The functions and effects of CUL3-E3 ligases mediated non-degradative ubiquitination
Gene, ISSN: 0378-1119, Vol: 832, Page: 146562
2022
- 12Citations
- 10Captures
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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
- Citations12
- Citation Indexes12
- 12
- CrossRef2
- Captures10
- Readers10
- 10
Review Description
Ubiquitination of substrates usually have two fates: one is degraded by 26S proteasome, and the other is non-degradative ubiquitination modification which is associated with cell cycle regulation, chromosome inactivation, protein transportation, tumorigenesis, achondroplasia, and neurological diseases. Cullin3 (CUL3), a scaffold protein, binding with the Bric-a-Brac-Tramtrack-Broad-complex (BTB) domain of substrates recognition adaptor and RING-finger protein 1 (RBX1) form ubiquitin ligases (E3). Based on the current researches, this review has summarized the functions and effects of CUL3-E3 ligases mediated non-degradative ubiquitination.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S037811192200381X; http://dx.doi.org/10.1016/j.gene.2022.146562; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85130974821&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/35580799; https://linkinghub.elsevier.com/retrieve/pii/S037811192200381X; https://dx.doi.org/10.1016/j.gene.2022.146562
Elsevier BV
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