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Showing 1–6 of 6 results
Advanced filters: Author: Brandon H Toyama Clear advanced filters

  • A comprehensive structural analysis of the complete and unmodified Sup35 prion domain in two distinct infectious conformations is presented. A variety of techniques is used to provide structural details of these two prion conformations, one weakly and one strongly propagating strain. The data show that the fibril conformation of both strains share a common amyloid-like core, comprising the glutamine/asparagine rich first 40 residues.

    In the weaker strain this stable structure is dramatically expanded to 70 amino acids.

    • Brandon H. Toyama
    • Mark J. S. Kelly
    • Jonathan S. Weissman
    Research
    Nature
    Volume: 449, P: 233-237

  • An increasing number of proteins have been discovered that evade turnover and instead are maintained over a cell's lifetime. Accumulation of damage in these long-lived proteins may contribute to the ageing process.

    • Brandon H. Toyama
    • Martin W. Hetzer
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 14, P: 55-61

  • An analytical model describes how the interplay of various physical parameters of prions and prion particles in yeast leads to the emergence of a particular prion strain. The ability of prion particles to divide and generate new seeds for further growth turns out to be a key determinant of their physiological impact.

    • Motomasa Tanaka
    • Sean R. Collins
    • Jonathan S. Weissman
    Research
    Nature
    Volume: 442, P: 585-589

  • [PSI+] is a well-studied prion from budding yeast. Here the dominant-negative effects of mutation G58D are found to depend on the prion conformation. Moreover, the curing effect of G58D on one particular prion conformation is attributed to an impact on the delivery of infectious particles from the mother to the daughter cells.

    • Katherine J Verges
    • Melanie H Smith
    • Jonathan S Weissman
    Research
    Nature Structural & Molecular Biology
    Volume: 18, P: 493-499

  • The prion strain phenomenon states that distinct amyloid conformations with different phenotypes and heritable states can arise from a single polypeptide. The decision about amyloid conformation is made at the level of the initial nucleus, where different nuclei will lead to different conformations.

    • Yumiko Ohhashi
    • Kazuki Ito
    • Motomasa Tanaka
    Research
    Nature Chemical Biology
    Volume: 6, P: 225-230