ER Stress and Disease: Toward Prevention and Treatment

Author:

Kaneko Masayuki1,Imaizumi Kazunori1,Saito Atsushi2,Kanemoto Soshi1,Asada Rie1,Matsuhisa Koji2,Ohtake Yosuke1

Affiliation:

1. Department of Biochemistry, Institute of Biomedical and Health Sciences, Hiroshima University

2. Department of Stress Protein Processing, Institute of Biomedical and Health Sciences, Hiroshima University

Publisher

Pharmaceutical Society of Japan

Subject

Pharmaceutical Science,Pharmacology,General Medicine

Reference50 articles.

1. 1) Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol., 8, 519–529 (2007).

2. 2) Tsai B, Ye Y, Rapoport TA. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol., 3, 246–255 (2002).

3. 3) Tirasophon W, Welihinda AA, Kaufman RJ. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev., 12, 1812–1824 (1998).

4. 4) Wang XZ, Harding HP, Zhang Y, Jolicoeur EM, Kuroda M, Ron D. Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J., 17, 5708–5717 (1998).

5. 5) Yoshida H, Haze K, Yanagi H, Yura T, Mori K. Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors. J. Biol. Chem., 273, 33741–33749 (1998).

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