The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
From JNK to Pay Dirt: Jun Kinases, their Biochemistry, Physiology and Clinical Importance
Abstract
The c‐Jun N‐terminal kinases (JNKs) were originally identified by their ability to phosphorylate c‐Jun in response to UV‐irradiation, but now are recognized as critical regulators of various aspects of mammalian physiology, including: cell proliferation, cell survival, cell death, DNA repair and metabolism. JNK‐mediated phosphorylation enhances the ability of c‐Jun, a component of the AP‐1 transcription factor, to activate transcription, in response to a plethora of extracellular stimuli. The JNK activation leads to induction of AP‐1‐dependent target genes involved in cell proliferation, cell death, inflammation, and DNA repair. The JNKs, which are encoded by three different Jnk loci, are now known to be regulated by many other stimuli, from pro‐inflammatory cytokines to obesity, in addition to UV‐irradiation. Targeted disruption of the Jnk loci in mice has proved to be a critical tool in better understanding their physiological functions. Such studies revealed that the JNKs play important roles in numerous cellular processes, including: programmed cell death, T cell differentiation, negative regulation of insulin signaling, control of fat deposition, and epithelial sheet migration. Importantly, the JNKs have become prime targets for drug development in several important clinical areas, including: inflammation, diabetes, and cancer. IUBMB Life, 57: 283‐295, 2005
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A central role for JNK in obesity and insulin resistance
Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359
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The jun proto-oncogene is positively autoregulated by its product, Jun/AP-1
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Self-citationAguirre, V., Werner, E. D., Giraud, J., Lee, Y. H., Shoelson, S. E., & White, M. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m101521200 · Cited by 1,010
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Smeal, T., Binetruy, B., Mercola, D. A., Birrer, M., & Karin, M. (1991) · Nature · doi:10.1038/354494a0 · Cited by 789
Self-citationInflammatory pathways and insulin action
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A Cytoplasmic Inhibitor of the JNK Signal Transduction Pathway
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The prolyl isomerase PIN1: a pivotal new twist in phosphorylation signalling and disease
Lu, K. P., & Zhou, X. Z. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2261 · Cited by 682
Allocati, N., Masulli, M., Di Ilio, C., & Federici, L. (2018) · Oncogenesis · doi:10.1038/s41389-017-0025-3 · Cited by 625
Gregor, M. F., & Hotamisligil, G. S. (2007) · Journal of Lipid Research · doi:10.1194/jlr.r700007-jlr200 · Cited by 586
Solinas, G., Vilcu, C., Neels, J. G., Bandyopadhyay, G. K., Luo, J.-L., Naugler, W., Grivennikov, S., Wynshaw-Boris, A., Scadeng, M., Olefsky, J. M., et al. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.09.011 · Cited by 513
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Metadata
- Authors
- Karin, M., & Gallagher, E.
- Venue
- IUBMB Life
- Publisher
- Wiley
- Published
- 2005-04
- Volume
- 57
- Issue
- 4-5
- Pages
- 283-295
- ISSN
- 1521-6543 (ISSN-L)
- 1521-6551
- OpenAlex
- W1986060421
- Cited by
- 412
- References
- 21
- FWCI
- 11.52
- Type
- journal article
- Language
- en
- Open access
- closed
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