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Showing 1–14 of 14 results
Advanced filters: Author: Bart W. Hoogenboom Clear advanced filters

  • The antibiotic polymyxin B requires bacterial metabolic activity to cause sufficient damage to the outer membrane to access the inner membrane, which it permeabilizes via an energy-independent mechanism to kill the cell.

    • Carolina Borrelli
    • Edward J. A. Douglas
    • Bart W. Hoogenboom
    ResearchOpen Access
    Nature Microbiology
    Volume: 10, P: 2919-2933

  • The structure-function relationships of a β-helix, a folding motif formed by parallel β-strands arranged in a helical repetitive pattern, remain poorly understood and underexploited. Here, the authors reconstitute a protein β-helix by design from an elementary sequence of 18 amino acids, which self-assembles into a self-contained multifunctional motif exhibiting a range of biological functions.

    • Camilla Dondi
    • Javier Garcia-Ruiz
    • Maxim G. Ryadnov
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-18

  • Cytotoxic T lymphocytes (CTLs) eliminate virus-infected and cancerous cells by secreting the pore-forming protein (perforin) and pro-apoptotic serine proteases (granzymes). Here authors show that two mechanisms protect the membranes of CTLs from disruption by perforin and granzymes.

    • Jesse A. Rudd-Schmidt
    • Adrian W. Hodel
    • Ilia Voskoboinik
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-13

  • The membrane attack complex (MAC) is a hetero-oligomeric protein assembly that kills pathogens by perforating their cell envelopes. Here, the authors use atomic force microscopy to show that MAC proteins oligomerize within the membrane, allowing them to identify the kinetic bottleneck of MAC formation.

    • Edward S. Parsons
    • George J. Stanley
    • Bart W. Hoogenboom
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-10

  • 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

  • Macrophage-expressed gene 1 (MPEG1) functions within the phagolysosome to damage engulfed microbes, presumably via forming pores in target membranes. In order to provide insights into the mechanism of MPEG1 function and membrane binding, the authors present structures of hexadecameric MPEG1 prepores both in solution and in complex with liposomes.

    • Siew Siew Pang
    • Charles Bayly-Jones
    • James C. Whisstock
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-9

  • Cholesterol-dependent cytolysins (CDCs) are bacterial pore-forming virulence factors. Cryo-EM structure of an early conformation of the CDC ILY from Streptococcus intermedius, bound to the human immune receptor CD59, provides insight into ILY oligomerization and role of cholesterol in membrane lysis.

    • Nita R. Shah
    • Tomas B. Voisin
    • Doryen Bubeck
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • With the growing threat of antibiotic resistance, unconventional approaches to antimicrobial discovery are needed. Here, the authors present a peptide topology that mimics virus architecture and assembles into antimicrobial capsids that disrupt bacterial membranes upon contact.

    • Emiliana De Santis
    • Hasan Alkassem
    • Maxim G. Ryadnov
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-11

  • Atomic force microscopy (AFM) is unique in visualizing functional biomolecules in aqueous solution at ~1 nm resolution. By borrowing localization methods from fluorescence microscopy, AFM has been shown to discern structural domains that may be separated by only a few Ångströms.

    • Bart W. Hoogenboom
    News & Views
    Nature Structural & Molecular Biology
    Volume: 28, P: 629-630

  • In cells, DNA is arranged into topologically-constrained (supercoiled) structures, but how this supercoiling affects the detailed double-helical structure of DNA remains unclear. Here authors use atomic force microscopy and atomistic molecular dynamics simulations, to resolve structures of negatively-supercoiled DNA minicircles at base-pair resolution.

    • Alice L. B. Pyne
    • Agnes Noy
    • Sarah A. Harris
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12