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December 17, 2016Protein ScienceOpen Access

Tuning BRCA1 and BARD1 activity to investigate RING ubiquitin ligase mechanisms

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Authors

MSMikaela D. StewartTexas Christian UniversityEDEmily D. DuncanECErnesto CoronadoUniversity of Washington

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Stewart et al. (2016) studied this question.

synapsesocial.com/papers/6aa69708041e43fea73a7c32https://doi.org/10.1002/pro.3091
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Also Consider

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  1. 1Massively Parallel Functional Analysis of BRCA1 RING Domain Variants2015 · 356 citations
  2. 2Activity-enhancing mutations in an E3 ubiquitin ligase identified by high-throughput mutagenesis2013 · 208 citations
  3. 3The RING Heterodimer BRCA1-BARD1 Is a Ubiquitin Ligase Inactivated by a Breast Cancer-derived Mutation2001 · 641 citations
  4. 4BRCA1 Tumor Suppression Depends on BRCT Phosphoprotein Binding, But Not Its E3 Ligase Activity2011 · 252 citations
  5. 5E2 enzymes: more than just middle men2016 · 633 citations