Evidence map›Paper›PMID 21816274›Full record

ArticleCell2011

Structure of a key intermediate of the SMN complex reveals Gemin2's crucial function in snRNP assembly.

Rundong Zhang, Byung Ran So, Pilong Li, Jeongsik Yong, Tina Glisovic, Lili Wan, Gideon Dreyfuss

Abstract read
In one paragraph

Article in Cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

83 citing papers in PubMed, 139 citations in OpenAlex.

  1. Article
  2. Article
  3. Microbiology (Reading, England) · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Spinal muscular atrophy: Biology, pathogenesis, and therapeutic advances.Therapeutic advances in neurological disorders · 2026
    Review
  8. Article
  9. Application of Biomarkers in Spinal Muscular Atrophy.International journal of molecular sciences · 2025
    Review
  10. AProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Review
  13. A unique mechanism of snRNP core assembly.Nature communications · 2025
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Frontiers in genetics · 2024
    Article
  19. Article
  20. Review

23 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 2 institutions in 1 country.

Rundong ZhangHoward Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6148, USA.
Byung Ran So
Pilong Li
Jeongsik Yong
Tina Glisovic
Lili Wan
Gideon Dreyfuss
Howard Hughes Medical Institute · USUniversity of Pennsylvania · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The SMN complex mediates the assembly of heptameric Sm protein rings on small nuclear RNAs (snRNAs), which are essential for snRNP function. Specific Sm core assembly depends on Sm proteins and snRNA recognition by SMN/Gemin2- and Gemin5-containing subunits, respectively. The mechanism by which the Sm proteins are gathered while preventing illicit Sm assembly on non-snRNAs is unknown. Here, we describe the 2.5 Å crystal structure of Gemin2 bound to SmD1/D2/F/E/G pentamer and SMN's Gemin2-binding domain, a key assembly intermediate. Remarkably, through its extended conformation, Gemin2 wraps around the crescent-shaped pentamer, interacting with all five Sm proteins, and gripping its bottom and top sides and outer perimeter. Gemin2 reaches into the RNA-binding pocket, preventing RNA binding. Interestingly, SMN-Gemin2 interaction is abrogated by a spinal muscular atrophy (SMA)-causing mutation in an SMN helix that mediates Gemin2 binding. These findings provide insight into SMN complex assembly and specificity, linking snRNP biogenesis and SMA pathogenesis.

Indexed as

Amino Acid SequenceAnimalsCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataMuscular Atrophy, SpinalMutationNerve Tissue ProteinsRibonucleoproteins, Small NuclearRNA-Binding ProteinsSequence AlignmentSMN Complex ProteinsGEMIN2 protein, humanNerve Tissue ProteinsRibonucleoproteins, Small NuclearRNA-Binding ProteinsSMN Complex Proteins

Identifiers

PMID21816274
PMCPMC3160754
OpenAlexW2048369796

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.