Evidence map›Paper›PMID 12192051›Full record

ArticleMolecular and cellular biology2002

The SMN complex is associated with snRNPs throughout their cytoplasmic assembly pathway.

Séverine Massenet, Livio Pellizzoni, Sergey Paushkin, Iain W Mattaj, Gideon Dreyfuss

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.5field-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

65 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
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  5. AProceedings of the National Academy of Sciences of the United States of America · 2025
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  6. Article
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  9. Sm complex assembly and 5' cap trimethylation promote selective processing of snRNAs by the 3' exonuclease TOE1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. DDX20: A Multifunctional Complex Protein.Molecules (Basel, Switzerland) · 2023
    Review
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  15. Article
  16. Review
  17. Article
  18. Article
  19. Osteoclast stimulation factor 1 (Ostf1) KNOCKOUT increases trabecular bone mass in mice.Mammalian genome : official journal of the International Mammalian Genome Society · 2017
    Article
  20. Review

5 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

5 authors at 3 institutions in 2 countries.

Séverine MassenetHoward Hughes Medical Institute and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia 19104-6148, USA.
Livio Pellizzoni
Sergey Paushkin
Iain W Mattaj
Gideon Dreyfuss
Howard Hughes Medical Institute · USEuropean Molecular Biology Laboratory · DEUniversity of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The common neurodegenerative disease spinal muscular atrophy is caused by reduced levels of the survival of motor neurons (SMN) protein. SMN associates with several proteins (Gemin2 to Gemin6) to form a large complex which is found both in the cytoplasm and in the nucleus. The SMN complex functions in the assembly and metabolism of several RNPs, including spliceosomal snRNPs. The snRNP core assembly takes place in the cytoplasm from Sm proteins and newly exported snRNAs. Here, we identify three distinct cytoplasmic SMN complexes, each representing a defined intermediate in the snRNP biogenesis pathway. We show that the SMN complex associates with newly exported snRNAs containing the nonphosphorylated form of the snRNA export factor PHAX. The second SMN complex identified contains assembled Sm cores and m(3)G-capped snRNAs. Finally, the SMN complex is associated with a preimport complex containing m(3)G-capped snRNP cores bound to the snRNP nuclear import mediator snurportin1. Thus, the SMN complex is associated with snRNPs during the entire process of their biogenesis in the cytoplasm and may have multiple functions throughout this process.

Indexed as

Nucleocytoplasmic Transport ProteinsCell LineCell NucleusCyclic AMP Response Element-Binding ProteinCytoplasmDNAHeLa CellsHumansMacromolecular SubstancesMicroscopy, FluorescenceModels, BiologicalNerve Tissue ProteinsPhosphoproteinsPlasmidsPrecipitin TestsProtein BindingCyclic AMP Response Element-Binding ProteinDNAMacromolecular SubstancesNerve Tissue ProteinsNucleocytoplasmic Transport ProteinsPHAX protein, humanPhosphoproteinsReceptors, Cytoplasmic and NuclearRibonucleoproteins, Small NuclearRNA-Binding ProteinsRNA Cap-Binding ProteinsSMN Complex ProteinsSNUPN protein, human

Identifiers

PMID12192051
PMCPMC135628
OpenAlexW2107128774

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.