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Showing 1–9 of 9 results
Advanced filters: Author: Remco Sprangers Clear advanced filters

  • By overcoming the molecular weight limitations that have traditionally hampered quantitative nuclear magnetic resonance spectroscopy (NMR) studies, the dynamics of the 670-kilodalton 20S proteasome core particle have been explored. A selective isotope labelling scheme along with experiments that preserve the lifetimes of the resulting NMR signals reveal functionally important motions and interactions by recording spectra on complexes with molecular weights up to 1 MDa.

    • Remco Sprangers
    • Lewis E. Kay
    Research
    Nature
    Volume: 445, P: 618-622

  • An integrated structural biology approach combining NMR, cryo-EM, X-ray crystallography and molecular dynamics simulations is implemented to characterise the conformational dynamics and interactions of the eukaryotic RNA exosome complex.

    • Jobst Liebau
    • Daniela Lazzaretti
    • Remco Sprangers
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-16

  • The allosteric regulation of the bienzyme complex imidazole glycerol phosphate synthase (HisFH) remains to be elucidated. Here, the authors provide structural insights into the dynamic allosteric mechanism by which ligand binding to the cyclase and glutaminase active sites of HisFH regulate enzyme activation.

    • Jan Philip Wurm
    • Sihyun Sung
    • Remco Sprangers
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-13

  • Processing bodies are membrane less organelles that contain enzymes involved in mRNA turnover, among them enhancer of decapping 3 (Edc3). Here the authors use solid- and solution-state NMR spectroscopy to characterize the structural organization and dynamics of Edc3 and find that its interactions with RNA and between the different Edc3 domains are largely preserved in the phase-separated state.

    • Reinier Damman
    • Stefan Schütz
    • Marc Baldus
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-11

  • Using methyl group and fluorine NMR spectroscopic methods, Overbeck et al revealed that the dynamics of the eukaryotic 5′→3′ exoribonuclease Xrn2 in the region around the active site are correlated with its catalytic activity.

    • Jan H. Overbeck
    • David Stelzig
    • Remco Sprangers
    ResearchOpen Access
    Nature Chemical Biology
    Volume: 18, P: 1152-1160

  • Structural and biochemical studies of scavenger decapping enzyme identify conformational changes induced by substrate binding to a second binding site that occur faster than catalytic turnover, such that high substrate concentrations inhibit enzyme activity.

    • Ancilla Neu
    • Ursula Neu
    • Remco Sprangers
    Research
    Nature Chemical Biology
    Volume: 11, P: 697-704