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- W2037596908 abstract "The endoplasmic reticulum (ER) is the organelle in which newly synthesized secretory and transmembrane proteins form their proper tertiary structure by post-translational modification, folding, and oligomerization. However, many of these proteins are unfolded or misfolded by extracellular or intracellular stimuli. The accumulation of misfolded proteins constitutes a risk for living cells. Eukaryotic cells possess at least three different mechanisms to adapt to ER stress and thereby survive: (1) translational attenuation to limit further accumulation of misfolded proteins; (2) transcriptional activation of genes encoding ER-resident chaperones; and (3) the ER-associated degradation (ERAD) pathway to restore the folding capacity. If the cells are exposed to prolonged or strong ER stress, the cells are destroyed by apoptosis. Recent evidence indicates that ER stress signaling pathways are mediated in part by several protein kinases and play an important role in the pathogenesis of neurodegenerative disorders. The main purpose of this review is to summarize current knowledge about the protein kinases involved in ER stress, and their involvement in the pathogenesis of neurodegenerative disorders." @default.
- W2037596908 created "2016-06-24" @default.
- W2037596908 creator A5039343897 @default.
- W2037596908 creator A5082943547 @default.
- W2037596908 creator A5086860343 @default.
- W2037596908 date "2004-09-01" @default.
- W2037596908 modified "2023-10-06" @default.
- W2037596908 title "Survival and apoptosis signals in ER stress: the role of protein kinases" @default.
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- W2037596908 doi "https://doi.org/10.1016/j.jchemneu.2004.05.004" @default.
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- W2037596908 hasPublicationYear "2004" @default.
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