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Showing 1–16 of 16 results
Advanced filters: Author: David J. Schiffrin Clear advanced filters

  • 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

  • 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

  • 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

  • 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 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

  • 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

    • John D. Baxter
    • John A. Lewicki
    • David G. Gardner
    Reviews
    Bio/Technology
    Volume: 6, P: 529-546

  • Endothelin-1 (ET-1) is a potent vasoactive peptide that is produced by various cell types of the kidney and regulates a variety of physiological processes. This Review describes the role of ET-1 in the kidney and in the development of chronic kidney disease, and the kidney-protective effects of endothelin-receptor antagonists in preclinical and clinical studies.

    • J. David Smeijer
    • Donald E. Kohan
    • Hiddo J. L. Heerspink
    Reviews
    Nature Reviews Nephrology
    Volume: 21, P: 175-188

  • 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

  • Endothelin 1 is the most potent vasoconstrictor in the human cardiovascular system. In this Review, Dhaun and Webb discuss the biology of the endothelins and endothelin receptors and how these pathways can be therapeutically targeted in cardiovascular and renal diseases.

    • Neeraj Dhaun
    • David J. Webb
    Reviews
    Nature Reviews Cardiology
    Volume: 16, P: 491-502