Evidence map›Paper›PMID 28221134›Full record

ArticleeLife2017

Human Nup98 regulates the localization and activity of DExH/D-box helicase DHX9.

Juliana S Capitanio, Ben Montpetit, Richard W Wozniak

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023
    Review
  10. Review
  11. Article
  12. Review
  13. GermlineInternational journal of molecular sciences · 2023
    Article
  14. Promotion of Lung Cancer Metastasis by SIRT2-Mediated Extracellular Protein Deacetylation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  15. Liquid-liquid phase separation in tumor biology.Signal transduction and targeted therapy · 2022
    Review
  16. Nuclear Pore Dysfunction in Neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. MARCH6 promotes Papillary Thyroid Cancer development by destabilizing DHX9.International journal of biological sciences · 2021
    Article
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

3 authors at 1 institution in 2 countries.

Juliana S CapitanioDepartment of Cell Biology, University of Alberta, Edmonton, Canada.ORCID 0000-0003-4283-8007
Ben MontpetitDepartment of Cell Biology, University of Alberta, Edmonton, Canada.ORCID 0000-0002-8317-983X
Richard W WozniakDepartment of Cell Biology, University of Alberta, Edmonton, Canada.ORCID 0000-0003-2328-0247
University of Alberta · CA

Funding

CIHR
6 · The paper itself

Abstract

Beyond their role at nuclear pore complexes, some nucleoporins function in the nucleoplasm. One such nucleoporin, Nup98, binds chromatin and regulates gene expression. To gain insight into how Nup98 contributes to this process, we focused on identifying novel binding partners and understanding the significance of these interactions. Here we report on the identification of the DExH/D-box helicase DHX9 as an intranuclear Nup98 binding partner. Various results, including in vitro assays, show that the FG/GLFG region of Nup98 binds to N- and C-terminal regions of DHX9 in an RNA facilitated manner. Importantly, binding of Nup98 stimulates the ATPase activity of DHX9, and a transcriptional reporter assay suggests Nup98 supports DHX9-stimulated transcription. Consistent with these observations, our analysis revealed that Nup98 and DHX9 bind interdependently to similar gene loci and their transcripts. Based on our results, we propose that Nup98 functions as a co-factor that regulates DHX9 and, potentially, other RNA helicases.

Indexed as

Gene Expression RegulationDEAD-box RNA HelicasesHumansNeoplasm ProteinsNuclear Pore Complex ProteinsProtein BindingProtein Interaction MappingProtein TransportRNADEAD-box RNA HelicasesDHX9 protein, humanNeoplasm ProteinsNuclear Pore Complex ProteinsNup98 protein, humanRNAcell biologyDExH/D-box helicaseDHX9gene expression and mRNA metabolismhumannuclear pore complexNup98RNA helicase A

Identifiers

PMID28221134
PMCPMC5338925
OpenAlexW2590354399

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.