Evidence map›Paper›PMID 26829225›Full record

ArticleNature2016

Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 Å resolution.

Thi Hoang Duong Nguyen, Wojciech P Galej, Xiao-Chen Bai, Chris Oubridge, Andrew J Newman, Sjors H W Scheres, Kiyoshi Nagai

Open access · greenAbstract read
In one paragraph

Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 131 papers.

0numbers the graph read from it
0cells of the map it votes in
131citing papers in PubMed
24.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

131 citing papers in PubMed, 217 citations in OpenAlex.

  1. Article
  2. Microbiology (Reading, England) · 2026
    Review
  3. Article
  4. Article
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  6. Article
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  10. Cryo-EM heterogeneity analysis using regularized covariance estimation and kernel regression.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Allosteric activation of VCP, an AAA unfoldase, by small molecule mimicry.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
  19. Sample Preparation for Electron Cryo-Microscopy of Macromolecular Machines.Advances in experimental medicine and biology · 2024
    Article
  20. Article

71 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Thi Hoang Duong Nguyen *MRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH UK.
Wojciech P Galej *MRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH UK.
Xiao-Chen BaiMRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH UK.
Chris OubridgeMRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH UK.
Andrew J NewmanMRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH UK.
Sjors H W ScheresMRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH UK.
Kiyoshi NagaiMRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH UK.
MRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184330Medical Research Council MC_UP_A025_1013
6 · The paper itself

Abstract

U4/U6.U5 tri-snRNP represents a substantial part of the spliceosome before activation. A cryo-electron microscopy structure of Saccharomyces cerevisiae U4/U6.U5 tri-snRNP at 3.7 Å resolution led to an essentially complete atomic model comprising 30 proteins plus U4/U6 and U5 small nuclear RNAs (snRNAs). The structure reveals striking interweaving interactions of the protein and RNA components, including extended polypeptides penetrating into subunit interfaces. The invariant ACAGAGA sequence of U6 snRNA, which base-pairs with the 5'-splice site during catalytic activation, forms a hairpin stabilized by Dib1 and Prp8 while the adjacent nucleotides interact with the exon binding loop 1 of U5 snRNA. Snu114 harbours GTP, but its putative catalytic histidine is held away from the γ-phosphate by hydrogen bonding to a tyrosine in the amino-terminal domain of Prp8. Mutation of this histidine to alanine has no detectable effect on yeast growth. The structure provides important new insights into the spliceosome activation process leading to the formation of the catalytic centre.

Indexed as

Cryoelectron MicroscopyBase PairingCatalytic DomainDNA HelicasesExonsGuanosine TriphosphateHydrogen BondingModels, MolecularNucleic Acid ConformationRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearRNA, Small NuclearRNA Splice SitesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA HelicasesGuanosine TriphosphateHCS1 protein, S cerevisiaePRP8 protein, S cerevisiaeRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearRNA, Small NuclearRNA Splice SitesSaccharomyces cerevisiae ProteinsSNU114 protein, S cerevisiae(U4-U6.U5)tri-snRNP-specific protein, S cerevisiaeU5 small nuclear RNA

Identifiers

PMID26829225
PMCPMC4762201
OpenAlexW2259134357

What OpenQuestion holds

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Registered trials

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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.