Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–5 of 5 results
Advanced filters: Author: Anna Plechanovová Clear advanced filters

  • Structural analyses capture RING E3 ligase RNF4 bound to Ube2V2–Ubc13 E2 complex charged with ubiquitin and, along with functional assays, reveal the basis for synthesis of K63-linked chains.

    • Emma Branigan
    • Anna Plechanovová
    • Ronald T Hay
    Research
    Nature Structural & Molecular Biology
    Volume: 22, P: 597-602

  • SUMO forms flexible polymeric chains that can interact with ubiquitin ligases, such as RNF4. Here Xu et al. have used NMR spectroscopy and biochemical experiments to investigate the interaction between SUMO and RNF4, and propose a mechanism for delivery of substrates to the ubiquitination machinery.

    • Yingqi Xu
    • Anna Plechanovová
    • Steve J. Matthews
    ResearchOpen Access
    Nature Communications
    Volume: 5, P: 1-12

  • RNF4 is a prototypical single-subunit E3 enzyme that can bind both substrate and ubiquitin-loaded E2. Here, the authors show that the RNF4 N-terminal region, although lacking a defined secondary structure, maintains a compact global conformation to facilitate ubiquitin transfer to the substrate.

    • Paul Murphy
    • Yingqi Xu
    • Ronald T. Hay
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-13

  • This study presents the crystal structure of a RING-type E3 ligase bound to ubiquitin-loaded E2; the structure reveals how ubiquitin binding to E2 leads to changes in the catalytic site, priming it for catalysis by the E3 enzyme.

    • Anna Plechanovová
    • Ellis G. Jaffray
    • Ronald T. Hay
    Research
    Nature
    Volume: 489, P: 115-120

  • RNF4 is an E3 ligase involved in ubiquitinating poly-SUMOylated proteins. The structure of the RNF4 dimer, along with modeling and functional analyses, now indicate that the dimer itself, rather than acting as a scaffold, plays a specific role in recognition by binding the E2~ubiquitin thioester and activating it for catalysis.

    • Anna Plechanovová
    • Ellis G Jaffray
    • Ronald T Hay
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 1052-1059