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Showing 1–8 of 8 results
Advanced filters: Author: Chloé Martens Clear advanced filters

  • Substrate binding to the multidrug exporter LmrP from Lactococcus lactis catalyzes proton entrance by stabilizing an outward-open conformation. Transitions between conformational states are dictated by proton passage down the transmembrane helical bundle.

    • Matthieu Masureel
    • Chloé Martens
    • Cédric Govaerts
    Research
    Nature Chemical Biology
    Volume: 10, P: 149-155

  • A crystal structure of bacterial multidrug transporter LmrP reveals the presence of a lipid inside the substrate binding cavity, with MD simulations and mutational analyses suggesting it could be involved in broad substrate specificity.

    • Vincent Debruycker
    • Andrew Hutchin
    • Cédric Govaerts
    Research
    Nature Structural & Molecular Biology
    Volume: 27, P: 829-835

  • The antiphage defence protein CapRelSJ46 in Escherichia coli can directly bind and sense two completely unrelated and structurally different proteins using the same sensory domain, with overlapping but distinct interfaces.

    • Tong Zhang
    • Albinas Cepauskas
    • Michael T. Laub
    ResearchOpen Access
    Nature
    Volume: 635, P: 728-735

  • The authors report a particle-particle correlation and velocity-difference profile method to measure nuclear lifetime. The results obtained for excited states of 23Mg are used to constrain the production of 22Na in the astrophysical novae explosions.

    • Chloé Fougères
    • François de Oliveira Santos
    • Magdalena Zielińska
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-7

  • Tissue-resident macrophages are mostly derived from embryonic progenitors. Scott et al. develop a mouse model to specifically deplete Kupffer cells (KC) in vivoand show that monocyte-derived cells can repopulate KC niche and behave similar to their embryonically-derived counterparts.

    • Charlotte L. Scott
    • Fang Zheng
    • Martin Guilliams
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-10

  • The cystic fibrosis transmembrane conductance regulator anion channel can adopt an alternate conformation of its nucleotide-binding domain, which affects channel activity and, under certain conditions, leads to unfolding and protein degradation.

    • Daniel Scholl
    • Maud Sigoillot
    • Cédric Govaerts
    Research
    Nature Chemical Biology
    Volume: 17, P: 989-997

  • EPR spectroscopy analyses elucidate how lipids affect the conformational dynamics of a multidrug secondary transporter, LmrP, and indicate a key role of the lipid headgroups in shaping the conformational-energy landscape of the transporter.

    • Chloé Martens
    • Richard A Stein
    • Hassane S Mchaourab
    Research
    Nature Structural & Molecular Biology
    Volume: 23, P: 744-751