ArticleThe EMBO journal1995
NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 101 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
101 citing papers in PubMed, 261 citations in OpenAlex.
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- Functional Role of RBP in Osteosarcoma: Regulatory Mechanism and Clinical Therapy.Analytical cellular pathology (Amsterdam) · 2023Review
- Crocodilepox Virus Protein 157 Is an Independently Evolved Inhibitor of Protein Kinase R.Viruses · 2022Article
- Redefining the architecture of ferlin proteins: Insights into multi-domain protein structure and function.PloS one · 2022Article
- Modulation of MicroRNA Processing by Dicer via Its Associated dsRNA Binding Proteins.Non-coding RNA · 2021Review
- To protect and modify double-stranded RNA - the critical roles of ADARs in development, immunity and oncogenesis.Critical reviews in biochemistry and molecular biology · 2021Review
- A multipronged approach to understanding the form and function of hStaufen protein.RNA (New York, N.Y.) · 2020Article
- Cancer the'RBP'eutics-RNA-binding proteins as therapeutic targets for cancer.Pharmacology & therapeutics · 2019Review
- The crystal structure of Staufen1 in complex with a physiological RNA sheds light on substrate selectivity.Life science alliance · 2018Article
- Molecular basis for asymmetry sensing of siRNAs by the Drosophila Loqs-PD/Dcr-2 complex in RNA interference.Nucleic acids research · 2017Article
- NF90-NF45 is a selective RNA chaperone that rearranges viral and cellular riboswitches: biochemical analysis of a virus host factor activity.Nucleic acids research · 2017Article
- ADAR RNA editing in human disease; more to it than meets the I.Human genetics · 2017Review
- AtMBD6, a methyl CpG binding domain protein, maintains gene silencing in Arabidopsis by interacting with RNA binding proteins.Journal of biosciences · 2017Article
- The protein domains of the Dictyostelium microprocessor that are required for correct subcellular localization and for microRNA maturation.RNA biology · 2016Article
- New Insights into the Biological Role of Mammalian ADARs; the RNA Editing Proteins.Biomolecules · 2015Review
- Homoiterons and expansion in ribosomal RNAs.FEBS open bio · 2015Article
- APTE: identification of indirect read-out A-DNA promoter elements in genomes.BMC bioinformatics · 2014Article
- 'Black sheep' that don't leave the double-stranded RNA-binding domain fold.Trends in biochemical sciences · 2014Review
- A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
41 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The double-stranded RNA binding domain (dsRBD) is an approximately 65 amino acid motif that is found in a variety of proteins that interact with double-stranded (ds) RNA, such as Escherichia coli RNase III and the dsRNA-dependent kinase, PKR. Drosophila staufen protein contains five copies of this motif, and the third of these binds dsRNA in vitro. Using multinuclear/multidimensional NMR methods, we have determined that staufen dsRBD3 forms a compact protein domain with an alpha-beta-beta-beta-alpha structure in which the two alpha-helices lie on one face of a three-stranded anti-parallel beta-sheet. This structure is very similar to that of the N-terminal domain of a prokaryotic ribosomal protein S5. Furthermore, the consensus derived from all known S5p family sequences shares several conserved residues with the dsRBD consensus sequence, indicating that the two domains share a common evolutionary origin. Using in vitro mutagenesis, we have identified several surface residues which are important for the RNA binding of the dsRBD, and these all lie on the same side of the domain. Two residues that are essential for RNA binding, F32 and K50, are also conserved in the S5 protein family, suggesting that the two domains interact with RNA in a similar way.
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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.