Author
S C Hubbard
Bio: S C Hubbard is an academic researcher. The author has contributed to research in topics: In vivo. The author has an hindex of 1, co-authored 1 publications receiving 245 citations.
Topics: In vivo
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245 citations
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TL;DR: This review summarizes how perturbation of three major functions of the endoplasmic reticulum in eukaryotic cells causes ER stress and activates signaling pathways collectively termed the unfolded protein response (UPR), and how the UPR reestablishes homeostasis.
Abstract: In homeostasis, cellular processes are in a dynamic equilibrium. Perturbation of homeostasis causes stress. In this review I summarize how perturbation of three major functions of the endoplasmic reticulum (ER) in eukaryotic cells–protein folding, lipid and sterol biosynthesis, and storing intracellular Ca2+ – causes ER stress and activates signaling pathways collectively termed the unfolded protein response (UPR). I discuss how the UPR reestablishes homeostasis, and summarize our current understanding of how the transition from protective to apoptotic UPR signaling is controlled, and how the UPR induces inflammatory signaling.
642 citations
626 citations
TL;DR: The results provided an explanation for trimming and reglucosylation activities in the endoplasmic reticulum and established a direct correlation between glycosylation and folding.
543 citations
441 citations
TL;DR: Findings suggest that once complexes between calnexin and glycoproteins are formed, oligosaccharide binding does not contribute significantly to the overall interaction, however, it is likely that the binding of Glc1Man9GlcNAc2 oligosACcharides is a crucial event during the initial recognition of newly synthesized glycoprotein by cal Nexin.
414 citations