Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response.

By Yanjun Ma, J. Brewer, J. Diehl, L. Hendershot. Journal of Molecular Biology, 2002

716 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/1604c86fe6c58191f8bded579e19b02b3524a8cc

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. R. Kaufman
2. D. Ron
3. J. Malhotra
4. G. Hotamışlıgil
5. Peter Walter
6. C. Hetz
7. H. Harding
8. John Calvin Reed

In Molecular Biology

1. R. Kaufman
2. D. Ron
3. J. Malhotra
4. H. Harding
5. G. Hotamışlıgil
6. Peter Walter
7. Junying Yuan
8. S. Marciniak

Citations in the corpus

• Pharmacological brake-release of mRNA translation enhances cognitive memory (2013, background): “ATF4 regulates the expression of many genes involved in metabolism and nutrient uptake and additional transcription factors, such as CHOP, which is under both translational and transcriptional control (Ma et al., 2002).”
• The role for endoplasmic reticulum stress in diabetes mellitus. (2008, background): “Activation of the PERK pathway can also induce apoptosis via ATF4 overexpression and consequent CHOP and ATF3 induction (91, 92, 130).”
• The eIF2α kinases: their structures and functions (2013, neutral): “Certainly, it is known that in the case of PERK, other elements of the UPR can influence CHOP expression [124]; conversely, a recent study has argued that mTOR signaling (which is expected to be inhibited in response to amino acid deprivation) has a positive influence on CHOP expression [26].”
• Cellular response to endoplasmic reticulum stress: a matter of life or death (2006, background): “ATF6 is a type II transmembrane Cell Death and Differentiation protein in the ER of unstressed cells.67 As with Ire1, the ER lumenal domain of ATF6 interacts with BiP, which binds to a Golgi localization signal (GLS) sequence on ATF6.”
• Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease (2010, neutral): “ATF4 is produced through alternative translation and induces expression of genes involved in apoptosis (CHOP, C/EBP homologous protein), ER redox control (ERO1, endoplasmic reticulum oxidoreductin), the negative feedback release of eIF2a inhibition (Gadd34, growth arrest, and DNA damageinducible pro”
• Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword? (2007, neutral): “CHOP/GADD153 (growth arrest and DNA damage 153) is a bZiP transcription factor that is induced through the ATF6 and PERK UPR pathways (80, 115).”
• CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. (2004, background): “The ER stress-activated kinase PERK phosphorylates the subunit of eukaryotic translation initiation factor 2 (eIF2 ), and the attendant decrease in eIF2 activity paradoxically activates the translation of the ATF4 mRNA, whose encoded protein binds to and activates the CHOP promoter (Fawcett et al. 1”
• Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins (2006, background): “The best characterized of these pro-apoptotic pathways is production of the CHOP/GADD153 transcription factor, which is regulated by ATF4 and possibly ATF6 [21,38,39].”
• The endoplasmic reticulum and the unfolded protein response. (2007, background): “CHOP/GADD153 (growth arrest and DNA damage 153) is a bZIP transcription factor that is induced through the ATF6 and PERK UPR pathways [18,60].”
• Endoplasmic Reticulum Stress in Liver Disease (2010, background): “CHOP transcription is primarily activated by ATF4 although ATF6a may contribute [33,87].”