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- W2767754387 endingPage "e0187571" @default.
- W2767754387 startingPage "e0187571" @default.
- W2767754387 abstract "Ubiquitination is a crucial post-translational modification that can target proteins for degradation. The E3 ubiquitin ligases are responsible for recognizing substrate proteins for ubiquitination, hence providing specificity to the process of protein degradation. Here, we describe a genetic modifier screen that identified E3 ligases that modified the rough-eye phenotype generated by expression of cindrRNAi transgenes during Drosophila eye development. In total, we identified 36 E3 ligases, as well as 4 Cullins, that modified the mild cindrRNA mis-patterning phenotype. This indicates possible roles for these E3s/Cullins in processes that require Cindr function, including cytoskeletal regulation, cell adhesion, cell signaling and cell survival. Three E3 ligases identified in our screen had previously been linked to regulating JNK signaling." @default.
- W2767754387 created "2017-11-17" @default.
- W2767754387 creator A5018637906 @default.
- W2767754387 creator A5035031500 @default.
- W2767754387 creator A5044381716 @default.
- W2767754387 date "2017-11-08" @default.
- W2767754387 modified "2023-09-27" @default.
- W2767754387 title "A screen for E3 ubiquitination ligases that genetically interact with the adaptor protein Cindr during Drosophila eye patterning" @default.
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- W2767754387 doi "https://doi.org/10.1371/journal.pone.0187571" @default.
- W2767754387 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5678704" @default.
- W2767754387 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29117266" @default.
- W2767754387 hasPublicationYear "2017" @default.
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