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Showing 1–6 of 6 results
Advanced filters: Author: "Claudio Hetz" Clear advanced filters

  • Understanding the mechanisms that determine cell fate under endoplasmic reticulum (ER) stress had been hampered by the lack of models to study unfolded protein response (UPR) adaptive phases. The development of an engineered protein to conditionally induce its misfolding allowed the establishment of a resolvable ER stress condition.

    • Danilo B Medinas
    • Claudio Hetz
    News & Views
    Nature Chemical Biology
    Volume: 10, P: 879-880

  • The unfolded protein response (UPR) buffers protein-folding stress at the endoplasmic reticulum (ER). Research has provided insight into the regulatory mechanisms of UPR branches initiated by the stress sensors protein kinase RNA-like ER kinase (PERK), inositol-requiring protein 1α (IRE1α) and activating transcription factor 6 (ATF6), and into outcomes of the UPR that are not directly related to protein misfolding.

    • Claudio Hetz
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 13, P: 89-102

  • The unfolded protein response (UPR) is a homeostatic mechanism by which cells regulate levels of misfolded proteins in the endoplasmic reticulum (ER). Here, Hetz and Mollereau provide an overview of the most recent findings addressing the relevance of ER stress in the nervous system.

    • Claudio Hetz
    • Bertrand Mollereau
    Reviews
    Nature Reviews Neuroscience
    Volume: 15, P: 233-249

  • Accumulation of misfolded protein in neurons is a common feature of many neurodegenerative diseases. In this Review, Hetz and Saxena discuss the latest advances in our understanding about the mechanisms by which protein misfolding causes neurodegeneration, and look at novel insights into the role of cellular responses to protein misfolding in synaptic function and in inflammatory and mechanical injury in the nervous system.

    • Claudio Hetz
    • Smita Saxena
    Reviews
    Nature Reviews Neurology
    Volume: 13, P: 477-491

  • Stress induced by the accumulation of unfolded proteins in the endoplasmic reticulum (ER) is observed in many diseases, including cancer, diabetes and neurodegenerative disorders. Cellular adaptation to ER stress is achieved by the activation of the unfolded protein response (UPR). Hetz and colleagues discuss the opportunities to modulate components of UPR signalling to therapeutically manipulate levels of ER stress in disease.

    • Claudio Hetz
    • Eric Chevet
    • Heather P. Harding
    Reviews
    Nature Reviews Drug Discovery
    Volume: 12, P: 703-719