Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death.

By Cole M. Haynes, Eric A Titus, A. Cooper. Molecules and Cells, 2004

640 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a280f6f6f3ac007964817b68d712b529bad42dc8

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. G. Hotamışlıgil
4. H. Harding
5. S. Oyadomari
6. S. Marciniak
7. Junying Yuan
8. M. Boyce

In Epidemiology

1. R. Kaufman
2. G. Hotamışlıgil
3. D. Ron
4. H. Harding
5. I. Novoa
6. S. S. Cao
7. S. Oyadomari
8. Yuhong Zhang

In Molecular Biology

1. R. Kaufman
2. G. Hotamışlıgil
3. D. Ron
4. H. Harding
5. S. Marciniak
6. S. Oyadomari
7. I. Novoa
8. Junying Yuan

Citations in the corpus

• Role of ROS and RNS Sources in Physiological and Pathological Conditions (2016, background): “Therefore, chromosome 10 mutations may be a possible risk factor in AD.”
• Mechanisms of obesity-associated insulin resistance: many choices on the menu. (2007, result): “Finally, it is also possible that ER stress might lead to an increase in oxidative stress that in turn might contribute to the insulin resistance seen in the above studies (Haynes et al. 2004).”
• ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response to ROS (2010, background): “mTORC1 hyperactivity has been shown to result in endoplasmic reticulum (ER) stress (34), which can lead to elevated ROS (35) suggesting a linkage between mTORC1 and production of ROS.”
• Endoplasmic reticulum stress signaling in disease. (2006, background): “the generation of ROS and cell death (58) and that ER”
• Endoplasmic Reticulum Stress and Oxidative Stress in Cell Fate Decision and Human Disease (2014, background): “When the microenvironment of ER protein folding is severely disrupted, or when a misfolding-prone protein is expressed in the cell, a futile cycle of disulfide bond formation and reduction could lead to oxidative stress by generating a large amount of H2O2 and depleting ER GSH levels (72).”
• Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease (2010, positive): “This reduced molecular oxygen accumulates during increased protein folding due to UPR activation and is toxic to cells (Haynes et al., 2004).”
• Cellular response to endoplasmic reticulum stress: a matter of life or death (2006, background): “These effects are achieved through three major pathways: (I) the unfolded protein response (UPR), a transcription-dependent induction of ER lumenal chaperone proteins and other components of the secretory apparatus to augment the polypeptide folding and processing capacity of the ER;5,7 (II) the act”
• Photoreceptor degeneration: genetic and mechanistic dissection of a complex trait (2010, neutral): “The UPR seems to result from increased RONS signalling in response to repeated attempts to fold reduced and unfolded protein substrate”
• CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. (2004, background): “2003) and yeast (Haynes et al. 2004), and that the aforementioned integrated stress response mitigates this tendency (Harding et al.”
• Endoplasmic Reticulum Stress and Associated ROS (2016, background): “Both cause a disturbance in the redox status of the ER lumen, which leads to ER stress after oxidative stress [46,47].”
• Protein Disulfide Isomerase: A Critical Evaluation of Its Function in Disulfide Bond Formation (2009, background): “This peroxide generation has been widely viewed as a harmful byproduct, such that the formation of native disulfide bonds in folding proteins is thought to cause oxidative stress in cells (116, 304).”