1. Harding, H. P., Zhang, Y., and Ron, D. Protein translation and folding are coupled by an endoplasmic reticulum-resident kinase. Nature, 397: 271-274, 1999.
2. Bertolotti, A., Zhang, Y., Hendershot, L. M., Harding, H. P., and Ron, D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol, 2: 326-332, 2000.
3. Liu, C. Y., Schroder, M., and Kaufman, R. J. Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J Biol Chem, 275: 24881-24885, 2000.
4. Ma, K., Vattem, K. M., and Wek, R. C. Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress. J Biol Chem, 277: 18728-18735, 2002.
5. Cullinan, S. B., Zhang, D., Hannink, M., Arvisais, E., Kaufman, R. J., and Diehl, J. A. Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival. Mol Cell Biol, 23: 7198-7209, 2003.
6. Kimball, S. R. Eukaryotic initiation factor eIF2. Int J Biochem Cell Biol, 31: 25-29, 1999.
7. Brewer, J. W., Hendershot, L. M., Sherr, C. J., and Diehl, J. A. Mammalian unfolded protein response inhibits cyclin D1 translation and cell-cycle progression. Proc Natl Acad Sci U S A, 96: 8505-8510, 1999.
8. Lee, J. S. and Surh, Y. J. Nrf2 as a novel molecular target for chemoprevention. Cancer Lett, 224: 171-184, 2005.
