The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Unfolded Protein Response Signaling and Metabolic Diseases
Open accessAbstract
The endoplasmic reticulum (ER) is a central organelle for protein biosynthesis, folding, and traffic. Perturbations in ER homeostasis create a condition termed ER stress and lead to activation of the complex signaling cascade called the unfolded protein response (UPR). Recent studies have documented that the UPR coordinates multiple signaling pathways and controls various physiologies in cells and the whole organism. Furthermore, unresolved ER stress has been implicated in a variety of metabolic disorders, such as obesity and type 2 diabetes. Therefore, intervening in ER stress and modulating signaling components of the UPR would provide promising therapeutics for the treatment of human metabolic diseases. The endoplasmic reticulum (ER) is a central organelle for protein biosynthesis, folding, and traffic. Perturbations in ER homeostasis create a condition termed ER stress and lead to activation of the complex signaling cascade called the unfolded protein response (UPR). Recent studies have documented that the UPR coordinates multiple signaling pathways and controls various physiologies in cells and the whole organism. Furthermore, unresolved ER stress has been implicated in a variety of metabolic disorders, such as obesity and type 2 diabetes. Therefore, intervening in ER stress and modulating signaling components of the UPR would provide promising therapeutics for the treatment of human metabolic diseases.
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Cites
ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs
Ye, J., Rawson, R. B., Komuro, R., Chen, X., Davé, U. P., Prywes, R., Brown, M. S., & Goldstein, J. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00133-7 · Cited by 1,871
Delépine, M., Nicolino, M., Barrett, T., Golamaully, M., Mark Lathrop, G., & Julier, C. (2000) · Nature Genetics · doi:10.1038/78085 · Cited by 813
Targeted disruption of the chop gene delays endoplasmic reticulum stress-mediated diabetes
Oyadomari, S., Koizumi, A., Takeda, K., Gotoh, T., Akira, S., Araki, E., & Mori, M. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0214550 · Cited by 752
Kammoun, H. L., Chabanon, H., Hainault, I., Luquet, S., Magnan, C., Koike, T., Ferré, P., & Foufelle, F. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37007 · Cited by 732
Moreno, J. A., Halliday, M., Molloy, C., Radford, H., Verity, N., Axten, J. M., Ortori, C. A., Willis, A. E., Fischer, P. M., Barrett, D. A., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3006767 · Cited by 589
Characterization of a novel PERK kinase inhibitor with antitumor and antiangiogenic activity
Atkins, C., Liu, Q., Minthorn, E., Zhang, S.-Y., Figueroa, D. J., Moss, K., Stanley, T. B., Sanders, B., Goetz, A., Gaul, N., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3109 · Cited by 443
Mimura, N., Fulciniti, M., Gorgun, G., Tai, Y.-T., Cirstea, D., Santo, L., Hu, Y., Fabre, C., Minami, J., Ohguchi, H., et al. (2012) · Blood · doi:10.1182/blood-2011-07-366633 · Cited by 432
ER Stress Controls Iron Metabolism Through Induction of Hepcidin
Vecchi, C., Montosi, G., Zhang, K., Lamberti, I., Duncan, S. A., Kaufman, R. J., & Pietrangelo, A. (2009) · Science · doi:10.1126/science.1176639 · Cited by 310 · cited 1×
“However, unlike ATF6, CREBH has shown to activate different sets of hepatic genes in the acute phase response (59), iron metabolism (60), gluconeogenesis (61), and TG metabolism (58).”
BackgroundWon, J. C., Jang, P., Namkoong, C., Koh, E. H., Kim, S. K., Park, J., Lee, K., & Kim, M. (2009) · Obesity · doi:10.1038/oby.2009.194 · Cited by 153 · cited 1×
“ER stress in the brain also contributes to central insulin resistance along with leptin resistance; central administration of insulin does not suppress food intake when acute ER stress is induced in the brain (67).”
Background
Cited by
Treatment of Obesity with Celastrol
Liu, J., Lee, J., Salazar Hernandez, M. A., Mazitschek, R., & Ozcan, U. (2015) · Cell · doi:10.1016/j.cell.2015.05.011 · Cited by 726
Self-citationTrimethylamine N-Oxide Binds and Activates PERK to Promote Metabolic Dysfunction
Chen, S., Henderson, A., Petriello, M. C., Romano, K. A., Gearing, M., Miao, J., Schell, M., Sandoval-Espinola, W. J., Tao, J., Sha, B., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.08.021 · Cited by 427
Obesity May Accelerate the Aging Process
Salvestrini, V., Sell, C., & Lorenzini, A. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00266 · Cited by 260
Yu, J., Marsh, S., Hu, J., Feng, W., & Wu, C. (2016) · Gastroenterology Research and Practice · doi:10.1155/2016/2862173 · Cited by 199
Wu, R., Zhang, Q.-H., Lu, Y.-J., Ren, K., & Yi, G.-H. (2015) · DNA and Cell Biology · doi:10.1089/dna.2014.2552 · Cited by 116
Metadata
- Authors
- Lee, J., & Ozcan, U.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 289
- Issue
- 3
- Pages
- 1203-1211
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2025347981
- Cited by
- 303
- References
- 9
- FWCI
- 17.34
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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