HCV NTPase/helicase by 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide-5 '-triphosphate (ribavirin-TP)', ACTA BIOCHIM POL, vol. 48, no. 3, pp. 739-44.

APA

Borowski, P., Lang, M., Niebuhr, A., Haag, A., Schmitz, H., Schulze zur Wiesch, J., Choe, J., Siwecka, M. A., & Kulikowski, T. (2001). Inhibition of the helicase activity of HCV NTPase/helicase by 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide-5 '-triphosphate (ribavirin-TP). ACTA BIOCHIM POL, 48(3), 739-44.

Vancouver

Borowski P, Lang M, Niebuhr A, Haag A, Schmitz H, Schulze zur Wiesch J et al. Inhibition of the helicase activity of HCV NTPase/helicase by 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide-5 '-triphosphate (ribavirin-TP). ACTA BIOCHIM POL. 2001;48(3):739-44.

Bibtex

@article{bc7f3cd0df94400d850dcb57288e83a2,
title = "Inhibition of the helicase activity of HCV NTPase/helicase by 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide-5 '-triphosphate (ribavirin-TP)",
abstract = "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.",
keywords = "Acid Anhydride Hydrolases/antagonists & inhibitors, Antiviral Agents/pharmacology, DNA/metabolism, DNA Helicases/antagonists & inhibitors, Hepacivirus/enzymology, Kinetics, Nucleoside-Triphosphatase, Nucleotides/pharmacology, Ribavirin/pharmacology, Substrate Specificity",
author = "P Borowski and M Lang and A Niebuhr and A Haag and H Schmitz and {Schulze zur Wiesch}, J and J Choe and Siwecka, {M A} and T Kulikowski",
year = "2001",
language = "English",
volume = "48",
pages = "739--44",
journal = "ACTA BIOCHIM POL",
issn = "0001-527X",
publisher = "Acta Biochimica Polonica",
number = "3",

}

RIS

TY - JOUR

T1 - Inhibition of the helicase activity of HCV NTPase/helicase by 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide-5 '-triphosphate (ribavirin-TP)

AU - Borowski, P

AU - Lang, M

AU - Niebuhr, A

AU - Haag, A

AU - Schmitz, H

AU - Schulze zur Wiesch, J

AU - Choe, J

AU - Siwecka, M A

AU - Kulikowski, T

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

KW - Acid Anhydride Hydrolases/antagonists & inhibitors

KW - Antiviral Agents/pharmacology

KW - DNA/metabolism

KW - DNA Helicases/antagonists & inhibitors

KW - Hepacivirus/enzymology

KW - Kinetics

KW - Nucleoside-Triphosphatase

KW - Nucleotides/pharmacology

KW - Ribavirin/pharmacology

KW - Substrate Specificity

M3 - SCORING: Journal article

C2 - 11833782

VL - 48

SP - 739

EP - 744

JO - ACTA BIOCHIM POL

JF - ACTA BIOCHIM POL

SN - 0001-527X

IS - 3

ER -