Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-02

AUTHORS

Alexei Degterev, Alexey Lugovskoy, Michael Cardone, Bradley Mulley, Gerhard Wagner, Timothy Mitchison, Junying Yuan

ABSTRACT

To study the role of the BH3 domain in mediating pro-apoptotic and anti-apoptotic activities of Bcl-2 family members, we identified a series of novel small molecules (BH3Is) that inhibit the binding of the Bak BH3 peptide to Bcl-xL. NMR analyses revealed that BH3Is target the BH3-binding pocket of Bcl-xL. Inhibitors specifically block the BH3-domain-mediated heterodimerization between Bcl-2 family members in vitro and in vivo and induce apoptosis. Our results indicate that BH3-dependent heterodimerization is the key function of anti-apoptotic Bcl-2 family members and is required for the maintenance of cellular homeostasis. More... »

PAGES

ncb0201_173

Journal

TITLE

Nature Cell Biology

ISSUE

2

VOLUME

3

From Grant

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/35055085

    DOI

    http://dx.doi.org/10.1038/35055085

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1031670473

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11175750


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