Evidence map›Paper›PMID 8855257›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cell-cell contacts.

C J Gottardi, M Arpin, A S Fanning, D Louvard

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

122 citing papers in PubMed, 358 citations in OpenAlex.

  1. Review
  2. Article
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  5. Review
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  7. Review
  8. Article
  9. Silica-coated LiYFRSC advances · 2024
    Article
  10. Emerging role of vitamin DAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Zonula Occludens Proteins Signaling in Inflammation and Tumorigenesis.International journal of biological sciences · 2023
    Review
  16. Working a second job: Cell adhesion proteins that moonlight in the nucleus.Frontiers in cell and developmental biology · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Review

62 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 2 institutions in 1 country.

C J GottardiLaboratory of Cell Signaling and Morphogenesis, UMR 144 Centre National de la Recherche Scientifique, Institut Curie, Paris, France.
M Arpin
A S Fanning
D Louvard
Biologie cellulaire et Cancer · FRUniversité Paris Sciences et Lettres · FR

Funding

FUNCTIONAL ANAYLSIS OF THE TIGHT JUNCTION PROTEIN ZO-1F32DK009261 · NIDDK · YALE UNIVERSITY · PI FANNING, ALAN S · 1995 to 1995
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ZO 1 AND SIGNAL TRANSDUCTION IN TIGHT JUNCTIONSP01CA066263 · NCI · UNIVERSITY OF CALIFORNIA IRVINE · PI CHISHTI, ATHAR H. · 1995 to 1999
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NCI NIH HHS CA66263NIDDK NIH HHS DK09261
6 · The paper itself

Abstract

The junction-associated protein zonula occludens-1 (ZO-1) is a member of a family of membrane-associated guanylate kinase homologues thought to be important in signal transduction at sites of cell-cell contact. We present evidence that under certain conditions of cell growth, ZO-1 can be detected in the nucleus. Two different antibodies against distinct portions of the ZO-1 polypeptide reveal nuclear staining in subconfluent, but not confluent, cell cultures. An exogenously expressed, epitope-tagged ZO-1 can also be detected in the nuclei of transfected cells. Nuclear accumulation can be stimulated at sites of wounding in cultured epithelial cells, and immunoperoxidase detection of ZO-1 in tissue sections of intestinal epithelial cells reveals nuclear labeling only along the outer tip of the villus. These results suggest that the nuclear localization of ZO-1 is inversely related to the extent and/or maturity of cell contact. Since cell-cell contacts are specialized sites for signaling pathways implicated in growth and differentiation, we suggest that the nuclear accumulation of ZO-1 may be relevant for its suggested role in membrane-associated guanylate kinase homologue signal transduction.

Indexed as

Cell AdhesionAnimalsCell CompartmentationCell LineCell NucleusChlorocebus aethiopsDogsFluorescent Antibody Technique, IndirectGuanylate KinasesImmunoenzyme TechniquesMembrane ProteinsNucleoside-Phosphate KinasePhosphoproteinsSignal TransductionTight JunctionsZonula Occludens-1 ProteinGuanylate KinasesMembrane ProteinsNucleoside-Phosphate KinasePhosphoproteinsZonula Occludens-1 Protein

Identifiers

PMID8855257
PMCPMC38232
OpenAlexW2037481900

What OpenQuestion holds

Textmetadata
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.