S6k1- and βTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth
Science, ISSN: 0036-8075, Vol: 314, Issue: 5798, Page: 467-471
2006
- 616Citations
- 309Captures
- 5Mentions
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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.
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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
- Citations616
- Citation Indexes616
- 616
- CrossRef573
- Captures309
- Readers309
- 309
- Mentions5
- References4
- Wikipedia4
- News Mentions1
- News1
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Article Description
The tumor suppressor programmed cell death protein 4 (PDCD4) inhibits the translation initiation factor eIF4A, an RNA helicase that catalyzes the unwinding of secondary structure at the 5′ untranslated region (5′UTR) of messenger RNAs (mRNAs). In response to mitogens, PDCD4 was rapidly phosphorylated on Ser by the protein kinase S6K1 and subsequently degraded via the ubiquitin ligase SCF. Expression in cultured cells of a stable PDCD4 mutant that is unable to bind βTRCP inhibited translation of an mRNA with a structured 5′UTR, resulted in smaller cell size, and slowed down cell cycle progression. We propose that regulated degradation of PDCD4 in response to mitogens allows efficient protein synthesis and consequently cell growth.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33750325725&origin=inward; http://dx.doi.org/10.1126/science.1130276; http://www.ncbi.nlm.nih.gov/pubmed/17053147; https://facultyopinions.com/prime/1047973#eval498004; http://dx.doi.org/10.3410/f.1047973.498004; https://facultyopinions.com/prime/1047973#eval505767; http://dx.doi.org/10.3410/f.1047973.505767; https://www.science.org/doi/10.1126/science.1130276; https://dx.doi.org/10.1126/science.1130276; https://www.science.org/lookup/doi/10.1126/science.1130276; https://science.sciencemag.org/content/314/5798/467; https://science.sciencemag.org/content/314/5798/467.abstract; https://science.sciencemag.org/content/sci/314/5798/467.full.pdf; http://science.sciencemag.org/lookup/doi/10.1126/science.1130276; http://science.sciencemag.org/content/314/5798/467; http://science.sciencemag.org/content/314/5798/467.abstract; http://science.sciencemag.org/content/314/5798/467.full.pdf; http://f1000.com/1047973#eval498004; http://f1000.com/1047973#eval505767; http://www.sciencemag.org/cgi/doi/10.1126/science.1130276; https://www.sciencemag.org/lookup/doi/10.1126/science.1130276; http://science.sciencemag.org/cgi/doi/10.1126/science.1130276; https://www.science.org/doi/abs/10.1126/science.1130276
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