ArticleDoklady. Biochemistry and biophysics2019
Multifunctional ENY2 Protein Interacts with RNA Helicase MLE.
Article in Doklady. Biochemistry and biophysics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- MLE/DHX9 without Helicase Activity Activates Constitutive Expression of Nuclear Receptor Genes in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2025Article
- Evolutionarily Conserved DHX9/MLE Helicase Is Involved in the Regulation of Its Own mRNA Expression Level in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2025Article
- MLE Helicase Is a New Participant in the Transcription Regulation of the ftz-f1 Gene Encoding Nuclear Receptor in Higher Eukaryotes.Doklady. Biochemistry and biophysics · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ENY2 protein of Drosophila melanogaster was previously discovered and characterized in our laboratory [1, 2]. It was found that ENY2 is a subunit of several multiprotein complexes and connects various stages of gene expression [3-5]. This work is devoted to studying the interaction of ENY2 with RNA helicase MLE. This interaction was confirmed by independent methods. Data indicating that this interaction is conserved in evolution and is important for the functioning of MLE in both sexes were obtained.
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