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Showing 1–8 of 8 results
Advanced filters: Author: Stephen Orlicky Clear advanced filters

  • Although general inhibitors of the ubiquitin-proteasome system have been reported, compounds targeting specific ubiquitylation enzymes should be beneficial in clinical applications and basic research. Orlicky et al. present an allosteric inhibitor specific to the yeast SCFCdc4 E3 ligase that prevents binding of the target protein to the WD40 domain of the complex.

    • Stephen Orlicky
    • Xiaojing Tang
    • Mike Tyers
    Research
    Nature Biotechnology
    Volume: 28, P: 733-737

  • In the ubiquitin-proteasome system, E2 enzymes such as Cdc34A mediate the transfer of ubiquitin to protein substrates, which are thus marked for proteasomal degradation or other fates. New structural data reveal that the small-molecule inhibitor CC0651 impairs Cdc34A activity by stabilizing the normally transient Cdc34A–ubiquitin complex.

    • Hao Huang
    • Derek F Ceccarelli
    • Frank Sicheri
    Research
    Nature Chemical Biology
    Volume: 10, P: 156-163

  • Antibody diversification relies on the intentional mutagenesis of immunoglobulin genes for adaptive immune responses. Here, the authors identified a CTLH E3 ubiquitin ligase complex that co-opts FAM72A to recruit and degrade the UNG2 base excision repair factor to permit mutagenesis.

    • Philip Barbulescu
    • Chetan K. Chana
    • Alberto Martin
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-19

  • KEOPS is an evolutionary conserved complex with a core of four core subunits—Pcc1, Kae1, Bud32 and Cgi121—that catalyzes the universal and essential tRNA modification N6-threonylcarbamoyl adenosine (t6A). Here the authors describe a Cgi121-tRNA crystal structure and new composite model of the KEOPS holo-enzyme-substrate complex that shed light on the t6A catalytic cycle and its regulation.

    • Jonah Beenstock
    • Samara Mishelle Ona
    • Frank Sicheri
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-17

  • A PROTAC termed P4B targeting BRAF V600E mutant has been developed, which displays enhanced inhibitory function in cell lines carrying BRAF mutations that impart resistance to conventional BRAF inhibitors.

    • Ganna Posternak
    • Xiaojing Tang
    • Frank Sicheri
    Research
    Nature Chemical Biology
    Volume: 16, P: 1170-1178

  • The WD40 domain of the SCFCdc4ubiquitin ligase targets substrates via multiple phosphorylated degron motifs. The authors define a second degron-binding WD40 pocket that imparts a negative allosteric effect on binding to the primary pocket, and thereby enables the dynamic exchange of bound degrons.

    • Veronika Csizmok
    • Stephen Orlicky
    • Julie D. Forman-Kay
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-14