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Showing 1–21 of 21 results
Advanced filters: Author: A. Guskov Clear advanced filters
  • The pathogen Pseudomonas aeruginosa uses a membrane complex, PelBC, to produce exopolysaccharides for biofilm formation. Here the authors combine structural analysis, simulations and single-channel recordings of PelBC to provide a detailed view on its unique architecture and dynamics, and reveal the export route for the polysaccharide.

    • Marius Benedens
    • Cristian Rosales-Hernandez
    • Alexej Kedrov
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-16
  • While Bell inequalities have been violated several times—mostly in photonic systems—their violations within particle physics experiments are less explored. Here, the BESIII Collaboration showcases Bell-violating nonlocal correlations between entangled hyperon pairs.

    • M. Ablikim
    • M. N. Achasov
    • J. Zu
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-9
  • Glutamate transporters are membrane transporters that clear the neurotransmitter L-glutamate from the synaptic cleft via a so-called elevator mechanism. Here the authors present five cryo-EM structures of the transporter homologue GltTk, which explain how substrate leakage is prevented.

    • Valentina Arkhipova
    • Albert Guskov
    • Dirk J. Slotboom
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-9
  • A cryo-EM structure of the human SLC1 transporter ASCT2 in the inward-facing conformation reveals the retrovirus-docking site and helps to elucidate the transport cycle. The transport domain is more solvent exposed than in most of the homolog structures.

    • Alisa A. Garaeva
    • Gert T. Oostergetel
    • Dirk J. Slotboom
    Research
    Nature Structural & Molecular Biology
    Volume: 25, P: 515-521
  • The bacterial zinc transporter ZntB is important for maintaining zinc homeostasis and is mechanistically not well understood. Here, the authors present the cryo-EM structure of ZntB at 4.2 Å resolution, perform transport assays and propose a model for its Zn2+ transport mechanism.

    • Cornelius Gati
    • Artem Stetsenko
    • Albert Guskov
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-8
  • Prokaryotes use energy-coupling factor transporters to uptake required micronutrients and an unusual toppling mechanism has been proposed for their function. Here, the authors provide structural support for this mechanism, allowing direct visualization of the toppled state.

    • Lotteke J. Y. M. Swier
    • Albert Guskov
    • Dirk J. Slotboom
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-11
  • Light-driven sodium-pumping rhodopsins are unique ion transporters. Here, authors present a characterization of such rhodopsins with a modified active center allowing for efficient sodium transport under various environmental conditions.

    • E. Podoliak
    • G. H. U. Lamm
    • K. Kovalev
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16
  • When bacteria enter the stationary growth phase, protein translation is suppressed via the dimerization of 70S ribosomes into inactive complexes. Here the authors provide a structural basis for how the dual domain hibernation promotion factor promotes ribosome dimerization and hibernation in bacteria.

    • Linda E. Franken
    • Gert T. Oostergetel
    • Albert Guskov
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-11
  • The semileptonic decay channels of the Λc baryon can give important insights into weak interaction, but decay into a neutron, positron and electron neutrino has not been reported so far, due to difficulties in the final products’ identification. Here, the BESIII Collaboration reports its observation in e+e- collision data, exploiting machine-learning-based identification techniques.

    • M. Ablikim
    • M. N. Achasov
    • J. Zu
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-12
  • How the human Alanine Serine Cysteine Transporter 2 (ASCT2) binds its substrates, neutral amino acids, and releases them on the cytoplasmic side remains unclear. Here authors present an inward-open structure of the human ASCT2 which shows that a hairpin serves as a gate in the inward-facing state.

    • Alisa A. Garaeva
    • Albert Guskov
    • Cristina Paulino
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-8
  • Investigating the inner structure of baryons is important to further our understanding of the strong interaction. Here, the BESIII Collaboration extracts the absolute value of the ratio of the electric to magnetic form factors and its relative phase for e + e − → J/ψ → ΛΣ decays, enhancing the signal thanks to the vacuum polarisation effect at the J/ψ peak.

    • M. Ablikim
    • M. N. Achasov
    • J. Zu
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-9
  • Uptake of vitamin B12 is essential for many prokaryotes, but in most cases the membrane proteins involved are yet to be identified. Here, the authors use X-ray crystallography and spectroscopy to characterize BtuM, a predicted bacterial substrate-modifying vitamin B12 transporter.

    • S. Rempel
    • E. Colucci
    • D. J. Slotboom
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-8
  • Using spin-entangled baryon–antibaryon pairs, the BESIII Collaboration reports on high-precision measurements of potential charge conjugation and parity (CP)-symmetry-violating effects in hadrons.

    • M. Ablikim
    • M. N. Achasov
    • J. H. Zou
    ResearchOpen Access
    Nature
    Volume: 606, P: 64-69
  • Form factors encode the structure of nucleons. Measurements from electron–positron annihilation at BESIII reveal an oscillating behaviour of the neutron electromagnetic form factor, and clarify a long-standing photon–nucleon interaction puzzle.

    • M. Ablikim
    • M. N. Achasov
    • J. H. Zou
    Research
    Nature Physics
    Volume: 17, P: 1200-1204
  • Trinco et al. measure aspartate uptake rates in proteoliposomes containing purified prokaryotic Na+-coupled aspartate transporter GltTk. To overcome limitation of protein orientation, they use synthetic nanobody that blocks transporters from outside and reveal mechanistic features of Na+-aspartate symport that cannot be observed in detergent solution.

    • Gianluca Trinco
    • Valentina Arkhipova
    • Dirk J. Slotboom
    ResearchOpen Access
    Communications Biology
    Volume: 4, P: 1-11