UPR proteins IRE1 and PERK switch BiP from chaperone to ER stress sensor
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/s41594-019-0324-9.pdf
Reference34 articles.
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3. Walter, P. & Ron, D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081–1086 (2011).
4. Adams, C. J., Kopp, M. C., Larburu, N., Nowak, P. R. & Ali, M. M. U. Structure and molecular mechanism of ER stress signaling by the unfolded protein response signal activator IRE1. Front. Mol. Biosci. 6, 11 (2019).
5. Zhou, J. et al. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proc. Natl Acad. Sci. USA 103, 14343–14348 (2006).
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