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Showing 1–7 of 7 results
Advanced filters: Author: Elena Seiradake Clear advanced filters

  • Activation of neutrophil leukocytes is tightly regulated, and it is important to understand the molecular mechanisms of their response to physiological and pathological stimuli. Here authors show that the adhesion molecule G protein-coupled receptor 97 and its interaction partners play pivotal roles in neutrophil leukocyte activation both in anti-microbial response and in inflammatory diseases.

    • Tai-Ying Chu
    • Céline Zheng-Gérard
    • Hsi-Hsien Lin
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-16

  • FLRT proteins are known to interact with Lphns and Unc5s, mediating cell adhesion and repulsion respectively. Here the authors use crystallography, native mass spectrometry, molecular dynamics simulations and cell-based assays to show that these three proteins form large super-complexes with functions distinct from their smaller subcomplexes.

    • Verity A. Jackson
    • Shahid Mehmood
    • Elena Seiradake
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-13

  • Teneurins are cell-cell adhesion receptors that evolved through horizontal gene transfer in which a bacterial YD-repeat protein fused to a eukaryotic receptor. Here the authors present crystallographic and cryo-EM structures of two Teneurins, revealing an ancient YD-repeat protein super-fold.

    • Verity A. Jackson
    • Dimphna H. Meijer
    • Elena Seiradake
    ResearchOpen Access
    Nature Communications
    Volume: 9, P: 1-9

  • Eph receptors are cell surface protein tyrosine kinases that mediate cell-cell communication. The crystal structure of the full ectodomain of unliganded human EphA2 (eEphA2) reveals that it forms linear arrays of staggered, parallel receptors, whereas that of eEphA2 in complex with ephrinA5 forms a more elaborate assembly with interfaces that are crucial for localization at cell-cell contacts and for activation-dependent degradation.

    • Elena Seiradake
    • Karl Harlos
    • E Yvonne Jones
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 398-402

  • Given the high degree of similarity between Eph receptors, it has remained unclear how the same ligand can produce different signaling outcomes. The crystal structures of apo and ligand-bound EphA4, combined with cellular assays with chimeric ectodomains, now indicate that the specificity of signaling outcome is largely dictated by clustering properties structurally encoded within the ectodomain.

    • Elena Seiradake
    • Andreas Schaupp
    • E Yvonne Jones
    Research
    Nature Structural & Molecular Biology
    Volume: 20, P: 958-964