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HTS Identification of Activators and Inhibitors of Endoplasmic Reticulum (ER) Stress and the Unfolded Protein Response (UPR)

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 2378))

Abstract

The identification of small molecules and natural product extracts that enhance or interfere with the productivity of protein folding in the endoplasmic reticulum (ER) has the potential to improve a wide variety of human pathologies. Every protein that is destined for a lysosome, integral to the cell membrane, or secreted, is folded, post-translationally modified, and exported to the cytoplasm from the ER-Golgi complex. The following protocols have successfully employed several high-fidelity cell-based luciferase high-throughput screens (HTS) to identify activators and inhibitors of ER stress and the unfolded protein response (UPR).

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Correspondence to Andrew M. Fribley .

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Ghafouri, M., Gauss, C.B., Fribley, A.M. (2022). HTS Identification of Activators and Inhibitors of Endoplasmic Reticulum (ER) Stress and the Unfolded Protein Response (UPR). In: Pérez-Torrado, R. (eds) The Unfolded Protein Response. Methods in Molecular Biology, vol 2378. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1732-8_20

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  • DOI: https://doi.org/10.1007/978-1-0716-1732-8_20

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-1731-1

  • Online ISBN: 978-1-0716-1732-8

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