Evidence map›Paper›PMID 19414608›Full record

ArticleThe Journal of cell biology2009

The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly.

Tadashi Makio, Leslie H Stanton, Cheng-Chao Lin, David S Goldfarb, Karsten Weis, Richard W Wozniak

Abstract read
In one paragraph

Article in The Journal of cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

57 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Review
  3. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  4. Identification of divergentbioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. The LEM-ESCRT toolkit: Repair and maintenance of the nucleus.Frontiers in cell and developmental biology · 2022
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Tadashi MakioDepartment of Cell Biology, University of Alberta, Edmonton, Alberta, Canada.
Leslie H Stanton
Cheng-Chao Lin
David S Goldfarb
Karsten Weis
Richard W Wozniak
University of Alberta · CAUniversity of California, Berkeley · USUniversity of Rochester · US

Funding

Structure and function of the nuclear pore complexR01GM058065 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI HEALD, REBECCA W · 1998 to 2015
$4.6M
Howard Hughes Medical InstituteNIGMS NIH HHS GM058065NIGMS NIH HHS R01 GM058065
6 · The paper itself

Abstract

We have established that two homologous nucleoporins, Nup170p and Nup157p, play an essential role in the formation of nuclear pore complexes (NPCs) in Saccharomyces cerevisiae. By regulating their synthesis, we showed that the loss of these nucleoporins triggers a decrease in NPCs caused by a halt in new NPC assembly. Preexisting NPCs are ultimately lost by dilution as cells grow, causing the inhibition of nuclear transport and the loss of viability. Significantly, the loss of Nup170p/Nup157p had distinct effects on the assembly of different architectural components of the NPC. Nucleoporins (nups) positioned on the cytoplasmic face of the NPC rapidly accumulated in cytoplasmic foci. These nup complexes could be recruited into new NPCs after reinitiation of Nup170p synthesis, and may represent a physiological intermediate. Loss of Nup170p/Nup157p also caused core and nucleoplasmically positioned nups to accumulate in NPC-like structures adjacent to the inner nuclear membrane, which suggests that these nucleoporins are required for formation of the pore membrane and the incorporation of cytoplasmic nups into forming NPCs.

Indexed as

Active Transport, Cell NucleusGene DeletionGenome, FungalMethionineNuclear EnvelopeNuclear PoreNuclear Pore Complex ProteinsPromoter Regions, GeneticSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMethionineNuclear Pore Complex ProteinsNUP157 protein, S cerevisiaeNUP170 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID19414608
PMCPMC2700392
OpenAlexW2061592942

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.