Evidence map›Paper›PMID 10601333›Full record

ArticleThe Journal of cell biology1999

Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems.

B Charroux, L Pellizzoni, R A Perkinson, A Shevchenko, M Mann, G Dreyfuss

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed, 1 pooled it
15.2field-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

123 citing papers in PubMed, 1 synthesis or guideline pooled it, 268 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Spinal muscular atrophy: Biology, pathogenesis, and therapeutic advances.Therapeutic advances in neurological disorders · 2026
    Review
  6. Review
  7. A unique mechanism of snRNP core assembly.Nature communications · 2025
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. DDX20: A Multifunctional Complex Protein.Molecules (Basel, Switzerland) · 2023
    Review
  14. Article
  15. Article
  16. Non-ubiquitous expression of core spliceosomal protein SmB/B' in chick and mouse embryos.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Article
  17. Review
  18. Review
  19. Article
  20. Article

63 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

6 authors at 4 institutions in 3 countries.

B CharrouxHoward Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6148, USA.
L Pellizzoni
R A Perkinson
A Shevchenko
M Mann
G Dreyfuss
Howard Hughes Medical Institute · USUniversity of Pennsylvania · USEuropean Molecular Biology Laboratory · DEUniversity of Southern Denmark · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The survival of motor neurons (SMN) gene is the disease gene of spinal muscular atrophy (SMA), a common motor neuron degenerative disease. The SMN protein is part of a complex containing several proteins, of which one, SIP1 (SMN interacting protein 1), has been characterized so far. The SMN complex is found in both the cytoplasm and in the nucleus, where it is concentrated in bodies called gems. In the cytoplasm, SMN and SIP1 interact with the Sm core proteins of spliceosomal small nuclear ribonucleoproteins (snRNPs), and they play a critical role in snRNP assembly. In the nucleus, SMN is required for pre-mRNA splicing, likely by serving in the regeneration of snRNPs. Here, we report the identification of another component of the SMN complex, a novel DEAD box putative RNA helicase, named Gemin3. Gemin3 interacts directly with SMN, as well as with SmB, SmD2, and SmD3. Immunolocalization studies using mAbs to Gemin3 show that it colocalizes with SMN in gems. Gemin3 binds SMN via its unique COOH-terminal domain, and SMN mutations found in some SMA patients strongly reduce this interaction. The presence of a DEAD box motif in Gemin3 suggests that it may provide the catalytic activity that plays a critical role in the function of the SMN complex on RNPs.

Indexed as

Amino Acid MotifsAmino Acid SequenceAntibodies, MonoclonalBlotting, WesternCloning, MolecularCyclic AMP Response Element-Binding ProteinCytoplasmDEAD Box Protein 20DEAD-box RNA HelicasesHeLa CellsHumansMolecular Sequence DataMolecular WeightMuscular Atrophy, SpinalNerve Tissue ProteinsOrganellesAntibodies, MonoclonalCyclic AMP Response Element-Binding ProteinDDX20 protein, humanDEAD Box Protein 20DEAD-box RNA HelicasesGEMIN2 protein, humanNerve Tissue ProteinsRecombinant Fusion ProteinsRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA HelicasesSMN Complex Proteins

Identifiers

PMID10601333
PMCPMC2168095
OpenAlexW2059997993

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.