BRADFORD SCHOLARS

    • Sign in
    View Item 
    •   Bradford Scholars
    • Life Sciences
    • Life Sciences Publications
    • View Item
    •   Bradford Scholars
    • Life Sciences
    • Life Sciences Publications
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of Bradford ScholarsCommunitiesAuthorsTitlesSubjectsPublication DateThis CollectionAuthorsTitlesSubjectsPublication Date

    My Account

    Sign in

    HELP

    Bradford Scholars FAQsCopyright Fact SheetPolicies Fact SheetDeposit Terms and ConditionsDigital Preservation Policy

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Polar, Functionalized Guanine-O6 Derivatives Resistant to Repair by O6-Alkylguanine-DNA Alkyltransferase: Implications for the Design of DNA-modifying Drugs.

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Publication date
    2009-07-28T08:31:51Z
    Author
    Wheelhouse, Richard T.
    Bibby, Michael C.
    Nicolaou, Anna
    Pletsas, Dimitrios
    Keyword
    Structure activity relation
    Guanine derivatives
    Competitive inhibition
    Purine derivatives
    Enzyme inhibitor
    In vitro
    Chemical synthesis
    Enzyme
    Transferases
    DNA
    Repair
    Show allShow less
    Peer-Reviewed
    Yes
    
    Metadata
    Show full item record
    Abstract
    The protein O6-alkylguanine-DNA alkyltransferase (Atase) is responsible for the repair of DNA lesions generated by several clinically important anti-cancer drugs; this is manifest as active resistance in those cancer cell lines proficient in Atase expression. Novel O6-substituted guanine analogues have been synthesized, bearing acidic, basic and hydrogen bonding functional groups. In contrast to existing O6-modified purine analogues, such as methyl or benzyl, the new compounds were found to resist repair by Atase even when tested at concentrations much higher than O6-benzylguanine, a well-established Atase substrate active both in vitro and in vivo. The inactivity of the new purines as covalent substrates for Atase indicates that agents to deliver these groups to DNA would represent a new class of DNA-modifying drug that circumvents Atase-mediated resistance.
    URI
    http://hdl.handle.net/10454/3168
    Version
    No full-text available in the repository
    Citation
    Pletsas, D., Wheelhouse, R.T., Pletsas, V., Nicolaou, A., Jenkins, T.C., Bibby, M.C. and Kyrtopoulos, S.A. (). Polar, Functionalized Guanine-O6 Derivatives Resistant to Repair by O6-Alkylguanine-DNA Alkyltransferase: Implications for the Design of DNA-modifying Drugs. European Journal of Medicinal Chemistry.
    Link to publisher’s version
    http://dx.doi.org/10.1016/j.ejmech.2005.11.007
    Type
    Article
    Collections
    Life Sciences Publications

    entitlement

     
    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Quick Guide | Contact Us
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.