Evidence map›Paper›PMID 25171873›Full record

ReviewSeminars in cell & developmental biology2014

Architecture of tight junctions and principles of molecular composition.

Christina M Van Itallie, James M Anderson

Open access · greenAbstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 284 papers.

0numbers the graph read from it
0cells of the map it votes in
284citing papers in PubMed
27.4field-weighted citation impact, top 1% 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

284 citing papers in PubMed, 510 citations in OpenAlex.

  1. Article
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  7. Barrier and Immune Modulation byInternational journal of molecular sciences · 2026
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  17. [Research progress in diagnosis and treatment of non-tumorous salivary gland diseases].Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · 2026
    Review
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  19. Article
  20. Review

224 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

2 authors at 1 institution in 1 country.

Christina M Van ItallieThe Laboratory of Tight Junction Structure and Function, National Heart, Lung, and Blood Institute, National Institutes of Health, Building 50, Room 4525, 50 South Drive, Bethesda, MD 20892, USA. Electronic address: christina.vanitallie@nih.gov.
James M AndersonThe Laboratory of Tight Junction Structure and Function, National Heart, Lung, and Blood Institute, National Institutes of Health, Building 50, Room 4525, 50 South Drive, Bethesda, MD 20892, USA. Electronic address: james.anderson2@nih.gov.
National Institutes of Health · US

Funding

Expanding the tight junction inventory through proteomicsZIAHL006176 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ANDERSON, JAMES · 2014 to 2014
$601k
Novel approaches to study dynamic coupling of the tight junction barrier to the actin cytoskeletonZIAHL006207 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ANDERSON, JAMES · 2016 to 2016
$461k
Intramural NIH HHS ZIA HL006176
6 · The paper itself

Abstract

The tight junction creates an intercellular barrier limiting paracellular movement of solutes and material across epithelia. Currently many proteins have been identified as components of the tight junction and understanding their architectural organization and interactions is critical to understanding the biology of the barrier. In general the architecture can be conceptualized into compartments with the transmembrane barrier proteins (claudins, occludin, JAM-A, etc.), linked to peripheral scaffolding proteins (such as ZO-1, afadin, MAGI1, etc.) which are in turned linked to actin and microtubules through numerous linkers (cingulin, myosins, protein 4.1, etc.). Within this complex network are associated many signaling proteins that affect the barrier and broader cell functions. The PDZ domain is a commonly used motif to specifically link individual junction protein pairs. Here we review some of the key proteins defining the tight junction and general themes of their organization with the perspective that much will be learned about function by characterizing the detailed architecture and subcompartments within the junction.

Indexed as

Biological TransportCytoskeletal ProteinsHumansJunctional Adhesion MoleculesMembrane ProteinsProtein Structure, TertiarySignal TransductionTight JunctionsCytoskeletal ProteinsJunctional Adhesion MoleculesMembrane ProteinsActinClaudinEpitheliumOccludinTight junctionZO-1

Identifiers

PMID25171873
PMCPMC4254347
OpenAlexW2056700437

What OpenQuestion holds

Textmetadata
LicenceTDM
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.