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Showing 1–6 of 6 results
Advanced filters: Author: A. Elisabeth Sauer-Eriksson Clear advanced filters

  • Systemic ATTR amyloidosis causes the abnormal accumulation of ATTR fibrils formed from the human plasma protein transthyretin (TTR) in multiple organs including the eye. Here, the authors present a 3.2 Å cryo-EM structure of an ATTR fibril isolated from the vitreous body of an ATTR patient’s eye and discuss the mechanism for the structural conversion of TTR into a fibrillar form.

    • Irina Iakovleva
    • Michael Hall
    • A. Elisabeth Sauer-Eriksson
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-10

  • The signal recognition particle plays a key role in the co-translational protein targeting of membrane and secretory proteins. Here the authors report a crystal structure of the ternary SRP complex in signal sequence bound and unbound forms, providing insight into how signal sequence binding is coupled to SRP receptor interaction.

    • Tobias Hainzl
    • A. Elisabeth Sauer-Eriksson
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-7

  • The first X-ray crystal structure of the catalytic core of Saccharomyces cerevisiae DNA polymerase ɛ with a primed DNA template and an incoming dNTP reveals a new 'P domain' that encircles the DNA and contributes to the high processivity of this replicative polymerase.

    • Matthew Hogg
    • Pia Osterman
    • Erik Johansson
    Research
    Nature Structural & Molecular Biology
    Volume: 21, P: 49-55

  • The signal sequence on nascent peptides is recognized by the signal recognition particle (SRP), with subsequent targeting of the SRP-ribosomal nascent complex to the membrane. The structure of a signal sequence bound to the core SRP is presented, revealing structural changes in the SRP upon signal sequence binding.

    • Tobias Hainzl
    • Shenghua Huang
    • A Elisabeth Sauer-Eriksson
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 389-391

  • Adenylate kinase (AdK) plays a key role in cellular energy homeostasis by catalysing the reversible magnesium-dependent formation of ADP from AMP and ATP. Here the authors present a detailed analysis of adenylate kinase’s conformational dynamics and characterize a high-energy state of AdK indispensable for catalysis.

    • Michael Kovermann
    • Jörgen Ådén
    • Magnus Wolf-Watz
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-9