ArticleSilence2010
Solution structure of the Drosha double-stranded RNA-binding domain.
Article in Silence, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed, 31 citations in OpenAlex.
- Mechanism by which T7 bacteriophage protein Gp1.2 inhibitsProceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Structural View of miRNA Biogenesis and Function.Non-coding RNA · 2022Review
- Evaluation of the clinical significance of RNase III enzyme DROSHA in pediatrics acute lymphocytic leukemia.Molecular biology reports · 2021Article
- Article
- Viral RNA intermediates as targets for detection and discovery of novel and emerging mosquito-borne viruses.PLoS neglected tropical diseases · 2015Article
- From guide to target: molecular insights into eukaryotic RNA-interference machinery.Nature structural & molecular biology · 2015Review
- RNA recognition by double-stranded RNA binding domains: a matter of shape and sequence.Cellular and molecular life sciences : CMLS · 2013Review
- Intrinsic dynamics of an extended hydrophobic core in the S. cerevisiae RNase III dsRBD contributes to recognition of specific RNA binding sites.Journal of molecular biology · 2013Article
- RNA targets and specificity of Staufen, a double-stranded RNA-binding protein in Caenorhabditis elegans.The Journal of biological chemistry · 2013Article
- Molecular mechanisms of RNA interference.Annual review of biophysics · 2013Review
- Biogenesis of mammalian microRNAs: a global view.Genomics, proteomics & bioinformatics · 2012Review
- Biogenesis and mechanism of action of small non-coding RNAs: insights from the point of view of structural biology.International journal of molecular sciences · 2012Review
- Dynamic origins of differential RNA binding function in two dsRBDs from the miRNA "microprocessor" complex.Biochemistry · 2010Article
- Indian journal of medical and paediatric oncology : official journal of Indian Society of Medical & Paediatric OncologyArticle
- Ribonuclease III mechanisms of double-stranded RNA cleavage.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundDrosha is a nuclear RNase III enzyme that initiates processing of regulatory microRNA. Together with partner protein DiGeorge syndrome critical region 8 (DGCR8), it forms the Microprocessor complex, which cleaves precursor transcripts called primary microRNA to produce hairpin precursor microRNA. In addition to two RNase III catalytic domains, Drosha contains a C-terminal double-stranded RNA-binding domain (dsRBD). To gain insight into the function of this domain, we determined the nuclear magnetic resonance (NMR) solution structure.
resultsWe report here the solution structure of the dsRBD from Drosha (Drosha-dsRBD). The alphabetabetabetaalpha fold is similar to other dsRBD structures. A unique extended loop distinguishes this domain from other dsRBDs of known structure.
conclusionsDespite uncertainties about RNA-binding properties of the Drosha-dsRBD, its structure suggests it retains RNA-binding features. We propose that this domain may contribute to substrate recognition in the Drosha-DGCR8 Microprocessor complex.
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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.