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March 18, 2013Proceedings of the National Academy of SciencesOpen Access

Activity-enhancing mutations in an E3 ubiquitin ligase identified by high-throughput mutagenesis

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Authors

LSLea M. StaritaUniversity of WashingtonJPJonathan N. PrunedaOregon Health & Science UniversityRLRussell S. LoPacific Northwest Diabetes Research Institute

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Starita et al. (2013) studied this question.

synapsesocial.com/papers/6a718e84ac440176ef2a3652https://doi.org/10.1073/pnas.1303309110
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Also Consider

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  1. 1Stability of thioester intermediates in ubiquitin‐like modifications2009 · 23 citations
  2. 2Identification of an unconventional E3 binding surface on the UbcH5 ∼ Ub conjugate recognized by a pathogenic bacterial E3 ligase.2010 · 66 citations
  3. 3Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex2003 · 352 citations