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 1–6 of 6 results
Advanced filters: Author: Bernhard C. Lechtenberg Clear advanced filters

  • A novel antiviral targeting the SARS-CoV-2 PLpro protease shows strong efficacy in a mouse model, preventing lung pathology and reducing brain dysfunction. The study provides proof-of-principle that PLpro inhibition may be a viable strategy for preventing and treating long COVID.

    • Stefanie M. Bader
    • Dale J. Calleja
    • David Komander
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-20

  • RBR E3 ubiquitin ligases utilise a 2-step catalytic mechanism previously defined for only few of the RBR family members. Here, the authors examine the poorly studied RBRs HOIL-1 and RNF216 to define general principles of RBR catalysis and regulation and identify specific functional differences.

    • Xiangyi S. Wang
    • Thomas R. Cotton
    • Bernhard C. Lechtenberg
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-17

  • Eph receptor tyrosine kinases and their ephrin ligands mediate cell-cell communication. Here, the authors assess the structure and dynamics of the EphA2 intracellular region and uncover complex effects of phosphorylation within the linker region between EphA2 kinase and SAM domains.

    • Bernhard C. Lechtenberg
    • Marina P. Gehring
    • Elena B. Pasquale
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-16

  • The PEAK family of pseudokinases are key hubs in cellular signalling, including cell motility and cancer. Here, the authors characterise how PEAK proteins interact with the adapter proteins CrkII and Grb2 and regulatory scaffold protein 14-3-3, to achieve functional signalling assemblies.

    • Michael J. Roy
    • Minglyanna G. Surudoi
    • Isabelle S. Lucet
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-19

  • The modification of proteins with the small protein ubiquitin constitutes a Daedalian system of posttranslational modifications in every eukaryotic cell, which is often referred to as the ubiquitin code1. Here we consider the scale and complexity of the ubiquitin system in light of recent developments.

    • Bernhard C. Lechtenberg
    • David Komander
    Comments & Opinion
    Nature Structural & Molecular Biology
    Volume: 31, P: 210-213

  • The first structure of fully active HOIP of the RBR family of RING-type E3 ligases in its transfer complex with an E2~ubiquitin conjugate provides insights into its mechanism of action, including the ideal alignment of the E2 and E3 catalytic centres for ubiquitin transfer and the allosteric regulation of the RBR family.

    • Bernhard C. Lechtenberg
    • Akhil Rajput
    • Stefan J. Riedl
    Research
    Nature
    Volume: 529, P: 546-550