Evidence map›Paper›PMID 10679015›Full record

ArticleMolecular biology of the cell2000

Conserved composition of mammalian box H/ACA and box C/D small nucleolar ribonucleoprotein particles and their interaction with the common factor Nopp140.

Y Yang, C Isaac, C Wang, F Dragon, V Pogacic, U T Meier

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

61 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Coilin and Cajal bodies.Nucleus (Austin, Tex.) · 2023
    Review
  8. Roles of NOLC1 in cancers and viral infection.Journal of cancer research and clinical oncology · 2023
    Review
  9. Article
  10. Review
  11. Role of main RNA modifications in cancer: NSignal transduction and targeted therapy · 2022
    Review
  12. Article
  13. Nucleolar stress inBiology open · 2020
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Review

1 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 2 institutions in 2 countries.

Y YangDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
C Isaac
C Wang
F Dragon
V Pogacic
U T Meier
Albert Einstein College of Medicine · USFriedrich Miescher Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small nucleolar ribonucleoprotein particles (snoRNPs) mainly catalyze the modification of rRNA. The two major classes of snoRNPs, box H/ACA and box C/D, function in the pseudouridylation and 2'-O-methylation, respectively, of specific nucleotides. The emerging view based on studies in yeast is that each class of snoRNPs is composed of a unique set of proteins. Here we present a characterization of mammalian snoRNPs. We show that the previously characterized NAP57 is specific for box H/ACA snoRNPs, whereas the newly identified NAP65, the rat homologue of yeast Nop5/58p, is a component of the box C/D class. Using coimmunoprecipitation experiments, we show that the nucleolar and coiled-body protein Nopp140 interacts with both classes of snoRNPs. This interaction is corroborated in vivo by the exclusive depletion of snoRNP proteins from nucleoli in cells transfected with a dominant negative Nopp140 construct. Interestingly, RNA polymerase I transcription is arrested in nucleoli depleted of snoRNPs, raising the possibility of a feedback mechanism between rRNA modification and transcription. Moreover, the Nopp140-snoRNP interaction appears to be conserved in yeast, because depletion of Srp40p, the yeast Nopp140 homologue, in a conditional lethal strain induces the loss of box H/ACA small nucleolar RNAs. We propose that Nopp140 functions as a chaperone of snoRNPs in yeast and vertebrate cells.

Indexed as

Conserved SequenceHydro-LyasesRibonucleoproteins, Small NuclearSaccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsCell NucleolusCOS CellsEpistasis, GeneticGenetic Complementation TestMicrotubule-Associated ProteinsMolecular ChaperonesMolecular Sequence DataMolecular WeightMutationNuclear ProteinsCBF5 protein, S cerevisiaeHydro-LyasesMicrotubule-Associated ProteinsMolecular ChaperonesNAP57NOLC1 protein, humanNolc1 protein, ratNop58 protein, ratNOP58 protein, S cerevisiaeNuclear ProteinsPhosphoproteinsRibonucleoproteinsRibonucleoproteins, Small NuclearRibonucleoproteins, Small NucleolarRNA-Binding ProteinsRNA Polymerase ISaccharomyces cerevisiae ProteinsSerine-Arginine Splicing Factors

Identifiers

PMID10679015
PMCPMC14794
OpenAlexW2124939400

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.