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Showing 1–9 of 9 results
Advanced filters: Author: Charles Bayly-Jones Clear advanced filters

  • Cryo-electron microscopy structures of the human lysosomal transmembrane protein LYCHOS show that it comprises a transporter-like domain fused to a G-protein-coupled receptor, and that the transporter domain is similar to the plant PIN family.

    • Charles Bayly-Jones
    • Christopher J. Lupton
    • Andrew M. Ellisdon
    ResearchOpen Access
    Nature
    Volume: 634, P: 1238-1244

  • Cryo-EM, X-ray crystallography and crosslinking mass spectrometry are harnessed to solve the structure of the full-length Rho-GEF P-Rex1, uncovering a two-layered mechanism of autoinhibition released upon Gβγ and PI(3,4,5)P3 binding.

    • Yong-Gang Chang
    • Christopher J. Lupton
    • Andrew M. Ellisdon
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 29, P: 767-773

  • Cryo-EM and three-dimensional variability analyses reveal the structure of the autoinhibited 640-kDa NF1 dimer, providing a long-sought-after molecular explanation for the extreme sensitivity of the NF1 gene to loss-of function mutation in disease.

    • Christopher J. Lupton
    • Charles Bayly-Jones
    • Andrew M. Ellisdon
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 982-988

  • 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

  • Meprin α is a proteolytic regulator of the extracellular matrix that forms enormous oligomeric filaments of unknown purpose. Here, the authors determine by cryo-EM the structural basis of the meprin supercoiled filament and further characterise a small molecule inhibitor bound to its active site.

    • Charles Bayly-Jones
    • Christopher J. Lupton
    • James C. Whisstock
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-14

  • The PEAK family of pseudokinases is known to play oncogenic roles in poor-prognosis triple negative breast cancer (TNBC). Here this group identifies the role of calcium/calmodulin-dependent protein kinase 2 (CAMK2) in targeting downstream of PEAK1 thereby utilizing RA306 (CAMK2 inhibitor) to effectively attenuate TNBC xenograft growth and block metastasis as well.

    • Xue Yang
    • Xiuquan Ma
    • Roger J. Daly
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-19

  • Cagrilintide is a long-acting agonist of amylin and calcitonin receptors in late phase trials for obesity. Here, authors present structures of cagilintide with each target receptor, revealing the molecular basis for its non-selective action.

    • Jianjun Cao
    • Matthew J. Belousoff
    • Patrick M. Sexton
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • The Complement component 9 (C9) is the pore-forming component of the Membrane Attack Complex which targets pathogens. Here authors use structural biology to compare monomeric C9 to C9 within the polymeric assembly and identify the element which inhibits C9 self-assembly in the absence of the target membrane.

    • Bradley A. Spicer
    • Ruby H. P. Law
    • Michelle A. Dunstone
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-7