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Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine
RING finger proteins constitute the large majority of ubiquitin ligases (E3s) and function by interacting with ubiquitin-conjugating enzymes (E2s) charged with ubiquitin. How low-affinity RING–E2 interactions result in highly processive substrate ubiquitination is largely unknown. The RING E3, gp78,...
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| Main Authors: | , , , , , , , , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
European Molecular Biology Organization
2013
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3770950/ https://ncbi.nlm.nih.gov/pubmed/23942235 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/emboj.2013.174 |
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