IRE1 signaling affects cell fate during the unfolded protein response.

@article{Lin2007IRE1SA,
  title={IRE1 signaling affects cell fate during the unfolded protein response.},
  author={Jonathan H Lin and Han Li and Douglas Yasumura and Hannah R. Cohen and Chao Zhang and Barbara Panning and Kevan M. Shokat and Matthew M. Lavail and Peter Walter},
  journal={Science},
  year={2007},
  volume={318 5852},
  pages={
          944-9
        }
}
Endoplasmic reticulum (ER) stress activates a set of signaling pathways, collectively termed the unfolded protein response (UPR). The three UPR branches (IRE1, PERK, and ATF6) promote cell survival by reducing misfolded protein levels. UPR signaling also promotes apoptotic cell death if ER stress is not alleviated. How the UPR integrates its cytoprotective and proapoptotic outputs to select between life or death cell fates is unknown. We found that IRE1 and ATF6 activities were attenuated by… CONTINUE READING

Similar Papers

Citations

Publications citing this paper.
SHOWING 1-10 OF 578 CITATIONS, ESTIMATED 44% COVERAGE

The effect of statin therapy on endoplasmic reticulum stress.

  • Pharmacological research
  • 2018
VIEW 7 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

Managing the protein folding demands in the endoplasmic reticulum of plants.

  • The New phytologist
  • 2016
VIEW 5 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

The unfolded protein response is shaped by the NMD pathway.

  • EMBO reports
  • 2015
VIEW 6 EXCERPTS
CITES BACKGROUND, RESULTS & METHODS
HIGHLY INFLUENCED

FILTER CITATIONS BY YEAR

2008
2019

CITATION STATISTICS

  • 63 Highly Influenced Citations

  • Averaged 41 Citations per year over the last 3 years