Targeting Phosphorylation of Eukaryotic Initiation Factor-2α to Treat Human Disease
Progress in Molecular Biology and Translational Science, ISSN: 1877-1173, Vol: 106, Page: 75-106
2012
- 35Citations
- 68Captures
Metric Options: CountsSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations35
- Citation Indexes34
- CrossRef34
- 34
- Patent Family Citations1
- Patent Families1
- Captures68
- Readers68
- 62
Book Chapter Description
The unfolded protein response, also known as endoplasmic reticulum (ER) stress, has been implicated in numerous human diseases, including atherosclerosis, cancer, diabetes, and neurodegenerative disorders. Protein misfolding activates one or more of the three ER transmembrane sensors to initiate a complex network of signaling that transiently suppresses protein translation while also enhancing protein folding and proteasomal degradation of misfolded proteins to ensure full recovery from ER stress. Gene disruption studies in mice have provided critical insights into the role of specific signaling components and pathways in the differing responses of animal tissues to ER stress. These studies have emphasized an important contribution of translational repression to sustained insulin synthesis and β-cell viability in experimental models of type-2 diabetes. This has focused attention on the recently discovered small-molecule inhibitors of eIF2α phosphatases that prolong eIF2α phosphorylation to reduce cell death in several animal models of human disease. These compounds show significant cytoprotection in cellular and animal models of neurodegenerative disorders, highlighting a potential strategy for future development of drugs to treat human protein misfolding disorders.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/B9780123964564000055; http://dx.doi.org/10.1016/b978-0-12-396456-4.00005-5; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84857207261&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/22340715; http://linkinghub.elsevier.com/retrieve/pii/B9780123964564000055; https://linkinghub.elsevier.com/retrieve/pii/B9780123964564000055
Elsevier BV
Provide Feedback
Have ideas for a new metric? Would you like to see something else here?Let us know