Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals.

By C. Patil, P. Walter. Current Opinion in Cell Biology, 2001

827 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/8a89fd132a0129dca43016c3e914dca86270d5c5

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. C. Hetz
6. Laurie H. Glimcher
7. H. Harding
8. Junying Yuan

In Epidemiology

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

In Molecular Biology

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

Citations in the corpus

• Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. (2005, background): “Here, the relatively small decrease results from induction of the unfolded protein response (UPR) (Figure 1B, bottom panel), an ESP-specific stress response that induces KAR2 transcription (Patil and Walter, 2001).”
• ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. (2002, background): “(Ma and Hendershot, 2001; Mori, 2000; Patil and Walter, 2001).”
• Regulation of apoptosis by endoplasmic reticulum pathways (2003, background): “All of these agents eventually induce apoptosis within 20–48 h depending on the cell type, suggesting that if the damage to the ER is too great, or if balance is not restored within a certain window of time, an apoptotic response is elicited (Patil and Walter, 2001).”
• Cellular response to endoplasmic reticulum stress: a matter of life or death (2006, background): “cerevisiae.(2,3,22) In yeast, ER stress is monitored by Ire1p, an ER transmembrane protein with an N-terminal lumenal domain and a C-terminal serine/threonine kinase and endonuclease domains in the cytoplasm or nucleus.”
• Transcriptional regulation of plant cell wall degradation by filamentous fungi. (2005, background): “The mechanism of the UPR induction was first characterised in the yeast Saccharomyces cerevisiae and, currently the stress response is well-known also in higher eukaryotes (for reviews see [187–190].”
• Ageing and vision: structure, stability and function of lens crystallins. (2004, background): “…protein evokes the heat shock response, while unfolding endoplasmic reticulum protein evokes the unfolded protein response (for review, see Morimoto and Santoro, 1998; van den IJssel et al., 1999; Patil and Walter, 2001; van Montfort et al., 2001; Arrigo and M .uller, 2002; Sonna et al., 2002).”
• 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).”
• The role for endoplasmic reticulum stress in diabetes mellitus. (2008, background): “The discovery of the signal transduction regulating the UPR is a telling example of the crucial role of basic research in model organisms such as yeast for the understanding of complex human diseases (42).”
• The endoplasmic reticulum and the unfolded protein response. (2007, background): “The protein encoded by spliced HAC1 mRNA binds and activates transcription from the UPR element [UPRE, minimal motif TGACGTG(C/A)] upstream of many UPR target genes [2,23].”
• Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease (2010, neutral): “The oldest branch of the UPR, in an evolutionary sense, is mediated through the stress-regulated kinase and ribonuclease IRE1, which is conserved from yeast to humans (Calfon et al., 2002; Patil and Walter, 2001).”
• Growth Arrest and DNA Damage-Inducible Protein GADD34 Targets Protein Phosphatase 1α to the Endoplasmic Reticulum and Promotes Dephosphorylation of the α Subunit of Eukaryotic Translation Initiation Factor 2 (2003, methodology): “The ability of WT GADD34(1-674) but not GADD34(1-600) to bind PP1 in the coimmunoprecipitation and affinity isolation assays suggested that the C terminus of GADD34 between amino acids 600 to 674 was crucial for PP1 binding.”
• Organelle-specific initiation of cell death pathways (2001, background): “Apoptosis regulation at the endoplasmic reticulum The endoplasmic reticulum (ER) participates in the initiation of apoptosis by at least two different mechanisms, namely the unfolded protein response (UPR) and Ca 2+ signallin”