Evidence map›Paper›PMID 16682526›Full record

ArticleThe Journal of cell biology2006

The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function.

Alexis S Madrid, Joel Mancuso, W Zacheus Cande, Karsten Weis

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

62 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Article
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  8. Article
  9. Article
  10. Article
  11. Article
  12. Nucleoporins in cardiovascular disease.Journal of molecular and cellular cardiology · 2020
    Review
  13. Article
  14. Mapping the native organization of the yeast nuclear pore complex using nuclear radial intensity measurements.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

2 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.

Alexis S MadridDivision of Cell and Developmental Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
Joel Mancuso
W Zacheus Cande
Karsten Weis
University of California, Berkeley · 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
Meiotic telemere clustering in fission yeastR01GM067992 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CANDE, WILLIAM ZACHEUS · 2003 to 2006
$1.2M
NIGMS NIH HHS GM067992NIGMS NIH HHS GM58065NIGMS NIH HHS R01 GM058065NIGMS NIH HHS R01 GM067992
6 · The paper itself

Abstract

The nuclear pore complex (NPC) is a large channel that spans the two lipid bilayers of the nuclear envelope and mediates transport events between the cytoplasm and the nucleus. Only a few NPC components are transmembrane proteins, and the role of these proteins in NPC function and assembly remains poorly understood. We investigate the function of the three integral membrane nucleoporins, which are Ndc1p, Pom152p, and Pom34p, in NPC assembly and transport in Saccharomyces cerevisiae. We find that Ndc1p is important for the correct localization of nuclear transport cargoes and of components of the NPC. However, the role of Ndc1p in NPC assembly is partially redundant with Pom152p, as cells lacking both of these proteins show enhanced NPC disruption. Electron microscopy studies reveal that the absence of Ndc1p and Pom152p results in aberrant pores that have enlarged diameters and lack proteinaceous material, leading to an increased diffusion between the cytoplasm and the nucleus.

Indexed as

Active Transport, Cell NucleusCell DivisionCell NucleusDiffusionDNA-Binding ProteinsMembrane GlycoproteinsMicroscopy, Electron, TransmissionMutationNuclear Localization SignalsNuclear PoreNuclear Pore Complex ProteinsNuclear ProteinsRNA-Binding ProteinsRNA TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsASM4 protein, S cerevisiaeDNA-Binding ProteinsMembrane GlycoproteinsNDC1 protein, S cerevisiaeNPL3 protein, S cerevisiaeNuclear Localization SignalsNuclear Pore Complex ProteinsNuclear ProteinsNUP159 protein, S cerevisiaeNup60 protein, S cerevisiaePHO4 protein, S cerevisiaePOM152 protein, S cerevisiaeRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID16682526
PMCPMC2063837
OpenAlexW1974131162

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.