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Showing 1–4 of 4 results
Advanced filters: Author: Doris Hellerschmied Clear advanced filters

  • BiP–glucose-regulated protein 94 chaperones are critical to the proper folding of secretory and transmembrane proteins. Brenner et al. provide biochemical and structural insight into a conserved mechanism of chaperone cooperation underlying this quality control process.

    • Joel Cyrille Brenner
    • Linda Charlotte Zirden
    • Doris Hellerschmied
    ResearchOpen Access
    Nature Structural & Molecular Biology
    P: 1-12

  • Myosin, a motor protein essential for intracellular transport to muscle contraction, requires a chaperone UNC-45 for folding and assembly. Here authors use in vitro reconstitution and structural biology to characterize the interplay between UNC-45 and muscle myosin MHC-B.

    • Doris Hellerschmied
    • Anita Lehner
    • Tim Clausen
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-14

  • The targeted development of proteome-wide selective covalent probes remains a challenge. Here, the authors show the exploration of the natural product Sulphostin as a starting point for dipeptidyl peptidase 8 and 9 inhibitor development.

    • Leonard Sewald
    • Werner W. A. Tabak
    • Markus Kaiser
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • The U-box ubiquitin ligase UFD-2 is one of the most abundant components of the ubiquitin proteasome system in muscle cells. Here the authors perform in vitro and in vivo experiments and show that UFD-2 has E3 ligase activity and that it ubiquitinates unfolded myosin using the C. elegans myosin chaperone UNC-45 as an adaptor protein.

    • Doris Hellerschmied
    • Max Roessler
    • Tim Clausen
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-15