Signal transduction: Splicing together the unfolded-protein response
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Signal transduction: Splicing together the unfolded-protein response
Cells respond to the accumulation of unfolded proteins in the endoplasmic reticulum (ER) by increasing the production of ER-resident chaperones, such as BiP and protein disulfide isomerase (PDI), that expedite protein folding and assembly in the ER lumen. In organisms as diverse as yeast and humans, this is accomplished by increasing the transcription of the genes that encode these chaperones. ...
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The endoplasmic reticulum (ER) is a principal site for folding and maturation of transmembrane, secretory and ERresident proteins. Perturbations that alter ER homeostasis can lead to accumulation of unfolded proteins (UPs), which is a threat to all living cells. To cope with the stress, cells activate an intracellular signaling pathway – the unfolded protein response (UPR). The UPR is an integr...
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ژورنال
عنوان ژورنال: Current Biology
سال: 1997
ISSN: 0960-9822
DOI: 10.1016/s0960-9822(06)00038-8