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    Selective pharmacological targeting of a DEAD box RNA helicase.

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    Author
    Lindqvist, L; Oberer, M; Reibarkh, M; Cencic, R; Bordeleau, M-E; Vogt, E; Marintchev, A; Tanaka, J; Fagotto, F; Altmann, M; ...
    Date
    2008-02-13
    Source Title
    PLoS One
    Publisher
    Public Library of Science (PLoS)
    University of Melbourne Author/s
    Lindqvist, Lisa
    Affiliation
    Medical Biology (W.E.H.I.)
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Lindqvist, L., Oberer, M., Reibarkh, M., Cencic, R., Bordeleau, M. -E., Vogt, E., Marintchev, A., Tanaka, J., Fagotto, F., Altmann, M., Wagner, G. & Pelletier, J. (2008). Selective pharmacological targeting of a DEAD box RNA helicase.. PLoS One, 3 (2), pp.e1583-. https://doi.org/10.1371/journal.pone.0001583.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/257189
    DOI
    10.1371/journal.pone.0001583
    Open Access at PMC
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2216682
    Abstract
    RNA helicases represent a large family of proteins implicated in many biological processes including ribosome biogenesis, splicing, translation and mRNA degradation. However, these proteins have little substrate specificity, making inhibition of selected helicases a challenging problem. The prototypical DEAD box RNA helicase, eIF4A, works in conjunction with other translation factors to prepare mRNA templates for ribosome recruitment during translation initiation. Herein, we provide insight into the selectivity of a small molecule inhibitor of eIF4A, hippuristanol. This coral-derived natural product binds to amino acids adjacent to, and overlapping with, two conserved motifs present in the carboxy-terminal domain of eIF4A. Mutagenesis of amino acids within this region allowed us to alter the hippuristanol-sensitivity of eIF4A and undertake structure/function studies. Our results provide an understanding into how selective targeting of RNA helicases for pharmacological intervention can be achieved.

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