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

Autor:	Ghafouri M; Carman and Ann Adams Department of Pediatrics, Wayne State University School of Medicine, Detroit, MI, USA., Gauss CB; Carman and Ann Adams Department of Pediatrics, Wayne State University School of Medicine, Detroit, MI, USA., Fribley AM; Carman and Ann Adams Department of Pediatrics, Wayne State University School of Medicine, Detroit, MI, USA. afribley@med.wayne.edu.; Department of Otolaryngology-Head and Neck Surgery, Wayne State University School of Medicine, Detroit, MI, USA. afribley@med.wayne.edu.; Molecular Therapeutics Program, Barbara Ann Karmanos Cancer Institute, Detroit, MI, USA. afribley@med.wayne.edu.
Jazyk:	angličtina
Zdroj:	Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2022; Vol. 2378, pp. 317-327.
DOI:	10.1007/978-1-0716-1732-8_20
Abstrakt:	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). (© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.)
Databáze:	MEDLINE
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