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Showing 1–14 of 14 results
Advanced filters: Author: Matthieu Masureel Clear advanced filters

  • NADPH oxidase NOX2 produces superoxide, a reactive oxygen species essential in innate immunity. Here, the authors reveal the structure of the NOX2 core, rationalize disease-causing mutations, and suggest avenues for selective NOX2 pharmacological modulation.

    • Sigrid Noreng
    • Naruhisa Ota
    • James T. Koerber
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-11

  • Single-molecule FRET imaging provides insights into the allosteric link between the ligand-binding and G-protein nucleotide-binding pockets of the β2 adrenergic receptor (β2AR) and improved understanding of the G-protein activation mechanism.

    • G. Glenn Gregorio
    • Matthieu Masureel
    • Scott C. Blanchard
    Research
    Nature
    Volume: 547, P: 68-73

  • 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

  • The molecular heterogeneity of glycosylated biotherapeutics often complicates analysis by intact mass spectrometry. Here, the authors propose a simplified procedure for characterization that employs proton transfer charge reduction. Integration with glycomic and glycopeptide datasets can further provide glycoform-level information.

    • Luis F. Schachner
    • Christopher Mullen
    • Wendy Sandoval
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-13

  • 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

  • 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

  • Transient engagement of the G protein-coupled receptor core can act as a catalyst to activate cellular β-arrestin function after dissociation from the receptor.

    • Kelsie Eichel
    • Damien Jullié
    • Mark von Zastrow
    Research
    Nature
    Volume: 557, P: 381-386

  • In this Review, the authors discuss recent insights into the mechanism of GPCR signaling provided by structural and biophysical elucidation of receptor interactions with G proteins and arrestins.

    • Daniel Hilger
    • Matthieu Masureel
    • Brian K. Kobilka
    Reviews
    Nature Structural & Molecular Biology
    Volume: 25, P: 4-12

  • Here, pharmacological and biochemical evidence is provided that shows that G-protein coupling to the β2-adrenergic receptor stabilizes a ‘closed’ conformation of the G-protein-coupled receptor (GPCR) and that that the effects of the G protein on the ligand-binding site of the GPCR are observed even in the absence of a bound agonist.

    • Brian T. DeVree
    • Jacob P. Mahoney
    • Roger K. Sunahara
    Research
    Nature
    Volume: 535, P: 182-186