• Login
    View Item 
    •   DSpace@RPI Home
    • The Linhardt Research Labs
    • Linhardt Research Labs Papers
    • View Item
    •   DSpace@RPI Home
    • The Linhardt Research Labs
    • Linhardt Research Labs Papers
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Regulation of PTP1B activation through disruption of redox-complex formation

    Author
    Londhe, Avinash D.; Bergeron, Alexandre; Curley, Stephanie M.; Zhang, Fuming; Rivera, Keith D.; Kannan, Akaash; Coulis, Gérald; Rizvi, Syed H.M.; Kim, Seung Jun; Pappin, Darryl J.; Tonks, Nicholas K.; Linhardt, Robert J.; Boivin, Benoit
    ORCID
    https://orcid.org/0000-0003-2219-5833
    Thumbnail
    View/Open
    REGULATION OF PTP1B ACTIVATION THROUGH DISRUPTION OF REDOX-.pdf (788.3Kb)
    Other Contributors
    Date Issued
    2020-02-01
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    Full Citation
    Regulation of PTP1B activation through disruption of redox-complex formation, A. D. Londhe, A. Bergeron, S. M. Curley, F. Zhang, K. D. Rivera, A. Kannan, G. Coulis, S. H. M. Rizvi, S. J. Kim, D. J. Pappin, N. K. Tonks, R. J. Linhardt, B. Boivin, Nature Chemical Biology, 16, 122-125, 2020.
    Metadata
    Show full item record
    URI
    https://hdl.handle.net/20.500.13015/5397; https://doi.org/10.1038/s41589-019-0433-0
    Abstract
    We have identified a molecular interaction between the reversibly oxidized form of protein tyrosine phosphatase 1B (PTP1B) and 14-3-3ζ that regulates PTP1B activity. Destabilizing the transient interaction between 14-3-3ζ and PTP1B prevented PTP1B inactivation by reactive oxygen species and decreased epidermal growth factor receptor phosphorylation. Our data suggest that destabilizing the interaction between 14-3-3ζ and the reversibly oxidized and inactive form of PTP1B may establish a path to PTP1B activation in cells.;
    Description
    Nature Chemical Biology, 16, 122-125; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Publisher
    Nature
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Nature Chemical Biology; https://harc.rpi.edu/;
    Access
    A full text version is available in DSpace@RPI;
    Collections
    • Linhardt Research Labs Papers

    Browse

    All of DSpace@RPICommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    Login

    DSpace software copyright © 2002-2022  DuraSpace
    Contact Us | Send Feedback
    DSpace Express is a service operated by 
    Atmire NV