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- W3150754345 endingPage "705" @default.
- W3150754345 startingPage "705" @default.
- W3150754345 abstract "The unfolded protein response (UPR) is a homeostatic response to endoplasmic reticulum (ER) stress within eukaryotic cells. The UPR initiates transcriptional and post-transcriptional programs to resolve ER stress; or, if ER stress is severe or prolonged, initiates apoptosis. ER stress is a common feature of bacterial infection although the role of the UPR in host defense is only beginning to be understood. While the UPR is important for host defense against pore-forming toxins produced by some bacteria, other bacterial effector proteins hijack the UPR through the activity of translocated effector proteins that facilitate intracellular survival and proliferation. UPR-mediated apoptosis can limit bacterial replication but also often contributes to tissue damage and disease. Here, we discuss the dual nature of the UPR during infection and the implications of UPR activation or inhibition for inflammation and immunity as illustrated by different bacterial pathogens." @default.
- W3150754345 created "2021-04-13" @default.
- W3150754345 creator A5004773303 @default.
- W3150754345 creator A5033323005 @default.
- W3150754345 creator A5051887598 @default.
- W3150754345 date "2021-03-29" @default.
- W3150754345 modified "2023-10-16" @default.
- W3150754345 title "Effectors Targeting the Unfolded Protein Response during Intracellular Bacterial Infection" @default.
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- W3150754345 doi "https://doi.org/10.3390/microorganisms9040705" @default.
- W3150754345 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8065698" @default.
- W3150754345 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33805575" @default.
- W3150754345 hasPublicationYear "2021" @default.
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