Results 221 to 230 of about 90,832 (259)
The PERK signaling pathway as a marker of the unfolded protein response in patients with acute myeloid leukemia. [PDF]
Erkut N +5 more
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Multi-omics analyses related to unfolded protein response in prostate cancer implicate pro-tumor role of IFRD1. [PDF]
Xue Y +14 more
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Mucin 2 and unfolded protein response reshape the mucus barrier in inflammatory bowel disease (Review). [PDF]
Yuan Z, Xia Z, Ling L, Xie J, Zhang F.
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THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Annual Review of Biochemistry, 2005▪ Abstract In the endoplasmic reticulum (ER), secretory and transmembrane proteins fold into their native conformation and undergo posttranslational modifications important for their activity and structure. When protein folding in the ER is inhibited, signal transduction pathways, which increase the biosynthetic capacity and decrease the biosynthetic ...
Martin, Schröder, Randal J, Kaufman
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2017
Under the unfolded protein response (UPR), transcripts encoding the endoplasmic reticulum (ER) chaperones are increased and those encoding proteins synthesized in the ER are decreased. To reproducibly detect such changes of an expression profile, homogeneous growth of plants is desired. In addition, uniform treatment with drugs inducing the UPR is also
Kazuki, Tabara +2 more
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Under the unfolded protein response (UPR), transcripts encoding the endoplasmic reticulum (ER) chaperones are increased and those encoding proteins synthesized in the ER are decreased. To reproducibly detect such changes of an expression profile, homogeneous growth of plants is desired. In addition, uniform treatment with drugs inducing the UPR is also
Kazuki, Tabara +2 more
openaire +2 more sources
Molecular Biotechnology, 2006
The unfolded protein response (UPR) is a signal transduction network activated by inhibition of protein folding in the endoplasmic reticulum (ER). The UPR coordinates adaptive responses to this stress situation, including induction of ER resident molecular chaperone and protein foldase expression to increase the protein folding capacity of the ER ...
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The unfolded protein response (UPR) is a signal transduction network activated by inhibition of protein folding in the endoplasmic reticulum (ER). The UPR coordinates adaptive responses to this stress situation, including induction of ER resident molecular chaperone and protein foldase expression to increase the protein folding capacity of the ER ...
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Sphingolipids and the unfolded protein response
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2019The unfolded protein response (UPR) is a response by the endoplasmic reticulum to stress, classically caused by any disruption to cell homeostasis that results in an accumulation in unfolded proteins. However, there is an increasing body of research demonstrating that the UPR can also be activated by changes in lipid homeostasis, including changes in ...
Bennett, M.K. +2 more
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Hypoxia and the Unfolded Protein Response
2007Tumor hypoxia refers to the development of regions within solid tumors in which the oxygen concentration is lower (0-3%) compared to that in most normal tissues (4-9%) (Vaupel and Hockel, 2000). Considerable experimental and clinical evidence exists supporting the notion that hypoxia fundamentally alters the physiology of the tumor towards a more ...
Constantinos, Koumenis +4 more
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Structural Basis of the Unfolded Protein Response
Annual Review of Cell and Developmental Biology, 2012The unfolded protein response (UPR) is a network of intracellular signaling pathways that maintain the protein-folding capacity of the endoplasmic reticulum (ER) in eukaryotic cells. Dedicated molecular sensors embedded in the ER membrane detect incompletely folded or unfolded proteins in the ER lumen and activate a transcriptional program that ...
Alexei, Korennykh, Peter, Walter
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Unfolded Protein Response after Neurotrauma
Journal of Neurotrauma, 2006The endoplasmic reticulum (ER) lumen, which actively monitors the synthesis, folding, and modification of newly synthesized transmembrane and secretory proteins as well as lipids, is quite sensitive to homeostatic perturbations. The biochemical, molecular, and physiological events that elevate cellular ER stress levels and disrupt Ca2+ homeostasis ...
Stephen F, Larner +2 more
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