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Showing 1–17 of 17 results
Advanced filters: Author: David J. Brockwell Clear advanced filters

  • The authors of this work characterize the effect of amino acid substitution on α-synuclein (α-Syn) aggregation. Residues 38 and 42 (in addition to 39) within the P1 region of α-Syn affect amyloid formation. The effect of substitution at position 38 is dependent on the amino-acid introduced, suggesting that specific interactions control α -Syn aggregation.

    • Sabine M. Ulamec
    • Roberto Maya-Martinez
    • David J. Brockwell
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-16

  • Protein aggregation remains a significant challenge for manufacturing of protein biopharmaceuticals. Here, the authors demonstrate the use of directed evolution and an assay for in vivo innate protein aggregation-propensity to generate aggregation-resistant scFv fragments.

    • Jessica S. Ebo
    • Janet C. Saunders
    • David J. Brockwell
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-12

  • Bacterial outer membrane TonB-dependent transporters (TBDTs) mediate the influx of several nutrients. Here the authors use single-molecule force spectroscopy to show that the interaction between TonB andEscherichia coliTBDT BtuB is mechanically resistant to the pulling that gates the BtuB channel.

    • Samuel J. Hickman
    • Rachael E. M. Cooper
    • David J. Brockwell
    ResearchOpen Access
    Nature Communications
    Volume: 8, P: 1-12

  • Dual binding sites are identified in the outer membrane chaperone SurA, providing substrate recognition and mechanistic insights into this ATP-independent chaperone.

    • Bob Schiffrin
    • Joel A. Crossley
    • Anastasia Zhuravleva
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • Fibrous networks constructed from high aspect ratio protein building blocks are ubiquitous in nature, but the functional advantage of such building blocks over globular proteins is not understood. Here, using shear rheology and small-angle neutron scattering, the authors characterise the mechanical and structural properties of photochemically crosslinked protein L and fibrin networks and show that aspect ratio is a crucial property that defines network architecture and mechanics.

    • Matt D. G. Hughes
    • Sophie Cussons
    • Lorna Dougan
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-11

  • The chaperone SurA is involved in outer membrane protein (OMP) biogenesis in Gram-negative bacteria, but its mechanism of action is not fully understood. Combining mass spectrometric, biophysical and computational approaches, the authors here show how the conformational dynamics of SurA facilitate OMP binding.

    • Antonio N. Calabrese
    • Bob Schiffrin
    • Sheena E. Radford
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-16

  • The folding of outer membrane proteins (OMPs) is catalyzed by the βbarrel assembly machinery (BAM). Here, structural and functional analyses of BAM stabilized in distinct conformations elucidate the roles of lateral gate opening and interactions of BAM with the lipid bilayer in OMP assembly.

    • Paul White
    • Samuel F. Haysom
    • Sheena E. Radford
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-13

  • Interferon-ε is a tumour suppressor expressed in the epithelial cell of origin of ovarian cancer, which it restricts by direct action on tumour cells and especially by activation of anti-tumour immunity.

    • Zoe R. C. Marks
    • Nicole K. Campbell
    • Paul J. Hertzog
    Research
    Nature
    Volume: 620, P: 1063-1070

  • Applying an in vivo bacterial-based system for monitoring the influence of small molecules on the aggregation of model amyloid proteins expressed in the periplasm identified dopamine as a new inhibitor of hIAPP aggregation, a protein involved in type 2 diabetes mellitus.

    • Janet C Saunders
    • Lydia M Young
    • Sheena E Radford
    Research
    Nature Chemical Biology
    Volume: 12, P: 94-101

  • Staphylococcal biofilm formation is promoted by the surface protein SasG. Here, the authors characterize the structure and remarkable mechanical strength of the repeat region of SasG, and show how elongation is achieved by obligate folding of the disordered regions within the repeating units.

    • Dominika T. Gruszka
    • Fiona Whelan
    • Jane Clarke
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-9

  • Mass spectrometry, kinetics studies and in silico analyses indicate that multiple copies of the Skp chaperone are required for sequestration of 16-stranded or larger OMPs and prevention of their aggregation.

    • Bob Schiffrin
    • Antonio N Calabrese
    • Sheena E Radford
    Research
    Nature Structural & Molecular Biology
    Volume: 23, P: 786-793

  • The β-barrel assembly machinery (BAM complex) is a key mediator of outer membrane protein biogenesis in Gram-negative bacteria. Here the authors report a cryo-EM structure of the intact BAM complex that suggests that lateral gate opening is a necessary part of the BAM functional cycle.

    • Matthew G. Iadanza
    • Anna J. Higgins
    • Neil A. Ranson
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-12

  • With cryo-EM, single-molecule FRET and MD simulations, Iadanza et al. characterise the membrane protein insertase complex BAM in lipid bilayer nanodiscs. They show that the β-barrel domain of BamA is in a ‘lateral open’ conformation, and that BAM-containing lipid nanodisc deform around BAM’s lateral gate, giving structural evidence for lipid ‘disruptase’ activity of BAM.

    • Matthew G. Iadanza
    • Bob Schiffrin
    • Neil A. Ranson
    ResearchOpen Access
    Communications Biology
    Volume: 3, P: 1-14