Evidence map›Paper›PMID 31426497›Full record

ReviewInternational journal of molecular sciences2019

Potential for Tight Junction Protein-Directed Drug Development Using Claudin Binders and Angubindin-1.

Yosuke Hashimoto, Keisuke Tachibana, Susanne M Krug, Jun Kunisawa, Michael Fromm, Masuo Kondoh

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
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  20. An Overview of Physical, Microbiological and Immune Barriers of Oral Mucosa.International journal of molecular sciences · 2021
    Review
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 3 institutions in 2 countries.

Yosuke HashimotoGraduate School of Pharmaceutical Sciences, Osaka University, Osaka 565-0871, Japan.
Keisuke TachibanaGraduate School of Pharmaceutical Sciences, Osaka University, Osaka 565-0871, Japan.
Susanne M KrugInstitute of Clinical Physiology, Charité-Universitätsmedizin Berlin, 12203 Berlin, Germany.ORCID 0000-0002-1293-2484
Jun KunisawaGraduate School of Pharmaceutical Sciences, Osaka University, Osaka 565-0871, Japan.
Michael FrommInstitute of Clinical Physiology, Charité-Universitätsmedizin Berlin, 12203 Berlin, Germany.ORCID 0000-0003-4497-7983
Masuo KondohGraduate School of Pharmaceutical Sciences, Osaka University, Osaka 565-0871, Japan. masuo@phs.osaka-u.ac.jp.
Osaka University of Pharmaceutical Sciences · JPCharité - Universitätsmedizin Berlin · DENational Institute of Biomedical Innovation, Health and Nutrition · JP

Funding

grants from the Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research [BINDS]) of AMED JP19am0101077, JP19am0101084, JP19am0101090Grants-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan 19H04468, 18K19400, 18H03190, 16K13044, and 24390042
6 · The paper itself

Abstract

The tight junction (TJ) is an intercellular sealing component found in epithelial and endothelial tissues that regulates the passage of solutes across the paracellular space. Research examining the biology of TJs has revealed that they are complex biochemical structures constructed from a range of proteins including claudins, occludin, tricellulin, angulins and junctional adhesion molecules. The transient disruption of the barrier function of TJs to open the paracellular space is one means of enhancing mucosal and transdermal drug absorption and to deliver drugs across the blood-brain barrier. However, the disruption of TJs can also open the paracellular space to harmful xenobiotics and pathogens. To address this issue, the strategies targeting TJ proteins have been developed to loosen TJs in a size- or tissue-dependent manner rather than to disrupt them. As several TJ proteins are overexpressed in malignant tumors and in the inflamed intestinal tract, and are present in cells and epithelia conjoined with the mucosa-associated lymphoid immune tissue, these TJ-protein-targeted strategies may also provide platforms for the development of novel therapies and vaccines. Here, this paper reviews two TJ-protein-targeted technologies, claudin binders and an angulin binder, and their applications in drug development.

Indexed as

Drug DevelopmentAnimalsClaudinsHumansProtein BindingTight Junction ProteinsTight JunctionsClaudinsTight Junction Proteinsangubindin-1angulinantibodyclaudinClostridium perfringens enterotoxinClostridium perfringens iota-toxindrug developmenttight junction

Identifiers

PMID31426497
PMCPMC6719960
OpenAlexW2968024589

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.