Evidence map›Paper›PMID 1370490›Full record

ArticleThe Journal of cell biology1992

Nuclear protein import is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glycoprotein.

U F Greber, L Gerace

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Hormonal regulation of nuclear permeability.The Journal of biological chemistry · 2007
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Calcium, ATP and nuclear pore channel gating.Pflugers Archiv : European journal of physiology · 2000
    Article
  14. Article
  15. Article
  16. The nuclear pore complex.Plant molecular biology · 1998
    Review
  17. Involvement of p62 nucleoporin in angiotensin II-induced nuclear translocation of STAT3 in brain neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
  18. Calmodulin activates nuclear protein import: a link between signal transduction and nuclear transport.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

U F GreberDepartment of Cell Biology, Scripps Research Institute, La Jolla, California 92037.
L Gerace
Scripps Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gp210 is a major transmembrane glycoprotein associated with the nuclear pore complex that is suggested to be important for organizing pore complex architecture and assembly. A mouse monoclonal IgG directed against an epitope in the lumenal domain of rat gp210 was expressed in cultured rat cells by microinjection of mRNA prepared from a hybridoma cell line. The expressed IgG, which becomes assembled into a functional antibody in the lumen of the endoplasmic reticulum, bound to the nuclear envelope in vivo. Expression of anti-gp210 antibody in interphase cells specifically reduced approximately fourfold the mediated nuclear import of a microinjected nuclear protein (nucleoplasmin) coupled to gold particles. The antibody also significantly decreased nuclear influx of a 10-kD dextran by passive diffusion. This transport inhibition did not result from removal of pore complexes from nuclear membranes or from gross alterations in pore complex structure, as shown by EM and immunocytochemistry. A physiological consequence of this transport inhibition was inhibition of cell progression from G2 into M phase. Hence, binding of this antibody to the lumenal side of gp210 must have a transmembrane effect on the structure and functions of the pore complex. These data argue that gp210 is directly or indirectly connected to pore complex constituents involved in mediated import and passive diffusion.

Indexed as

Antibodies, MonoclonalAnimalsCell LineCell NucleusDNA-Directed DNA PolymeraseEpitopesG2 PhaseImmunoglobulin GMembrane GlycoproteinsMicroscopy, ElectronMicroscopy, FluorescenceMitosisMolecular WeightNuclear EnvelopeNuclear ProteinsRNA, MessengerAntibodies, MonoclonalDNA-Directed DNA PolymeraseEpitopesImmunoglobulin GMembrane GlycoproteinsNuclear ProteinsRNA, Messenger

Identifiers

PMID1370490
PMCPMC2289267
OpenAlexW2079995076

What OpenQuestion holds

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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.