Mediators of endoplasmic reticulum stress‐induced apoptosis

By E. Szegezdi, S. Logue, A. Gorman, Afshin Samali. EMBO Reports, 2006

2,369 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Physiology

View Paper: https://www.semanticscholar.org/paper/d627296586664e740c3d3df891db19d0af9aed27

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. B. Ogretmen
2. Afshin Samali
3. A. Gorman
4. C. Senkal
5. I. Tabas
6. J. Bielawski
7. Tiziana Anelli
8. S. Ponnusamy

In Epidemiology

1. I. Tabas
2. Afshin Samali
3. A. Gorman
4. Roberto Sitia
5. G. Svegliati-Baroni
6. R. Yadav
7. H. Chae
8. Yusuf A. Hannun

In Physiology

1. B. Ogretmen
2. R. Yadav
3. H. Chae
4. Yusuf A. Hannun
5. Hyung-Ryong Kim
6. H. Rashid
7. G. Hotamışlıgil

Citations in the corpus

• Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress (2011, background): “Overview of ER-stress-induced apoptosis Prolonged activation of IRE1 and CHOP can trigger apoptosis in cells under certain physiologic and pathophysiologic condition”
• The Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress (2016, background): “Remarkably, this suggests that during prolonged ER stress, when adaptive responses are insufficient to sustain ER homeostasis, PERK-dependent signaling pathways may elicit pro-apoptotic signals and, as a result, rapid cell death ensues [97].”
• Lipotoxicity and the gut-liver axis in NASH pathogenesis. (2018, background): “due to lipid overload, causes a 'stress' to the ER, which initially determines the activation of signaling pathways collectively termed 'unfolded protein response' [34].”
• Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “The discoveries of the Bcl-2 family of proteins [14–16], death receptors [17], caspases [18], mitochondrial cytochrome c release [19], and a role for the endoplasmic reticulum [20] in apoptosis were just a few major milestones in the history of the field.”
• The eIF2α kinases: their structures and functions (2013, neutral): “PERK (also known as PEK, EIF2AK3) is primarily activated by the accumulation of misfolded proteins in the endoplasmic reticulum (ER), a phenomenon termed ER stress [185].”
• ER stress: Autophagy induction, inhibition and selection (2015, background): “Mild to moderate ER stress-induced UPR signaling is seen as a compensatory mechanism, whereas severe and chronically prolonged ER stress deteriorates cellular functions and switches from an adaptation program to apoptosis to remove irreversibly injured cells.(18,19) Decreasing the ER protein load is”
• Antiapoptotic roles of ceramide‐synthase‐6‐generated C16‐ceramide via selective regulation of the ATF6/ CHOP arm of ER‐stress‐response pathways (2010, background): “evolved to minimize ER stress by increasing the protein folding capacity of ER, decreasing the rate of secretory protein synthesis, and/or increasing the chaperone capacity in cells (10, 11).”
• Role of ROS and RNS Sources in Physiological and Pathological Conditions (2016, neutral): “apoptotic program activation [218].”
• Protein quality control in the early secretory pathway (2008, background): “If these measures are not sufficient for eliminating misfolded proteins from the ER, apoptotic pathways are activated (reviewed in Szegezdi et al, 2006).”