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• W2010053735 abstract "Significance Ubiquitin is a 76 residue protein that is attached to target proteins as a posttranslational modification. This modification is dependent on the successive activity of three enzymes, designated E1, E2, and E3. We developed a high-throughput mutagenesis strategy to probe the mechanism of E3-catalyzed transfer of ubiquitin from the E2 to the target protein. By scoring the effect of nearly 100,000 mutations in an E3, we identified mutations that affect direct and allosteric interactions between the E3 and the E2. These results highlight the general utility of high-throughput mutagenesis in delineating the molecular basis of enzyme activity." @default.
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• W2010053735 date "2013-03-18" @default.
• W2010053735 modified "2023-10-15" @default.
• W2010053735 title "Activity-enhancing mutations in an E3 ubiquitin ligase identified by high-throughput mutagenesis" @default.
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• W2010053735 doi "https://doi.org/10.1073/pnas.1303309110" @default.
• W2010053735 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3619334" @default.
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