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 1–14 of 14 results
Advanced filters: Author: David Haselbach Clear advanced filters

  • The proteasome regulates several important cellular processes and has been identified as a target for therapeutic interventions. Here the authors map the conformational and energy landscape of the 26S proteasome upon Oprozomib binding and uncover long-range allosteric effects that control the dynamic behaviour of the proteasome.

    • David Haselbach
    • Jil Schrader
    • Holger Stark
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-8

  • Usnic acid is a lichen secondary metabolite and has a antitumor activity. Here the authors show that usnic acid rapidly blocks large ribosomal subunit formation. This hinders pre-rRNA processing and leads to depletion of key maturation factors such as Dbp10.

    • Lisa Kofler
    • Lorenz Grundmann
    • Helmut Bergler
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-17

  • Here, using cryogenic electron microscopy and cryoDRGN, the authors delineate how the anaphase-promoting complex/cyclosome is reconfigurated to interact with its cognate E2s and thus polyubiquitinate its target. Unexpectedly, multiple ubiquitin moieties are shown to interact with the anaphase-promoting complex/cyclosome machinery, including its activator Cdh1.

    • Tatyana Bodrug
    • Kaeli A. Welsh
    • Nicholas G. Brown
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 30, P: 1663-1674

  • The AAA-ATPase Drg1 is a key factor in eukaryotic ribosome biogenesis that initiates cytoplasmic maturation of the large subunit. Here the authors report the structure of Drg1 in complex with its specific inhibitor diazaborine and provide insight into the mechanism of inhibition and specificity of this class of inhibitors.

    • Michael Prattes
    • Irina Grishkovskaya
    • Helmut Bergler
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • Mass photometry is a label-free optical approach capable of detecting, imaging and accurately measuring the mass of single biomolecules in solution. Here, the authors demonstrate the potential of mass photometry for quantitatively characterizing sample heterogeneity of purified protein complexes with implications for structural studies specifically and in vitro studies more generally.

    • Adar Sonn-Segev
    • Katarina Belacic
    • Philipp Kukura
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • Mass spectrometry and structural studies demonstrate the specific changes in protein composition that accompany the transition of ribosomes in zebrafish and Xenopus eggs from a dormant to an active state during early embryogenesis.

    • Friederike Leesch
    • Laura Lorenzo-Orts
    • Andrea Pauli
    Research
    Nature
    Volume: 613, P: 712-720

  • The AAA-ATPase Drg1 assembles at the pre-60S ribosomal particle to release the ribosomal maturation factor Rlp24. Here, single-particle cryo-EM and 3D variability analysis dynamically visualize Rlp24 release by hand-over-hand substrate translocation.

    • Michael Prattes
    • Irina Grishkovskaya
    • Helmut Bergler
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 942-953

  • The full-length structure of HUWE1 reveals the bipartite organization of a giant E3 ubiquitin ligase, comprising a catalytic HECT domain and a large, ring-shaped scaffold that provides docking sites for various substrates and regulates E3 activity.

    • Daniel B. Grabarczyk
    • Olga A. Petrova
    • Tim Clausen
    Research
    Nature Chemical Biology
    Volume: 17, P: 1084-1092

  • 3D Flexible Refinement (3DFlex) is a generative neural network model for continuous molecular heterogeneity for cryo-EM data that can be used to determine the structure and motion of flexible biomolecules. It enables visualization of nonrigid motion and improves 3D structure resolution by aggregating information from particle images spanning the conformational landscape of the target molecule.

    • Ali Punjani
    • David J. Fleet
    ResearchOpen Access
    Nature Methods
    Volume: 20, P: 860-870