ArticleRNA (New York, N.Y.)2006
Structural study of the H/ACA snoRNP components Nop10p and the 3' hairpin of U65 snoRNA.
Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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
18 citing papers in PubMed, 37 citations in OpenAlex.
- The importance of pseudouridylation: human disorders related to the fifth nucleoside.Biologia futura · 2023Review
- Transcriptome-wide mapping reveals a diverse dihydrouridine landscape including mRNA.PLoS biology · 2022Article
- Small but strong: Pivotal roles and potential applications of snoRNAs in hematopoietic malignancies.Frontiers in oncology · 2022Review
- H/ACA Small Ribonucleoproteins: Structural and Functional Comparison Between Archaea and Eukaryotes.Frontiers in microbiology · 2021Review
- Pseudouridylation defect due toProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Reconstitution and structural analysis of the yeast box H/ACA RNA-guided pseudouridine synthase.Genes & development · 2011Article
- The box H/ACA ribonucleoprotein complex: interplay of RNA and protein structures in post-transcriptional RNA modification.The Journal of biological chemistry · 2010Review
- Different mechanisms for pseudouridine formation in yeast 5S and 5.8S rRNAs.Molecular and cellular biology · 2008Article
- Unveiling substrate RNA binding to H/ACA RNPs: one side fits all.Current opinion in structural biology · 2008Review
- Genetic heterogeneity in autosomal recessive dyskeratosis congenita with one subtype due to mutations in the telomerase-associated protein NOP10.Human molecular genetics · 2007Article
- H/ACA small nucleolar RNA pseudouridylation pockets bind substrate RNA to form three-way junctions that position the target U for modification.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Identification of determinants in the protein partners aCBF5 and aNOP10 necessary for the tRNA:Psi55-synthase and RNA-guided RNA:Psi-synthase activities.Nucleic acids research · 2007Article
- The structure and function of small nucleolar ribonucleoproteins.Nucleic acids research · 2007Review
- Analysis of the binding of the N-terminal conserved domain of yeast Cbf5p to a box H/ACA snoRNA.RNA (New York, N.Y.) · 2006Article
- How a single protein complex accommodates many different H/ACA RNAs.Trends in biochemical sciences · 2006Review
- hNaf1 is required for accumulation of human box H/ACA snoRNPs, scaRNPs, and telomerase.RNA (New York, N.Y.) · 2006Article
- Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5-aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity.Nucleic acids research · 2006Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The H/ACA small nucleolar ribonucleoprotein (snoRNP) complexes guide the modification of uridine to pseudouridine at conserved sites in rRNA. The H/ACA snoRNPs each comprise a target-site-specific snoRNA and four core proteins, Nop10p, Nhp2p, Gar1p, and the pseudouridine synthase, Cbf5p, in yeast. The secondary structure of the H/ACA snoRNAs includes two hairpins that each contain a large internal loop (the pseudouridylation pocket), one or both of which are partially complementary to the target RNA(s). We have determined the solution structure of an RNA hairpin derived from the human U65 box H/ACA snoRNA including the pseudouridylation pocket and adjacent stems, providing the first three-dimensional structural information on these H/ACA snoRNAs. We have also determined the structure of Nop10p and investigated its interaction with RNA using NMR spectroscopy. Nop10p contains a structurally well-defined N-terminal region composed of a beta-hairpin, and the rest of the protein lacks a globular structure. Chemical shift mapping of the interaction of RNA constructs of U65 box H/ACA 3' hairpin with Nop10p shows that the beta-hairpin binds weakly but specifically to RNA. The unstructured region of Nop10p likely interacts with Cbf5p.
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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.