Transcriptional and translational control in the Mammalian unfolded protein response.

By H. Harding, M. Calfon, F. Urano, I. Novoa, D. Ron. Annual Review of Cell and Developmental Biology, 2002

970 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Surgery

View Paper: https://www.semanticscholar.org/paper/b9acf22265dea63d39b65455ac8dd1d81d1f112e

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. R. Kaufman
2. D. Ron
3. G. Hotamışlıgil
4. J. Malhotra
5. H. Harding
6. S. Oyadomari
7. Junying Yuan
8. M. Boyce

In Epidemiology

1. R. Kaufman
2. J. Malhotra
3. D. Ron
4. E. White
5. H. Harding
6. I. Novoa
7. R. Amaravadi
8. Junying Yuan

In Surgery

1. R. Kaufman
2. J. Malhotra
3. D. Ron
4. F. Urano
5. H. Harding
6. Roberto Sitia
7. G. Hotamışlıgil
8. C. Hetz

Citations in the corpus

• Roles of CHOP/GADD153 in endoplasmic reticulum stress (2004, background): “attenuation, reducing the load of new protein synthesis and preventing further accumulation of unfolded proteins.(6) The second response is upregulation of genes encoding ER chaperone proteins such as BiP/GRP78 and GRP94, en-”
• A trip to the ER: coping with stress. (2004, background): “Groundbreaking research over the past few years has led to an exhaustive description of the basic pathways involved in UPR activation, signal transduction and transcriptional activation in mammals; these advances have been thoroughly reviewed elsewhere [ 2 ,3] .B y contrast, much less is known about”
• Principles and Current Strategies for Targeting Autophagy for Cancer Treatment (2011, background): “Because uncompensated ER stress can lead to cell death (59, 67), the compensatory activation of autophagy pro-”
• Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword? (2007, positive): “Coordinate regulation of all these processes is required to restore proper protein folding and ER homeostasis (40, 63, 86, 107, 122, 150).”
• Phosphorylation of the α Subunit of Eukaryotic Initiation Factor 2 Is Required for Activation of NF-κB in Response to Diverse Cellular Stresses (2003, background): “ER chaperones GRP78/BiP and GRP94 (22, 35, 47).”
• Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis. (2006, background): “What is particularly striking is the fact that although palmitate clearly activates PERK and IRE1 signaling, the main ER chaperone target genes of these signaling pathways are not induced by palmitate (19).”
• ATF4 is a substrate of RSK2 and an essential regulator of osteoblast biology; implication for Coffin-Lowry Syndrome. (2004, background): “A 271 bp 5 untrans-pression of Atf4 is dependent on eIF2 phosphorylation lated region of Atf4 and a 390 bp 5 untranslated and partial of coding(Harding et al., 2002).”
• Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival (2003, background): “Because the UPR is known to elicit oxidative stress (18, 31), a known inducer of Nrf2 nuclear translocation, we assessed whether tunicamycin-dependent activation of Nrf2 was directed by a burst of reactive oxygen species (ROS) generated as a consequence of ER stress.”
• CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. (2004, background): “The UPR has evolved considerably during phylogeny, a purely transcriptional response in unicellular organisms like yeast; a translational PERK-mediated component was acquired by simple metazoans, whereas in vertebrates, a GADD34-mediated mechanism to recover protein synthesis and secretory capacity ”
• Coupling endoplasmic reticulum stress to the cell death program (2004, background): “In turn, the UPR triggers two downstream signal transduction events: the induction of genes coding for ER-resident stress proteins and the suppression of initiation of protein synthesis.(4,5,7) The ERresident protein kinase PERK has been implicated in the latter process.”
• Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones (2004, background): “The molecular basis for this specificity is partially understood, as some of the proximal transducers that selectively activate genes encoding cytoplasmic or ER chaperones have been identified (Morimoto, 1998; Kaufman, 1999; Patil and Walter, 2001; Harding et al., 2002).”