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An invisible ubiquitin conformation is required for efficient phosphorylation by PINK1
The Ser/Thr protein kinase PINK1 phosphorylates the well‐folded, globular protein ubiquitin (Ub) at a relatively protected site, Ser65. We previously showed that Ser65 phosphorylation results in a conformational change in which Ub adopts a dynamic equilibrium between the known, common Ub conformatio...
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| Publicado en: | EMBO J |
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| Autores principales: | , , , , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
John Wiley and Sons Inc.
2017
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5730886/ https://ncbi.nlm.nih.gov/pubmed/29133469 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.15252/embj.201797876 |
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