ER chaperones in mammalian development and human diseases

By Min Ni, Amy S. Lee. FEBS Letters, 2007

749 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/61833c3a75116fb804136d5fa54dc7ecd7b86c9a

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. E. White
2. Robert S. DiPaola
3. A. Dinkova-Kostova
4. V. Karantza-Wadsworth
5. V. Calabrese
6. T. Walsh
7. Edward J. Calabrese
8. A. Ibrahim

In Epidemiology

1. E. White
2. Robert S. DiPaola
3. A. Dinkova-Kostova
4. V. Karantza-Wadsworth
5. T. Walsh
6. Guanghua Chen
7. A. Ibrahim
8. Mark P. Mattson

In Molecular Biology

1. E. White
2. Robert S. DiPaola
3. A. Dinkova-Kostova
4. V. Karantza-Wadsworth
5. V. Calabrese
6. T. Walsh
7. Edward J. Calabrese
8. A. Ibrahim

Citations in the corpus

• Autophagy Suppresses Tumorigenesis Through Elimination of p62 (2009, positive): “While p62 and ER chaperone upregulation are common in human tumors and are associated with poor prognosis, the cause is unknown (Ni and Lee, 2007; Zatloukal et al., 2007).”
• Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “[152] M.”
• Cellular Stress Responses, The Hormesis Paradigm, and Vitagenes: Novel Targets for Therapeutic Intervention in Neurodegenerative Disorders (2010, positive): “The expression of GRP78 is highly sensitive to metabolic stress, and its upregulation under such adverse conditions has been shown to protect cells against death (326).”
• Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities (2008, background): “Another proposed strategy for removing insoluble protein inclusions is to increase chaperone activity in cells, especially the cytosolic heat-shock protein 70 (HSP70) family of proteins (reviewed in Ref”
• The role for endoplasmic reticulum stress in diabetes mellitus. (2008, background): “Treatment with IFN-␥ decreases expression of XBP1s mRNA, several ER chaperones (BiP, GRP94, and ORP150, but not calnexin/calreticulin), and Sec61␣, while augmenting CHOP and ATF-4 expression (241, 242).”
• Pathogenesis of mucormycosis. (2012, background): “It functions as a major chaperone that is involved in many cellular processes, including protein folding and assembly, marking misfolded proteins for proteosome degradation [48], regulating calcium homeostasis, and serving as a sensor for endoplasmic reticulum stress [49].”