Bimolecular fluorescence complementation to assay the interactions of ubiquitylation enzymes in living yeast cells
Methods in Molecular Biology, ISSN: 1064-3745, Vol: 1449, Page: 223-241
2016
- 4Citations
- 14Captures
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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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Metrics Details
- Citations4
- Citation Indexes4
- Captures14
- Readers14
- 14
Book Chapter Description
Ubiquitylation is a versatile posttranslational protein modification catalyzed through the concerted action of ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s). These enzymes form transient complexes with each other and their modification substrates and determine the nature of the ubiquitin signals attached to their substrates. One challenge in the field of protein ubiquitylation is thus to identify the E2-E3 pairs that function in the cell. In this chapter, we describe the use of bimolecular fluorescence complementation to assay E2-E3 interactions in living cells, using budding yeast as a model organism.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84987808243&origin=inward; http://dx.doi.org/10.1007/978-1-4939-3756-1_13; http://www.ncbi.nlm.nih.gov/pubmed/27613039; http://link.springer.com/10.1007/978-1-4939-3756-1_13; https://dx.doi.org/10.1007/978-1-4939-3756-1_13; https://link.springer.com/protocol/10.1007/978-1-4939-3756-1_13
Springer Nature
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