Evidence map›Paper›PMID 20936941›Full record

ReviewAnnual review of physiology2011

Tight junction pore and leak pathways: a dynamic duo.

Le Shen, Christopher R Weber, David R Raleigh, Dan Yu, Jerrold R Turner

Abstract readReview
In one paragraph

Review in Annual review of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 468 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
468citing papers in PubMed, 1 pooled it
–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

468 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Emerging microbes & infections · 2026
    Article
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  8. Tight junction structure, assembly and (dys)function.Nature reviews. Molecular cell biology · 2026
    Review
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408 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

5 authors.

Le Shen *Department of Pathology, The University of Chicago, Chicago, Illinois 60637.
Christopher R Weber *Department of Pathology, The University of Chicago, Chicago, Illinois 60637.
David R RaleighDepartment of Pathology, The University of Chicago, Chicago, Illinois 60637.
Dan YuDepartment of Pathology, The University of Chicago, Chicago, Illinois 60637.
Jerrold R TurnerDepartment of Pathology, The University of Chicago, Chicago, Illinois 60637.

Funding

VIRAL ONCOLOGY CORE FACILITYP30CA014599 · NCI · UNIVERSITY OF CHICAGO · PI MARK W. LINGEN · 1985 to 2026
$122.1M
MEDICAL SCIENTIST TRAININGT32GM007281 · NIGMS · UNIVERSITY OF CHICAGO · PI CLARK, MARCUS RAMSAY · 1985 to 2022
$32.1M
ULTRASTRUCTURE AND CYTOMORPHOLOGY COREP30DK042086 · NIDDK · UNIVERSITY OF CHICAGO · PI LIU, CAMBRIAN YANGSHAO · 1990 to 2025
$29.8M
TRANSLATIONAL RESEARCH UNIVERSITY OF CHICAGO: CLINICAL TRIALSUL1RR024999 · NCRR · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2007 to 2011
$25.3M
ZO-1-MEDIATED PROTEIN INTERACTIONS: REGULATORS AND INTEGRATORS OF DIVERSE EPITHELIAL FUNCTIONS IN HEALTH AND DISEASER01DK061931 · NIDDK · UNIVERSITY OF CHICAGO · PI JERROLD R. TURNER · 2001 to 2026
$15.0M
Therapeutic targeting of protein interactions to reverse MLCK1-mediated intestinal barrier loss and ameliorate disease.R01DK068271 · NIDDK · UNIVERSITY OF CHICAGO · PI JERROLD R. TURNER · 2005 to 2026
$11.3M
Transcriptional Regulation of NHE-3 Isoform in Human IntestineP01DK067887 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI HECHT, GAIL A · 2006 to 2011
$4.9M
Mechanisms and pathways of trans-tight junction conductanceK08DK088953 · NIDDK · UNIVERSITY OF CHICAGO · PI WEBER, CHRISTOPHER · 2010 to 2014
$733k
Mechanisms of epithelial barrier dysfunction mediated by inflammatory cytokinesF32DK082134 · NIDDK · UNIVERSITY OF CHICAGO · PI WEBER, CHRISTOPHER · 2008 to 2009
$108k
NCI NIH HHS P30 CA014599NCI NIH HHS P30CA14599NCRR NIH HHS UL1 RR024999NCRR NIH HHS UL1RR024999NIDDK NIH HHS F32 DK082134NIDDK NIH HHS F32DK082134NIDDK NIH HHS K08 DK088953NIDDK NIH HHS K08DK088953NIDDK NIH HHS P01 DK067887NIDDK NIH HHS P01DK067887NIDDK NIH HHS P30 DK042086NIDDK NIH HHS P30DK042086NIDDK NIH HHS R01 DK061931NIDDK NIH HHS R01 DK068271NIDDK NIH HHS R01DK61931NIDDK NIH HHS R01DK68271NIGMS NIH HHS 5T32GM007281NIGMS NIH HHS T32 GM007281
6 · The paper itself

Abstract

Tissue barriers that restrict passage of liquids, ions, and larger solutes are essential for the development of multicellular organisms. In simple organisms this allows distinct cell types to interface with the external environment. In more complex species, the diversity of cell types capable of forming barriers increases dramatically. Although the plasma membranes of these barrier-forming cells prevent flux of most hydrophilic solutes, the paracellular, or shunt, pathway between cells must also be sealed. This function is accomplished in vertebrates by the zonula occludens, or tight junction. The tight junction barrier is not absolute but is selectively permeable and is able to discriminate between solutes on the basis of size and charge. Many tight junction components have been identified over the past 20 years, and recent progress has provided new insights into the proteins and interactions that regulate structure and function. This review presents these data in a historical context and proposes an integrated model in which dynamic regulation of tight junction protein interactions determines barrier function.

Indexed as

AnimalsEpithelial CellsHumansMembrane ProteinsMiceProtein Interaction Domains and MotifsTight JunctionsMembrane Proteins

Identifiers

PMID20936941
PMCPMC4655434

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.