A trip to the ER: coping with stress.

By D. Rutkowski, R. Kaufman. Trends in Cell Biology, 2004

1,464 citations recorded by the source corpus.

Subfields: Biotechnology, Cell Biology, Epidemiology

View Paper: https://www.semanticscholar.org/paper/e96f8c78e5829ce4b052acc2feddf3df9844e770

How researchers see this paper

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

In Biotechnology

1. R. Kaufman
2. M. Pagliassotti
3. Dong Wang
4. Yuren Wei
5. F. Topczewski
6. D. Rutkowski
7. Jun Wu

In Cell Biology

1. R. Kaufman
2. D. Rutkowski
3. G. Hotamışlıgil
4. M. Pagliassotti
5. Dong Wang
6. Yuren Wei
7. F. Topczewski
8. Jun Wu

In Epidemiology

1. R. Kaufman
2. Jun Wu
3. F. Urano
4. J. Malhotra
5. C. Hetz

Citations in the corpus

• Autophagy Is Activated for Cell Survival after Endoplasmic ReticulumStress (2006, background): “In mammalian cells, PERK, IRE1, and ATF6 sense the presence of unfolded proteins in the ER lumen and transduce signals to the cytoplasm and the nucleus (32).”
• From acute ER stress to physiological roles of the Unfolded Protein Response (2006, background): “These include nutrient deprivation, alterations in the oxidation–reduction balance, changes in calcium concentration, failure of post-translational modifications, or simply increases in secretory protein synthesis.(3) Pharmacological reagents”
• Stress-induced ER to Golgi translocation of ceramide synthase 1 is dependent on proteasomal processing (2009, neutral): “Other reported examples of translocation in response to stress include the ATF6 protein, which is part of the unfolded protein response, and translocates from the ER to the Golgi in response to a variety of metabolic, chemical or genetic stresses [31], and the sterol”
• The Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress (2016, background): “The ER is a multifunctional organelle, that plays a central role in protein folding, biosynthesis of phospholipids, and maintaining calcium homeostasis [11].”
• Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins (2006, background): “]. The mammalian cell senses the accumulation of unfolded proteins that these insults generate through the action of three key ER-resident transmembrane proteins—PERK, IRE1, and ATF6 [”
• Saturated fatty acids induce endoplasmic reticulum stress and apoptosis independently of ceramide in liver cells. (2006, background): “Accumulation of unfolded proteins in the lumen of the ER activates a highly regulated, adaptive program termed the unfolded protein response (UPR) (33, 35).”
• Polyamines: essential factors for growth and survival (2008, background): “The underlying mechanisms of UPR in yeasts and mammals have been well researched (Rutkowski and Kaufman 2004), although those in plants have not (Kamauchi et al. 2005; Urade 2007).”