Evidence map›Paper›PMID 8682854›Full record

ArticleThe Journal of cell biology1996

Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p.

U Zabel, V Doye, H Tekotte, R Wepf, P Grandi, E C Hurt

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. 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
4.1field-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

62 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
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  4. Decreased mechanotransduction prevents nuclear collapse in aProceedings of the National Academy of Sciences of the United States of America · 2020
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  6. Identification of the NovelG3 (Bethesda, Md.) · 2018
    Article
  7. Review
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  13. Review
  14. Article
  15. Article
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  17. Article
  18. Article
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  20. Article

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

6 authors at 1 institution in 1 country.

U ZabelUniversity of Würzburg, Institut für Pharmakologie und Toxikologie, Germany.
V Doye
H Tekotte
R Wepf
P Grandi
E C Hurt
University of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The amino-terminal domain of Nic96p physically interacts with the Nsp1p complex which is involved in nucleocytoplasmic transport. Here we show that thermosensitive mutations mapping in the central domain of Nic96p inhibit nuclear pore formation at the nonpermissive temperature. Furthermore, the carboxyterminal domain of Nic96p functionally interacts with a novel nucleoporin Nup188p in an allele-specific fashion, and when ProtA-Nup188p was affinity purified, a fraction of Nic96p was found in physical interaction. Although NUP188 is not essential for viability, a null mutant exhibits striking abnormalities in nuclear envelope and nuclear pore morphology. We propose that Nic96p is a multivalent protein of the nuclear pore complex linked to several nuclear pore proteins via its different domains.

Indexed as

Membrane ProteinsNuclear Pore Complex ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceBase SequenceCloning, MolecularFungal ProteinsGenes, FungalGenes, LethalGenetic Complementation TestMolecular Sequence DataMolecular WeightMutationNuclear EnvelopeNuclear ProteinsProtein BindingFungal ProteinsMembrane ProteinsNIC96 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsNUP188 protein, S cerevisiaeRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID8682854
PMCPMC2120893
OpenAlexW2065877983

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.