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Publication : A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells.

First Author  Han J Year  1994
Journal  Science Volume  265
Issue  5173 Pages  808-11
PubMed ID  7914033 Mgi Jnum  J:46351
Mgi Id  MGI:1197767 Doi  10.1126/science.7914033
Citation  Han J, et al. (1994) A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265(5173):808-11
abstractText  Mammalian cells respond to endotoxic lipopolysaccharide (LPS) by activation of protein kinase cascades that lead to new gene expression. A protein kinase, p38, that was tyrosine phosphorylated in response to LPS, was cloned. The p38 enzyme and the product of the Saccharomyces cerevisiae HOG1 gene, which are both members of the mitogen-activated protein (MAP) kinase family, have sequences at and adjacent to critical phosphorylation sites that distinguish these proteins from most other MAP kinase family members. Both HOG1 and p38 are tyrosine phosphorylated after extracellular changes in osmolarity. These findings link a signaling pathway in mammalian cells with a pathway in yeast that is responsive to physiological stress.
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