Evidence map›Paper›PMID 22083955›Full record

ReviewMolecular and cellular biology2012

Occludin: one protein, many forms.

Philip M Cummins

Abstract readReview
In one paragraph

Review in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 225 papers.

0numbers the graph read from it
0cells of the map it votes in
225citing papers in PubMed
–field-weighted citation impact
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

225 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Occludin acts as a dynein adaptor regulating permeability and collateral angiogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Memory under siege: the cognitive costs of smoking and vaping.Brain, behavior, & immunity - health · 2025
    Review
  17. Article
  18. Epithelial Barrier Function and Altered Cell Signaling Pathways in the Esophageal Epithelium of Achalasia Patients.The Turkish journal of gastroenterology : the official journal of Turkish Society of Gastroenterology · 2025
    Article
  19. Article
  20. Article

165 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

1 author.

Philip M CumminsSchool of Biotechnology and Centre for Preventive Medicine, Dublin City University, Dublin, Ireland. phil.cummins@dcu.ie

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intercellular tight junctions (TJs) exhibit a complex molecular architecture involving the regulated cointeraction of cytoplasmic adaptor proteins (e.g., zonula occludens) and integral membrane linker proteins (e.g., occludin and claudins). They provide structural integrity to epithelial and endothelial tissues and create highly polarized barriers essential to homeostatic maintenance within vertebrate physiological systems, while their dysregulation is an established pathophysiological hallmark of many diseases (e.g., cancer, stroke, and inflammatory lung disease). The junctional complex itself is a highly dynamic signaling entity wherein participant proteins constantly undergo a blend of regulatory modifications in response to diverse physiological and pathological cues, ultimately diversifying the overall adhesive properties of the TJ. Occludin, a 65-kDa tetraspan integral membrane protein, contributes to TJ stabilization and optimal barrier function. This paper reviews our current knowledge of how tissue occludin is specifically modified at the posttranscriptional and posttranslational levels in diverse circumstances, with associated consequences for TJ dynamics and epithelial/endothelial homeostasis. Mechanistic concepts such as splice variance and alternate promoter usage, proteolysis, phosphorylation, dimerization, and ubiquitination are comprehensively examined, and possible avenues for future investigation highlighted.

Indexed as

AnimalsHumansMembrane ProteinsOccludinProtein IsoformsProtein Processing, Post-TranslationalTight JunctionsMembrane ProteinsOccludinOCLN protein, humanProtein Isoforms

Identifiers

PMID22083955
PMCPMC3255790

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.