The role of the unfolded protein response in tumour development: friend or foe?
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Earth and Planetary Sciences,General Environmental Science
Link
http://www.nature.com/articles/nrc1505.pdf
Reference109 articles.
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4. Brodsky, J. L. et al. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J. Biol. Chem. 274, 3453–3460 (1999).
5. Kozutsumi, Y., Segal, M., Normington, K., Gething, M. J. & Sambrook, J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332, 462–464 (1988). A range of pharmacological agents had been used to activate an undefined signal-transduction cascade that led to the coordinate upregulation of resident ER chaperones. The authors of this paper hypothesized that all of the agents used could affect normal protein folding in the ER and demonstrated that the upstream signal was the presence of unfolded proteins in the ER.
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