ArticleScientific reports2014
Structural model of ubiquitin transfer onto an artificial RING finger as an E3 ligase.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Solution structure of the zinc finger domain of human RNF144A ubiquitin ligase.Protein science : a publication of the Protein Society · 2020Article
- Zinc finger domain of the human DTX protein adopts a unique RING fold.Protein science : a publication of the Protein Society · 2019Article
- Unique RING finger structure from the human HRD1 protein.Protein science : a publication of the Protein Society · 2019Article
- Unique auto-ubiquitination activities of artificial RING fingers in cancer cells.Protein science : a publication of the Protein Society · 2018Article
- Concise machinery for monitoring ubiquitination activities using novel artificial RING fingers.Protein science : a publication of the Protein Society · 2018Review
- Solution structure of the PHD finger from the human KIAA1045 protein.Protein science : a publication of the Protein Society · 2018Article
- The unique N-terminal zinc finger of synaptotagmin-like protein 4 reveals FYVE structure.Protein science : a publication of the Protein Society · 2017Article
- The zinc finger domain of RING finger protein 141 reveals a unique RING fold.Protein science : a publication of the Protein Society · 2017Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The artificial WSTF PHD_EL5 RING finger was designed via "α-helical region substitution", and its structural model for the attachment of activated ubiquitin has been demonstrated. Chemical modifications of Cys residues, the circular dichroism spectra, and substrate-independent ubiquitination assays illustrated that the WSTF PHD_EL5 RING finger has E3 activity, and it is ubiquitinated via Lys14. Homology modeling calculations revealed that the WSTF PHD_EL5 RING finger possesses a classical RING fold for specific E2-E3 binding. The docking poses of the WSTF PHD_EL5 RING finger with the UbcH5b-ubiquitin conjugate provided insight into its functional E2 interaction and development of ubiquitination at the atomic level. The structural model of the artificial WSTF PHD_EL5 RING finger proposed by the present work is useful and may help to extend the strategy of α-helical region substitution.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.