These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: [The interaction of NS3 protein of hepatitis C virus with polymethylen derivatives of nucleic bases].
    Author: Mukovnia AV, Komissarov VV, Kritsyn AM, Mit'kevich VA, Tunitskaia VL, Kochetkov SN.
    Journal: Mol Biol (Mosk); 2010; 44(6):1045-53. PubMed ID: 21290826.
    Abstract:
    NS3 protein of hepatitis C virus plays the key role in the virus functioning. It possesses three enzymatic activities, namely protease activity, associated with N-terminal domain of the protein, and helicase/NTPase activities specific for C-terminal domain. Here, the effect of some polimethylenic derivatives of the nucleic bases on helicase and ATPase enzyme activities has been studied. Several of compounds tested displayed inhibitory activity towards NS3 helicase. However, most compounds demonstrated strong activating effect on ATPase activity of the enzyme as well as several other ATPases. The ATPase activating mechanism was not described earlier. The activation potency of the compounds depended on substrate/activator concentration ratio, and was maximal at the 1000:1. The activation mechanism scheme that allows us to explain phenomena observed is proposed.
    [Abstract] [Full Text] [Related] [New Search]