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A Proteome-wide, Quantitative Survey of In Vivo Ubiquitylation Sites Reveals Widespread Regulatory Roles
Post-translational modification of proteins by ubiquitin is a fundamentally important regulatory mechanism. However, proteome-wide analysis of endogenous ubiquitylation remains a challenging task, and almost always has relied on cells expressing affinity tagged ubiquitin. Here we combine single-step...
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| Asıl Yazarlar: | , , , , , , |
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| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
The American Society for Biochemistry and Molecular Biology
2011
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3205876/ https://ncbi.nlm.nih.gov/pubmed/21890473 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/mcp.M111.013284 |
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