Exploring the role of p97 and its UBX-domain cofactors through identification of their interacting proteins

G. Alexandru

    Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

    4 Citations (Scopus)

    Abstract

    The elucidation of protein-protein interaction networks can provide preliminary insights into the function of uncharacterized proteins based on the interactions they establish in the cell. Here, we describe a protein immunoprecipitation protocol that can be used in combination with mass spectrometry analysis to identify the p97 interactome as well as specific subgroups of proteins interacting with its UBX-domain adaptors. This approach aims to dissect the role played by individual UBX cofactors within the complex array of cellular functions performed by p97.
    Original languageEnglish
    Title of host publicationUbiquitin family modifiers and the proteasome
    Subtitle of host publicationreviews and protocols
    EditorsR. Jürgen Dohmen , Martin Scheffner
    PublisherHumana Press
    Pages305-312
    Number of pages8
    ISBN (Electronic)9781617794742
    ISBN (Print)9781617794735
    DOIs
    Publication statusPublished - 2012

    Publication series

    NameMethods in molecular biology
    PublisherHumana Press
    Volume832
    ISSN (Print)1064-3745

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  • Cite this

    Alexandru, G. (2012). Exploring the role of p97 and its UBX-domain cofactors through identification of their interacting proteins. In R. J. Dohmen , & M. Scheffner (Eds.), Ubiquitin family modifiers and the proteasome: reviews and protocols (pp. 305-312). (Methods in molecular biology; Vol. 832). Humana Press. https://doi.org/10.1007/978-1-61779-474-2_21