Evidence map›Paper›PMID 34493804›Full record

ArticleCommunications biology2021

Regulation of cadherin dimerization by chemical fragments as a trigger to inhibit cell adhesion.

Akinobu Senoo, Sho Ito, Satoru Nagatoishi, Yutaro Saito, Go Ueno, Daisuke Kuroda, Kouhei Yoshida, Takumi Tashima, Shota Kudo, Shinsuke Sando and 1 more

Abstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Review
  5. Article
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

11 authors.

Akinobu SenooDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0001-6911-360X
Sho ItoGraduate School of Life Science, University of Hyogo, Kamigori-cho, Ako-gun, Hyogo, Japan.ORCID http://orcid.org/0000-0002-7439-7050
Satoru NagatoishiInstitute of Medical Science, The University of Tokyo, Shirokanedai, Minato-ku, Tokyo, Japan. ngtoishi@ims.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0002-0794-3963
Yutaro SaitoDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0001-7610-121X
Go UenoRIKEN SPring-8 Center, Sayo-cho, Sayo-gun, Hyogo, Japan.ORCID http://orcid.org/0000-0003-0648-3632
Daisuke KurodaDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0003-2390-4785
Kouhei YoshidaDepartment of Bioengineering, Graduate School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0001-8106-9437
Takumi TashimaDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.
Shota KudoDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.
Shinsuke SandoDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0003-0275-7237
Kouhei TsumotoDepartment of Chemistry and Biotechnology, Graduate School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan. tsumoto@bioeng.t.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0001-7643-5164

Funding

Japan Agency for Medical Research and Development (AMED) JP19am0101094MEXT | Japan Society for the Promotion of Science (JSPS) 16H02420MEXT | Japan Society for the Promotion of Science (JSPS) 19H05766
6 · The paper itself

Abstract

Many cadherin family proteins are associated with diseases such as cancer. Since cell adhesion requires homodimerization of cadherin molecules, a small-molecule regulator of dimerization would have therapeutic potential. Herein, we describe identification of a P-cadherin-specific chemical fragment that inhibits P-cadherin-mediated cell adhesion. Although the identified molecule is a fragment compound, it binds to a cavity of P-cadherin that has not previously been targeted, indirectly prevents formation of hydrogen bonds necessary for formation of an intermediate called the X dimer and thus modulates the process of X dimerization. Our findings will impact on a strategy for regulation of protein-protein interactions and stepwise assembly of protein complexes using small molecules.

Indexed as

Cell AdhesionProtein MultimerizationCadherinsHumansProtein BindingCadherins

Identifiers

PMID34493804
PMCPMC8423723

What OpenQuestion holds

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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.