ArticleNature2011
Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis.
Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 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
75 citing papers in PubMed, 130 citations in OpenAlex.
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- Monoallelic and biallelic RNU4-2 variants in neurodevelopmental disorders.Journal of human genetics · 2026Article
- Review
- Clinical significance of SNRPD1 expression in predicting post-transplant recurrence of hepatocellular carcinoma.American journal of translational research · 2026Article
- Development of a Modular Ribonucleoprotein Complex as a General Strategy to Deliver RNAi Therapeutics.Advanced healthcare materials · 2025Article
- Interconversion and mechanisms between Lsm-type and Sm-type heteroheptameric rings: implications for spliceosome evolution and RNA metabolism.Nucleic acids research · 2025Article
- Alternative Splicing: A Critical Regulator in Human Bone Biology and Tumor Progression.Research (Washington, D.C.) · 2025Review
- Mutations in the U4 snRNA gene RNU4-2 cause one of the most prevalent monogenic neurodevelopmental disorders.Nature medicine · 2024Article
- Systematic discovery of protein interaction interfaces using AlphaFold and experimental validation.Molecular systems biology · 2024Article
- In vitro methylation of the U7 snRNP subunits Lsm11 and SmE by the PRMT5/MEP50/pICln methylosome.RNA (New York, N.Y.) · 2023Article
- The SMN complex drives structural changes in human snRNAs to enable snRNP assembly.Nature communications · 2023Article
- Ontology Specific Alternative Splicing Changes in Alzheimer's Disease.Frontiers in genetics · 2022Article
- U7 deciphered: the mechanism that forms the unusual 3' end of metazoan replication-dependent histone mRNAs.Biochemical Society transactions · 2021Review
- Human spliceosomal snRNA sequence variants generate variant spliceosomes.RNA (New York, N.Y.) · 2021Article
- Engineering Crystal Packing in RNA-Protein Complexes II: A Historical Perspective from the Structural Studies of the Spliceosome.Crystals · 2021Article
- Engineering Crystal Packing in RNA Structures I: Past and Future Strategies for Engineering RNA Packing in Crystals.Crystals · 2021Article
- psiCLIP reveals dynamic RNA binding by DEAH-box helicases before and after exon ligation.Nature communications · 2021Article
- Reconstitution and biochemical assays of an active human histone pre-mRNA 3'-end processing machinery.Methods in enzymology · 2021Article
- Molecular basis for the distinct cellular functions of the Lsm1-7 and Lsm2-8 complexes.RNA (New York, N.Y.) · 2020Article
- Composition and processing activity of a semi-recombinant holo U7 snRNP.Nucleic acids research · 2020Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The spliceosome is a dynamic macromolecular machine that assembles on pre-messenger RNA substrates and catalyses the excision of non-coding intervening sequences (introns). Four of the five major components of the spliceosome, U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), contain seven Sm proteins (SmB/B', SmD1, SmD2, SmD3, SmE, SmF and SmG) in common. Following export of the U1, U2, U4 and U5 snRNAs to the cytoplasm, the seven Sm proteins, chaperoned by the survival of motor neurons (SMN) complex, assemble around a single-stranded, U-rich sequence called the Sm site in each small nuclear RNA (snRNA), to form the core domain of the respective snRNP particle. Core domain formation is a prerequisite for re-import into the nucleus, where these snRNPs mature via addition of their particle-specific proteins. Here we present a crystal structure of the U4 snRNP core domain at 3.6 Å resolution, detailing how the Sm site heptad (AUUUUUG) binds inside the central hole of the heptameric ring of Sm proteins, interacting one-to-one with SmE-SmG-SmD3-SmB-SmD1-SmD2-SmF. An irregular backbone conformation of the Sm site sequence combined with the asymmetric structure of the heteromeric protein ring allows each base to interact in a distinct manner with four key residues at equivalent positions in the L3 and L5 loops of the Sm fold. A comparison of this structure with the U1 snRNP at 5.5 Å resolution reveals snRNA-dependent structural changes outside the Sm fold, which may facilitate the binding of particle-specific proteins that are crucial to biogenesis of spliceosomal snRNPs.
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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.