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Phosphorylation of ubiquitin at Ser65 affects its polymerization, targets, and proteome-wide turnover
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin can itself be phosphorylated at nearly every serine, threonine, and tyrosine residue. However, the effect of this modification on ubiquitin function...
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| Udgivet i: | EMBO Rep |
|---|---|
| Main Authors: | , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
John Wiley & Sons, Ltd
2015
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4576982/ https://ncbi.nlm.nih.gov/pubmed/26142280 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.15252/embr.201540298 |
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