Evidence map›Paper›PMID 10369684›Full record

ArticleThe EMBO journal1999

Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin.

J Salgado-Garrido, E Bragado-Nilsson, S Kandels-Lewis, B Séraphin

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1999. 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
8.8field-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, 259 citations in OpenAlex.

  1. Microbiology (Reading, England) · 2026
    Review
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  8. Analysis of Lsm Protein-Mediated Regulation in the HaloarchaeonInternational journal of molecular sciences · 2024
    Article
  9. Article
  10. Article
  11. Review
  12. Article
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  14. Article
  15. Article
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  17. mRNA decapping: finding the right structures.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  18. The Roles of TwoThe plant pathology journal · 2018
    Article
  19. Article
  20. Review

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

4 authors at 1 institution in 1 country.

J Salgado-GarridoEMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
E Bragado-Nilsson
S Kandels-Lewis
B Séraphin
European Molecular Biology Organization · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A group of seven Sm proteins forms a complex that binds to several RNAs in metazoans. All Sm proteins contain a sequence signature, the Sm domain, also found in two yeast Sm-like proteins associated with the U6 snRNA. We have performed database searches revealing the presence of 16 proteins carrying an Sm domain in the yeast genome. Analysis of this protein family confirmed that seven of its members, encoded by essential genes, are homologues of metazoan Sm proteins. Immunoprecipitation revealed that an evolutionarily related subgroup of seven Sm-like proteins is directly associated with the nuclear U6 and pre-RNase P RNAs. The corresponding genes are essential or required for normal vegetative growth. These proteins appear functionally important to stabilize U6 snRNA. The two last yeast Sm-like proteins were not found associated with RNA, and neither was essential for vegetative growth. To investigate whether U6-associated Sm-like protein function is widespread, we cloned several cDNAs encoding homologous human proteins. Two representative human proteins were shown to associate with U6 snRNA-containing complexes. We also identified archaeal proteins related to Sm and Sm-like proteins. Our results demonstrate that Sm and Sm-like proteins assemble in at least two functionally conserved complexes of deep evolutionary origin.

Indexed as

Evolution, MolecularRibonucleoproteins, Small NuclearAnimalsArchaeal ProteinsAutoantigensCell LineCloning, MolecularConserved SequenceDatabases, FactualEndoribonucleasesFungal ProteinsGenes, EssentialGenome, FungalHumansMiceMutationArchaeal ProteinsAutoantigensEndoribonucleasesFungal ProteinsRibonuclease PRibonucleoproteins, Small NuclearRNA, CatalyticRNA, Small NuclearRPP14 protein, humansnRNP Core Proteins

Identifiers

PMID10369684
PMCPMC1171424
OpenAlexW2073688200

What OpenQuestion holds

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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.