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Showing 1–11 of 11 results
Advanced filters: Author: Natalya Lukoyanova Clear advanced filters

  • The membrane attack complex is a heteromeric assembly of complement proteins where multiple copies of C9 are recruited by the C5b678 complex to form lytic pores in pathogen membranes. Here the authors present the structure of a soluble pore-like form of the C9 component that reveals details of the oligomerization interfaces.

    • Natalya V. Dudkina
    • Bradley A. Spicer
    • Michelle A. Dunstone
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-6

  • Perforin monomers self-assemble into pre-pores that first insert into the membrane and then recruit additional subunits to grow in size.

    • Carl Leung
    • Adrian W. Hodel
    • Bart W. Hoogenboom
    Research
    Nature Nanotechnology
    Volume: 12, P: 467-473

  • Natural killer cells and cytotoxic T cells kill virus-infected and malignant cells, releasing the pore-forming protein perforin in the process. Perforin is required for the delivery of pro-apoptotic granzymes to the target cell. These authors present the crystal structure of a perforin monomer together with a cryo-electron microscopy reconstruction of the oligomeric pore. Perforin monomers within the pore are arranged with an inside-out orientation relative to the structurally homologous monomers of cholesterol-dependent cytolysins.

    • Ruby H. P. Law
    • Natalya Lukoyanova
    • James C. Whisstock
    Research
    Nature
    Volume: 468, P: 447-451

  • Numerous viruses use a portal system for dsDNA entry and exit from their capsid. Here the authors report the atomic structure of phage SPP1 portal DNA gatekeeper and its mechanism of assembly. They also identify evolution breakpoints between different tailed bacteriophages morphotypes and herpesviruses.

    • Igor Orlov
    • Stéphane Roche
    • Elena V. Orlova
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12

  • Cryo-electron microscopy structures of a 2.8 megadalton bacterial type IV secretion system encoded by the plasmid R388 and comprising 92 polypeptides provide insights into the stepwise mechanism of pilus assembly.

    • Kévin Macé
    • Abhinav K. Vadakkepat
    • Gabriel Waksman
    ResearchOpen Access
    Nature
    Volume: 607, P: 191-196

  • Understanding the structural basis for the inhibition of archaeal eukaryotic-like RNA polymerases (RNAPs) during virus infection is of interest for drug design. Here, the authors present the cryo-EM structures of apo Sulfolobus acidocaldarius RNAP and the RNAP complex structures with two regulatory factors, RIP and TFS4 that inhibit transcription and discuss their inhibitory mechanisms.

    • Simona Pilotto
    • Thomas Fouqueau
    • Finn Werner
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-15

  • A membrane-embedded complex (called T4CC) is essential for injection of Legionella pneumophila effector proteins into human macrophages via a Type IV secretion system. Here, the authors purify and study the T4CC using functional and cryo-EM structural analyses, providing insights into the secretion mechanisms.

    • Amit Meir
    • Kevin Macé
    • Gabriel Waksman
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-11

  • The insecticidal protein Mpf2Ba1 shows potent control against corn rootworm. Here, the authors present detailed structural analyses revealing transitions between its three main stages of pore formation. These findings uncover molecular mechanisms of bacterial pore assembly and advance both crop biotechnology and food security.

    • Guendalina Marini
    • Brad Poland
    • Helen R. Saibil
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-11

  • The cryo-EM structure of budding yeast supercomplex III2IV2 is now presented, providing molecular details of CIV (also known as cytochrome c oxidase) and revealing notable differences with mammalian systems.

    • Andrew M. Hartley
    • Natalya Lukoyanova
    • Amandine Maréchal
    Research
    Nature Structural & Molecular Biology
    Volume: 26, P: 78-83