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Showing 1–3 of 3 results
Advanced filters: Author: Patricia Yuste-Checa Clear advanced filters
  • The authors reveal a three-domain architecture of glycoprotein clusterin and show that the hydrophobic tails are crucial for clusterin’s functions as an extracellular molecular chaperone and apolipoprotein, as well as for receptor binding and cellular uptake.

    • Patricia Yuste-Checa
    • Alonso I. Carvajal
    • Andreas Bracher
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 32, P: 2035-2045
  • Tau aggregates are associated with several neurodegenerative disorders. In this work, I. Saha and colleagues show that valosin-containing protein (VCP) recruited to Tau fibrils disaggregates them. However, this process comes at a cost: it generates seeding-active Tau species as byproduct.

    • Itika Saha
    • Patricia Yuste-Checa
    • Mark S. Hipp
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-17
  • Variants of the extracellular chaperone Clusterin are associated with Alzheimer’s disease (AD) and Clusterin levels are elevated in AD patient brains. Here, the authors show that Clusterin binds to oligomeric Tau, which enhances the seeding capacity of Tau aggregates upon cellular uptake. They also demonstrate that Tau/Clusterin complexes enter cells via the endosomal pathway, resulting in damage to endolysosomes and entry into the cytosol, where they induce the aggregation of endogenous, soluble Tau.

    • Patricia Yuste-Checa
    • Victoria A. Trinkaus
    • F. Ulrich Hartl
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-15