Targeting the unfolded protein response in disease

By C. Hetz, É. Chevet, H. Harding. Nature reviews. Drug discovery, 2013

894 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/522a6590044407a361709bed1ecfaf85d5053a98

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. J. Cubillos-Ruiz
2. Sarah Bettigole
3. Laurie H. Glimcher
4. Ann-Hwee Lee
5. G. Hotamışlıgil
6. R. Kaufman
7. C. Hetz
8. F. Papa

In Epidemiology

1. J. Cubillos-Ruiz
2. Laurie H. Glimcher
3. Ann-Hwee Lee
4. Sarah Bettigole
5. G. Hotamışlıgil
6. R. Kaufman
7. C. Hetz

In Molecular Biology

1. J. Cubillos-Ruiz
2. Laurie H. Glimcher
3. Sarah Bettigole
4. Ann-Hwee Lee
5. R. Kaufman
6. C. Hetz
7. G. Hotamışlıgil

Citations in the corpus

• Tumorigenic and Immunosuppressive Effects of Endoplasmic Reticulum Stress in Cancer (2017, neutral): “Besides PERK, other kinases such as HRI, GCN2 and PKR can regulate the eIF2α/ATF4/ CHOP axis of the UPR (Hetz et al., 2013).”
• The Unfolded Protein Response and Cell Fate Control. (2017, neutral): “In the case of PERK, the levels of eIF2a phosphorylation are negatively controlled by two phosphatase complexes, the ER stress-inducible PPP1R15A/GADD34 (a target of ATF4/CHOP) form and the constitutive phosphatase PPP1R15B/CReP (Hetz et al., 2013).”
• ER Stress Sensor XBP1 Controls Anti-tumor Immunity by Disrupting Dendritic Cell Homeostasis (2015, background): “Abnormal accumulation of unfolded proteins in this compartment causes a state of ‘‘ER stress,’’ which is a hallmark feature of secretory cells and many diseases, including diabetes, neurodegeneration, and cancer (Hetz et al., 2013).”