Nuclear-accumulated SQSTM1/p62-based ALIS act as microdomains sensing cellular stresses and triggering oxidative stress-induced parthanatos
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cancer Research,Cell Biology,Cellular and Molecular Neuroscience,Immunology
Link
http://www.nature.com/articles/s41419-018-1245-y.pdf
Reference62 articles.
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3. Liu, X. D. et al. Transient aggregation of ubiquitinated proteins is a cytosolic unfolded protein response to inflammation and endoplasmic reticulum stress. J. Biol. Chem. 287, 19687–19698 (2012).
4. Nozawa, N., Yamauchi, Y., Ohtsuka, K., Kawaguchi, Y. & Nishiyama, Y. Formation of aggresome-like structures in herpes simplex virus type 2-infected cells and a potential role in virus assembly. Exp. Cell Res. 299, 486–497 (2004).
5. Vasconcellos, L. R. C. et al. Protein aggregation as a cellular response to oxidative stress induced by heme and iron. Proc. Natl Acad. Sci. USA 113, E7474–E7482 (2016).
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