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Showing 1–14 of 14 results
Advanced filters: Author: Peter Loppnau Clear advanced filters

  • The authors show that DCAF1, a substrate receptor of CUL4 and EDVP E3 ligases, can be recruited by PROTACs to degrade the cancer drug target, WDR5. They also report the crystal structures of PROTAC ternary complexes that reveal a significant role for loops in DCAF1 substrate recognition, a potential mechanism behind the diverse substrate specificity of DCAF1.

    • Mark F. Mabanglo
    • Brian Wilson
    • Masoud Vedadi
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-17

  • The SMN protein recognizes symmetric dimethylarginine by its Tudor domain, and SMN deficiency leads to spinal muscular atrophy. Here, Liu et al. discover a small molecule that binds to the SMN Tudor domain and disrupts the interaction between SMN and RNA Polymerase II.

    • Yanli Liu
    • Aman Iqbal
    • Jinrong Min
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12

  • PRDM9 is a PR domain containing histone methyl transferase which expression is normally restricted to the germline that has also been linked to a number of somatic cancers. Here the authors describe the identification of a small molecule that selectivity inhibits the methyltransferase activity of PRDM9 in biochemical and cellular assays

    • Abdellah Allali-Hassani
    • Magdalena M. Szewczyk
    • Masoud Vedadi
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-11

  • Owens et al. reported PFI-7, a selective and potent antagonist of GID4 of the CTLH E3 ligase complex, which enables identification of human GID4 targets. This study provides valuable insights into GID4 functions and a powerful tool for advancing new targeted protein degradation strategies.

    • Dominic D. G. Owens
    • Matthew E. R. Maitland
    • Cheryl H. Arrowsmith
    Research
    Nature Chemical Biology
    Volume: 20, P: 1164-1175

  • OICR-41103 is a potent, selective probe targeting the DCAF1 WDR domain and displacing viral Vpr protein. It enables new opportunities in cancer research, antiviral therapy, and targeted protein degradation via PROTACs.

    • Serah W. Kimani
    • Mahmoud Noureldin
    • Levon Halabelian
    ResearchOpen Access
    Communications Biology
    Volume: 8, P: 1-12

  • SETDB1 is a histone methyltransferase that generates H3K9me3 marks in euchromatic regions. Here the authors show that the triple Tudor domain (3TD) of SETDB1 binds histone H3 tails containing K14 acetylation combined with K9 methylation, and that the K9me–K14ac modification defines a novel chromatin state enriched at SETDB1 binding sites.

    • Renata Z. Jurkowska
    • Su Qin
    • Albert Jeltsch
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-13

  • MLL3 and MLL4 are members of the SET1/MLL family of histone H3K4 methyltransferases, which are responsible for monomethylating histone H3K4 on enhancers. Here the authors show that an extended PHD domain (ePHD6) in MLL3 and MLL4 specifically recognizes an H4H18-containing fragment of histone H4, and that modifications of residues surrounding H4H18 modulate H4 binding to MLL3/4.

    • Yanli Liu
    • Su Qin
    • Jinrong Min
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-11

  • HomoFRET sensors based on G6PD homodimerization allow direct sensing of NADPH/NADP+ redox state in living cells. Spectrally tuning the Apollo-NADP+ sensor allows multiplex imaging for studies of oxidative stress in beta cells.

    • William D Cameron
    • Cindy V Bui
    • Jonathan V Rocheleau
    Research
    Nature Methods
    Volume: 13, P: 352-358

  • Harding et al. present a biophysical and structural characterization of the complex between huntingtin (HTT) and HAP40 proteins. They show that the abundance of HAP40 is coupled with that of HTT and that there is greater conformational variety in the exon 1 of the mutant HTT than WT, important for the future drug discovery studies targeting Huntington’s disease.

    • Rachel J. Harding
    • Justin C. Deme
    • Cheryl H. Arrowsmith
    ResearchOpen Access
    Communications Biology
    Volume: 4, P: 1-16

  • A multilaboratory pilot project demonstrates that hybridoma and phage display technologies can be applied to produce high-affinity, high-specificity renewable antibodies to a set of 20 human SH2 domain proteins in a reasonable time frame, suggesting that a systematic, large-scale effort to generate renewable protein binders will be feasible.

    • Karen Colwill
    • Helena Persson
    • Susanne Gräslund
    Research
    Nature Methods
    Volume: 8, P: 551-558