Evidence map›Paper›PMID 20335358›Full record

ArticleDevelopment (Cambridge, England)2010

The C. elegans homolog of nucleoporin Nup98 is required for the integrity and function of germline P granules.

Ekaterina Voronina, Geraldine Seydoux

Open access · greenAbstract read
In one paragraph

Article in Development (Cambridge, England), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

52 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Hybrid incompatibility emerges at the one-cell stage in interspeciesbioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. DLC-1 facilitates germ granule assembly inMolecular biology of the cell · 2022
    Article
  14. Review
  15. Disruption ofmicroPublication biology · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Multifunctionality of F-rich nucleoporins.Biochemical Society transactions · 2020
    Review
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

2 authors at 2 institutions in 1 country.

Ekaterina VoroninaDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Geraldine Seydoux
Howard Hughes Medical Institute · USJohns Hopkins University · US

Funding

REGULATION OF GERM CELL FATE DURING EMBRYOGENESISR01HD037047 · NICHD · JOHNS HOPKINS UNIVERSITY · PI GERALDINE Catherine Joelle SEYDOUX · 1999 to 2026
$4.3M
Regulation of Germ Cell Fate During EmbryogenesisR37HD037047 · NICHD · JOHNS HOPKINS UNIVERSITY · PI SEYDOUX, GERALDINE CATHERINE JOELLE · 2016 to 2025
$3.8M
Components of C. elegans P-granules and regulation of their functionF32GM080923 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VORONINA, EKATERINA · 2007 to 2009
$165k
Howard Hughes Medical InstituteNICHD NIH HHS HD37047NICHD NIH HHS R01 HD037047NICHD NIH HHS R37 HD037047NIGMS NIH HHS 5F32GM080923NIGMS NIH HHS F32 GM080923
6 · The paper itself

Abstract

C. elegans P granules are conserved cytoplasmic ribonucleoprotein complexes that are unique to the germline and essential for fertility. During most of germline development, P granules are perinuclear and associate with clusters of nuclear pores. In an RNAi screen against nucleoporins, we have identified a specific nucleoporin essential for P granule integrity and function. The C. elegans homolog of vertebrate Nup98 (CeNup98) is enriched in P granules and associates with the translationally repressed, P granule-enriched mRNA nos-2 (nanos homolog). Loss of CeNup98 causes P granules to disperse in the cytoplasm and to release nos-2 mRNA. Embryos depleted for CeNup98 express a nos-2 3'UTR reporter prematurely. In the mouse, Nup98 immunoprecipitates with the germ granule component MVH. Our findings suggest that, in germ cells, the function of Nup98 extends beyond transport at the nuclear pore to include mRNA regulation in the cytoplasm.

Indexed as

AnimalsAnimals, Genetically ModifiedBlotting, WesternCaenorhabditis elegansCaenorhabditis elegans ProteinsDEAD-box RNA HelicasesEmbryo, NonmammalianGerm CellsImmunoprecipitationIn Situ HybridizationMiceMice, Inbred C57BLNuclear Pore Complex ProteinsProtein BindingReverse Transcriptase Polymerase Chain ReactionRNA InterferenceCaenorhabditis elegans ProteinsDdx4 protein, mouseDEAD-box RNA Helicasesnuclear pore complex protein 98Nuclear Pore Complex Proteins

Identifiers

PMID20335358
PMCPMC2853846
OpenAlexW2154740350

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.