The assembly pathway of the 19S regulatory particle of the yeast 26S proteasome
Molecular Biology of the Cell, ISSN: 1059-1524, Vol: 18, Issue: 2, Page: 569-580
2007
- 90Citations
- 77Captures
- 2Mentions
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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
- Citations90
- Citation Indexes90
- 90
- CrossRef83
- Captures77
- Readers77
- 77
- Mentions2
- References2
- 2
Article Description
The 26S proteasome consists of the 20S proteasome (core particle) and the 19S regulatory particle made of the base and lid substructures, and it is mainly localized in the nucleus in yeast. To examine how and where this huge enzyme complex is assembled, we performed biochemical and microscopic characterization of proteasomes produced in two lid mutants, rpn5-1 and rpn7-3, and a base mutant ΔN rpn2, of the yeast Saccharomyces cerevisiae. We found that, although lid formation was abolished in rpn5-1 mutant cells at the restrictive temperature, an apparently intact base was produced and localized in the nucleus. In contrast, in ΔN rpn2 cells, a free lid was formed and localized in the nucleus even at the restrictive temperature. These results indicate that the modules of the 26S proteasome, namely, the core particle, base, and lid, can be formed and imported into the nucleus independently of each other. Based on these observations, we propose a model for the assembly process of the yeast 26S proteasome. © 2007 by The American Society for Cell Biology.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33846842251&origin=inward; http://dx.doi.org/10.1091/mbc.e06-07-0635; http://www.ncbi.nlm.nih.gov/pubmed/17135287; https://www.molbiolcell.org/doi/10.1091/mbc.e06-07-0635; http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-07-0635; http://www.molbiolcell.org/content/18/2/569
American Society for Cell Biology (ASCB)
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