A time-dependent phase shift in the mammalian unfolded protein response.

By Hiderou Yoshida, Toshie Matsui, N. Hosokawa, R. Kaufman, K. Nagata, K. Mori. Developmental Cell, 2003

704 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Immunology

View Paper: https://www.semanticscholar.org/paper/7e116a2266023e750161a379b6f2682414980ef2

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. C. Hetz
3. J. Malhotra
4. Laurie H. Glimcher
5. G. Hotamışlıgil
6. D. Ron
7. Peter Walter
8. Ann-Hwee Lee

In Epidemiology

1. R. Kaufman
2. C. Hetz
3. J. Malhotra
4. Laurie H. Glimcher
5. D. Ron
6. Junying Yuan
7. M. Boyce
8. Peter Walter

In Immunology

1. R. Kaufman
2. J. Malhotra
3. C. Hetz
4. Laurie H. Glimcher
5. Junying Yuan
6. D. Ron
7. Ann-Hwee Lee

Citations in the corpus

• Measuring ER stress and the unfolded protein response using mammalian tissue culture system (2011, background): “Spliced XBP1 mRNA encodes a basic leucine zipper (b-ZIP) transcription factor that upregulates UPR target genes, including genes that function in ERAD such as ER-degradation-enhancing-a-mannidose-like protein (EDEM; Yoshida et al., 2003), as well as genes that function in folding proteins such as pr”
• Endoplasmic reticulum stress in disease pathogenesis. (2008, background): “This specific blockage may be tied to the fact that some of the genes activatedbyXBP-1 code for proteins involved in ER-associated protein degradation (84).”
• Endoplasmic Reticulum Stress in Liver Disease (2010, background): “Transcriptional targets of sXBP1 include genes that encode functions in ER protein folding and quality control, ER-associated degradation (ERAD) and ER biogenesis [128, 155].”
• Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword? (2007, neutral): “One of the substrates of ERAD ubiquitinated by Parkin is the Pael receptor, a homologue of endothelin receptor type B (54).”
• Quality control in the endoplasmic reticulum protein factory (2003, background): “The two-step activation of XBP-1 (transcriptionally induced by ATF6 and post-transcriptionally regulated by Ire1) guarantees the proper timing of the UPR; attempts to fold proteins precede the decision to degrade the”
• Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins (2006, background): “The subset of genes dependent upon XBP1 action remains only partially characterized, but in general seems to encompass those involved in facilitating protein degradation [30,31].”
• Signal integration in the endoplasmic reticulum unfolded protein response (2007, background): “Nonetheless, there appear to be important differences in the direct targets of the transcriptional activators of the UP”
• The unfolded protein response: controlling cell fate decisions under ER stress and beyond (2012, background): “An early report suggested that, under certain conditions, ATF6 may be activated first, before IRE1α and PER”
• Cellular response to endoplasmic reticulum stress: a matter of life or death (2006, background): “that of XBP-1 during ER stress, suggesting a time-dependent shift in the UPR transcriptional response.(72) ATF6 and XBP-1 therefore play distinct but complementary roles in adjusting UPR-mediated transcription during persistent”