Orchestrating the unfolded protein response in health and disease.

By R. Kaufman. Journal of Clinical Investigation, 2002

1,325 citations recorded by the source corpus.

Subfields: Biotechnology, Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/e757d169dbe968b850ba0fa503f5495890ac1cb7

How researchers see this paper

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

In Biotechnology

1. R. Kaufman
2. C. Hetz
3. D. Ron
4. J. Malhotra
5. I. Tabas
6. Jerry M. Adams
7. M. Pagliassotti
8. Dong Wang

In Cell Biology

1. R. Kaufman
2. G. Hotamışlıgil
3. C. Hetz
4. D. Ron
5. J. Malhotra
6. Laurie H. Glimcher
7. H. Harding
8. Afshin Samali

In Molecular Biology

1. R. Kaufman
2. G. Hotamışlıgil
3. D. Ron
4. C. Hetz
5. J. Malhotra
6. Laurie H. Glimcher
7. H. Harding
8. Ann-Hwee Lee

Citations in the corpus

• A trip to the ER: coping with stress. (2004, background): “The inhibition of N-linked glycosylation in the ER, depletion of ER calcium stores, reductive stress and the expression of mutant, and even some wild-type, secretory or transmembrane proteins all probably saturate folding pathways and clog the ER lumen [ 3 ].”
• Mechanisms, regulation and functions of the unfolded protein response (2020, background): “(3) ATF6 transits from the ER to the Golgi apparatus, where it is cleaved”
• Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins (2006, background): “The accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) lumen results in activation of the unfolded protein response (UPR). Protein folding stress on the ER can result from a number of insults, including exposure to pharmacological agents that perturb protein folding, ge”
• Quality control in the endoplasmic reticulum protein factory (2003, background): “The unfolded proteins titrate BiP, releasing ATF6 for transport and subsequent cleavage by Golgi protease”
• Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword? (2007, neutral): “All proteins that transit the secretory pathway in eukaryotic cells first enter the endoplasmic reticulum (ER), where they fold and assemble into multisubunit complexes before transit to the Golgi compartment (63).”
• The cell biology of lysosomal storage disorders (2004, neutral): “This latter point is not entirely obvious as cells could,in principle, have an ‘intra-lysosomal protein response’that is analogous to the ‘ UNFOLDED PROTEIN RESPONSE ’in the ER,in which similar pathways are activated irrespective of the nature of the unfolded protein 32 .”
• XBP-1 Regulates a Subset of Endoplasmic Reticulum Resident Chaperone Genes in the Unfolded Protein Response (2003, background): “UPRE reporter (5xATF6GL3), pCGNATF6, and pCGNAF6(1-373) were previously described (57).”
• Role of cholesterol and lipid organization in disease (2005, background): “One of several UPR effector proteins is a protein called CHOP (GADD153), which can, in turn, affect the transcription of a number of genes that participate in the UPR programm”
• CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. (2004, background): “This load, which can be very heavy in secretory cells, imposes a physiological ER stress that is counteracted by a stereotyped set of adaptations collectively known as the unfolded protein response (UPR) (Patil and Walter 2001; Harding et al. 2002; Kaufman 2002).”
• Autophagy Is Activated for Cell Survival after Endoplasmic ReticulumStress (2006, background): “The UPR involves at least three distinct components, namely transcriptional induction of genes encoding ER-resident chaperones to facilitate protein folding, translational attenuation to decrease the demands made on the organelle, and ER-associated degradation (ERAD) to degrade the unfolded proteins”
• Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress (2011, background): “In contrast to these scenarios of limited and selective apoptosis, chronic ER stress can induce widespread pathologic apoptosi”