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    Rational development of novel activity probes for the analysis of human cytochromes P450

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    Publication date
    2016-06-08
    End of Embargo
    2017-05-06
    2017-05-06
    Author
    Sellars, J.D.
    Skipsey, M.
    Sadr-ul-Shaheed
    Gravell, Sebastian
    Abumansour, Hamza M.A.
    Kashtl, Ghasaq
    Irfan, Jawaria
    Khot, Mohamed
    Pors, Klaus
    Patterson, Laurence H.
    Sutton, Chris W.
    Keyword
    Human cytochromes P450; Functional cytochromes; CYPs; Drug efficacy; Probe binding; NADPH
    Rights
    (c) Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. This is the peer-reviewed version of the following article: Sellars JD, Skipsey M, Sadr-ul-Shaheed S et al (2016) Rational development of novel activity probes for the analysis of human cytochromes P450. ChemMedChem. 11(11): 1122-1128, which has been published in final form at http://dx.doi.org/10.1002/cmdc.201600134. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
    Peer-Reviewed
    Yes
    
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    Abstract
    The identification and quantification of functional cytochromes P450 (CYPs) in biological samples is proving important for robust analyses of drug efficacy and metabolic disposition. In this study, a novel CYP activity-based probe was rationally designed and synthesised, demonstrating selective binding of CYP isoforms. The dependence of probe binding upon the presence of NADPH permits the selective detection of functionally active CYP. This allows the detection and analysis of these enzymes using biochemical and proteomic methodologies and approaches.
    URI
    http://hdl.handle.net/10454/8900
    Version
    final draft paper
    Citation
    Sellars JD, Skipsey M, Sadr-ul-Shaheed et al (2016) Rational development of novel activity probes for the analysis of human cytochromes P450. ChemMedChem. 11(11): 1122-1128.
    Link to publisher’s version
    http://dx.doi.org/10.1002/cmdc.201600134
    Type
    Article
    Notes
    The full-text of this article will be released for public view at the end of the publisher embargo on 6 May 2017.
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    Life Sciences Publications

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