The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Mitogen-activated protein kinases: new signaling pathways functioning in cellular responses to environmental stress
Open accessAbstract
SUMMARY: The mitogen-activated protein kinase (MAPK) superfamily consists of three main protein kinase families: the extracellular signal-regulated protein kinases (ERKs), the c-Jun N-terminal kinases (JNKs) and the p38 family of kinases. Each is proving to have major roles in the regulation of intracellular metabolism and gene expression and integral actions in many areas including growth and development, disease, apoptosis and cellular responses to external stresses. To date, this cellular signal transduction network has received relatively little attention from comparative biochemists,despite the high probability that MAPKs have critical roles in the adaptive responses to thermal, osmotic and oxygen stresses. The present article reviews the current understanding of the roles and regulation of ERKs, JNKs and p38,summarizes what is known to date about MAPK roles in animal models of anoxia tolerance, freeze tolerance and osmoregulation, and highlights the potential that studies of MAPK pathways have for advancing our understanding of the mechanisms of biochemical adaptation.
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Cites
AP-1 as a regulator of cell life and death
Shaulian, E., & Karin, M. (2002) · Nature Cell Biology · doi:10.1038/ncb0502-e131 · Cited by 2,961
A Mammalian Scaffold Complex That Selectively Mediates MAP Kinase Activation
Whitmarsh, A. J., Cavanagh, J., Tournier, C., Yasuda, J., & Davis, R. J. (1998) · Science · doi:10.1126/science.281.5383.1671 · Cited by 652 · cited 1×
“JIP1 binds specifically to JNK1, as well as to MKK7, and the MKK7 activators MLK3 and DLK (dual leucine zipper-bearing kinase) (Whitmarsh et al., 1998).”
BackgroundNuclear Accumulation of NFAT4 Opposed by the JNK Signal Transduction Pathway
Chow, C.-W., Rincón, M., Cavanagh, J., Dickens, M., & Davis, R. J. (1997) · Science · doi:10.1126/science.278.5343.1638 · Cited by 357
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Hayley, S., Poulter, M. O., Merali, Z., & Anisman, H. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.03.051 · Cited by 324
Endocrine disruptors in marine organisms: Approaches and perspectives
Porte, C., Janer, G., Lorusso, L. C., Ortiz-Zarragoitia, M., Cajaraville, M. P., Fossi, M. C., & Canesi, L. (2006) · Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology · doi:10.1016/j.cbpc.2006.03.004 · Cited by 310
The discovery of the benzhydroxamate MEK inhibitors CI-1040 and PD 0325901
Barrett, S. D., Bridges, A. J., Dudley, D. T., Saltiel, A. R., Fergus, J. H., Flamme, C. M., Delaney, A. M., Kaufman, M., LePage, S., Leopold, W. R., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.10.054 · Cited by 289
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Metadata
- Authors
- Cowan, K. J., & Storey, K. B.
- Venue
- Journal of Experimental Biology
- Publisher
- The Company of Biologists
- Published
- 2003-04-01
- Volume
- 206
- Issue
- 7
- Pages
- 1107-1115
- ISSN
- 0022-0949 (ISSN-L)
- 1477-9145
- OpenAlex
- W2155124532
- Cited by
- 593
- References
- 3
- FWCI
- 10.40
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
