Unfolded Proteins Are Ire1-Activating Ligands That Directly Induce the Unfolded Protein Response

By B. Gardner, Peter Walter. Science, 2011

660 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology

View Paper: https://www.semanticscholar.org/paper/d37c449d49ac25deb931330186f8f2d3b9dd7c3d

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. C. Hetz
2. R. Kaufman
3. F. Papa
4. Afshin Samali
5. Peter Walter
6. D. Ron
7. A. Gorman
8. John Calvin Reed

In Epidemiology

1. R. Kaufman
2. C. Hetz
3. F. Papa
4. John Calvin Reed
5. Afshin Samali
6. A. Gorman
7. Peter Walter
8. D. Ron

Citations in the corpus

• Endoplasmic Reticulum Stress and Associated ROS (2016, background): “To restore cell homeostasis after ER stress, a sequence of reactions known as the unfolded protein response (UPR) is initiated [7,8].”
• Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains (2013, background): “The other process involves unfolded proteins that may also engage the stress-sensing luminal domain directly and favor its dimerization and thereby downstream signaling (7, 8).”
• Endoplasmic reticulum stress sensing in the unfolded protein response. (2013, background): “Cite this article as Cold Spring Harb Perspect Biol 2013;5:a013169 set of peptides (Gardner and Walter 2011).”
• The unfolded protein response: controlling cell fate decisions under ER stress and beyond (2012, background): “Remarkably, this idea was recently validated by an elegant study in living yeast cells, in which model misfolded proteins were shown to be the ligand that activates Ire1 (Ref”
• The integrated stress response (2016, positive): “While there is somewhat limited direct evidence for the latter model of PERK activation, it is supported by evidence from another ER sensor of unfolded proteins, inositol-requiring enzyme-1 (IRE1), whose ER luminal domain exhibits strong sequence homology with that of PERK and which in yeast has bee”
• The impact of the unfolded protein response on human disease (2012, background): “However, additional mechanisms that initiate and modulate the activity of individual UPR branches have been reported, in particular for IRE1 (Gardner and Walter, 2011; Promlek et al., 2011), which may explain their diverse responses to different signals and/or in different cell types.”
• ER stress-induced cell death mechanisms. (2013, background): “When unfolded proteins accumulate in the ER, BiP is released from these complexes to assist with the folding of accumulated proteins [1].”
• The Unfolded Protein Response and Cell Fate Control. (2017, positive): “In yeast, a direct recognitionmodel has been proposed, where IRE1 binds misfolded proteins as ligands through a groove similar to themajor histocompatibility complex (MHC) I as demonstrated through structural and biochemical analysis (Gardner and Walter, 2011).”
• Pharmacological brake-release of mRNA translation enhances cognitive memory (2013, background): “The lumenal stress-sensing domains of PERK and IRE1 are homologous and likely activated in analogous ways by direct binding to unfolded peptides (Gardner and Walter, 2011).”